WO2022097675A1 - 分散安定性及び/又は溶解性を高めた加工植物性ミルクの製造方法 - Google Patents
分散安定性及び/又は溶解性を高めた加工植物性ミルクの製造方法 Download PDFInfo
- Publication number
- WO2022097675A1 WO2022097675A1 PCT/JP2021/040557 JP2021040557W WO2022097675A1 WO 2022097675 A1 WO2022097675 A1 WO 2022097675A1 JP 2021040557 W JP2021040557 W JP 2021040557W WO 2022097675 A1 WO2022097675 A1 WO 2022097675A1
- Authority
- WO
- WIPO (PCT)
- Prior art keywords
- milk
- protein
- vegetable
- drink
- less
- Prior art date
Links
- 239000006185 dispersion Substances 0.000 title claims abstract description 99
- 238000004519 manufacturing process Methods 0.000 title claims description 33
- 235000020245 plant milk Nutrition 0.000 title abstract description 5
- 230000001965 increasing effect Effects 0.000 title description 24
- 239000004367 Lipase Substances 0.000 claims abstract description 76
- 102000004882 Lipase Human genes 0.000 claims abstract description 76
- 108090001060 Lipase Proteins 0.000 claims abstract description 76
- 235000019421 lipase Nutrition 0.000 claims abstract description 76
- 235000020197 coconut milk Nutrition 0.000 claims abstract description 60
- 235000020265 peanut milk Nutrition 0.000 claims abstract description 58
- 235000020261 walnut milk Nutrition 0.000 claims abstract description 40
- 235000020262 oat milk Nutrition 0.000 claims abstract description 30
- 108010025880 Cyclomaltodextrin glucanotransferase Proteins 0.000 claims abstract description 27
- 102000004190 Enzymes Human genes 0.000 claims description 168
- 108090000790 Enzymes Proteins 0.000 claims description 165
- 102000004169 proteins and genes Human genes 0.000 claims description 144
- 108090000623 proteins and genes Proteins 0.000 claims description 144
- 108010082495 Dietary Plant Proteins Proteins 0.000 claims description 135
- 235000013305 food Nutrition 0.000 claims description 117
- 235000013336 milk Nutrition 0.000 claims description 101
- 210000004080 milk Anatomy 0.000 claims description 101
- 239000008267 milk Substances 0.000 claims description 97
- 239000000463 material Substances 0.000 claims description 96
- 244000068988 Glycine max Species 0.000 claims description 61
- 235000010469 Glycine max Nutrition 0.000 claims description 61
- 235000013311 vegetables Nutrition 0.000 claims description 50
- 241000235527 Rhizopus Species 0.000 claims description 30
- 244000060011 Cocos nucifera Species 0.000 claims description 23
- 235000013162 Cocos nucifera Nutrition 0.000 claims description 23
- 229920000858 Cyclodextrin Polymers 0.000 claims description 22
- HFHDHCJBZVLPGP-UHFFFAOYSA-N schardinger α-dextrin Chemical compound O1C(C(C2O)O)C(CO)OC2OC(C(C2O)O)C(CO)OC2OC(C(C2O)O)C(CO)OC2OC(C(O)C2O)C(CO)OC2OC(C(C2O)O)C(CO)OC2OC2C(O)C(O)C1OC2CO HFHDHCJBZVLPGP-UHFFFAOYSA-N 0.000 claims description 22
- 239000002994 raw material Substances 0.000 claims description 20
- 241000235395 Mucor Species 0.000 claims description 8
- 239000003795 chemical substances by application Substances 0.000 claims description 6
- 235000013322 soy milk Nutrition 0.000 abstract description 11
- 101001122938 Homo sapiens Lysosomal protective protein Proteins 0.000 abstract description 5
- 102100028524 Lysosomal protective protein Human genes 0.000 abstract description 5
- 238000012545 processing Methods 0.000 abstract description 4
- 238000005516 engineering process Methods 0.000 abstract description 2
- 229940088598 enzyme Drugs 0.000 description 164
- 235000018102 proteins Nutrition 0.000 description 136
- 230000000694 effects Effects 0.000 description 43
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 35
- 230000002708 enhancing effect Effects 0.000 description 33
- 238000011282 treatment Methods 0.000 description 33
- 239000000243 solution Substances 0.000 description 31
- 239000000203 mixture Substances 0.000 description 23
- 239000000047 product Substances 0.000 description 22
- 239000002002 slurry Substances 0.000 description 22
- 244000105624 Arachis hypogaea Species 0.000 description 19
- 238000000034 method Methods 0.000 description 19
- 235000020232 peanut Nutrition 0.000 description 19
- 235000020234 walnut Nutrition 0.000 description 17
- QGZKDVFQNNGYKY-UHFFFAOYSA-N Ammonia Chemical compound N QGZKDVFQNNGYKY-UHFFFAOYSA-N 0.000 description 16
- 102000009127 Glutaminase Human genes 0.000 description 16
- 108010073324 Glutaminase Proteins 0.000 description 16
- 241000758789 Juglans Species 0.000 description 16
- 235000009496 Juglans regia Nutrition 0.000 description 16
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 15
- 238000010521 absorption reaction Methods 0.000 description 14
- 108090000637 alpha-Amylases Proteins 0.000 description 13
- 102000004139 alpha-Amylases Human genes 0.000 description 13
- 230000000052 comparative effect Effects 0.000 description 13
- 238000002360 preparation method Methods 0.000 description 13
- CSCPPACGZOOCGX-UHFFFAOYSA-N Acetone Chemical compound CC(C)=O CSCPPACGZOOCGX-UHFFFAOYSA-N 0.000 description 12
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 12
- 229940024171 alpha-amylase Drugs 0.000 description 12
- 230000001747 exhibiting effect Effects 0.000 description 12
- 238000010438 heat treatment Methods 0.000 description 12
- 239000012085 test solution Substances 0.000 description 12
- 235000017060 Arachis glabrata Nutrition 0.000 description 11
- 235000010777 Arachis hypogaea Nutrition 0.000 description 11
- 235000018262 Arachis monticola Nutrition 0.000 description 11
- 240000005384 Rhizopus oryzae Species 0.000 description 11
- 235000013752 Rhizopus oryzae Nutrition 0.000 description 11
- 239000000758 substrate Substances 0.000 description 10
- 238000012360 testing method Methods 0.000 description 10
- 241000193830 Bacillus <bacterium> Species 0.000 description 9
- KRKNYBCHXYNGOX-UHFFFAOYSA-N citric acid Chemical compound OC(=O)CC(O)(C(O)=O)CC(O)=O KRKNYBCHXYNGOX-UHFFFAOYSA-N 0.000 description 9
- 238000011156 evaluation Methods 0.000 description 9
- 229910021529 ammonia Inorganic materials 0.000 description 8
- 238000006243 chemical reaction Methods 0.000 description 8
- 238000003756 stirring Methods 0.000 description 8
- 230000009849 deactivation Effects 0.000 description 7
- 238000001914 filtration Methods 0.000 description 7
- 108010073771 Soybean Proteins Proteins 0.000 description 6
- 235000014113 dietary fatty acids Nutrition 0.000 description 6
- 238000004090 dissolution Methods 0.000 description 6
- 229930195729 fatty acid Natural products 0.000 description 6
- 239000000194 fatty acid Substances 0.000 description 6
- 210000003491 skin Anatomy 0.000 description 6
- 235000019710 soybean protein Nutrition 0.000 description 6
- 235000007319 Avena orientalis Nutrition 0.000 description 5
- 244000075850 Avena orientalis Species 0.000 description 5
- 241001107116 Castanospermum australe Species 0.000 description 5
- 241000611330 Chryseobacterium Species 0.000 description 5
- 238000002835 absorbance Methods 0.000 description 5
- 235000021279 black bean Nutrition 0.000 description 5
- 238000009835 boiling Methods 0.000 description 5
- 150000004665 fatty acids Chemical class 0.000 description 5
- 244000005700 microbiome Species 0.000 description 5
- 241000196324 Embryophyta Species 0.000 description 4
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 4
- 108010064851 Plant Proteins Proteins 0.000 description 4
- 229920002472 Starch Polymers 0.000 description 4
- 239000011259 mixed solution Substances 0.000 description 4
- 235000021118 plant-derived protein Nutrition 0.000 description 4
- 239000012488 sample solution Substances 0.000 description 4
- 239000008107 starch Substances 0.000 description 4
- 235000019698 starch Nutrition 0.000 description 4
- 239000006228 supernatant Substances 0.000 description 4
- SOUXAAOTONMPRY-UHFFFAOYSA-N 2-[[5-amino-5-oxo-2-(phenylmethoxycarbonylamino)pentanoyl]amino]acetic acid Chemical compound OC(=O)CNC(=O)C(CCC(=O)N)NC(=O)OCC1=CC=CC=C1 SOUXAAOTONMPRY-UHFFFAOYSA-N 0.000 description 3
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 3
- NLXLAEXVIDQMFP-UHFFFAOYSA-N Ammonia chloride Chemical compound [NH4+].[Cl-] NLXLAEXVIDQMFP-UHFFFAOYSA-N 0.000 description 3
- 241000626621 Geobacillus Species 0.000 description 3
- 229920001503 Glucan Polymers 0.000 description 3
- 239000004372 Polyvinyl alcohol Substances 0.000 description 3
- 150000001408 amides Chemical class 0.000 description 3
- 238000001035 drying Methods 0.000 description 3
- 239000003623 enhancer Substances 0.000 description 3
- 239000007788 liquid Substances 0.000 description 3
- 239000008363 phosphate buffer Substances 0.000 description 3
- 229920002451 polyvinyl alcohol Polymers 0.000 description 3
- NWUYHJFMYQTDRP-UHFFFAOYSA-N 1,2-bis(ethenyl)benzene;1-ethenyl-2-ethylbenzene;styrene Chemical compound C=CC1=CC=CC=C1.CCC1=CC=CC=C1C=C.C=CC1=CC=CC=C1C=C NWUYHJFMYQTDRP-UHFFFAOYSA-N 0.000 description 2
- ZCYVEMRRCGMTRW-UHFFFAOYSA-N 7553-56-2 Chemical compound [I] ZCYVEMRRCGMTRW-UHFFFAOYSA-N 0.000 description 2
- 241000228212 Aspergillus Species 0.000 description 2
- 241000228245 Aspergillus niger Species 0.000 description 2
- 241000193744 Bacillus amyloliquefaciens Species 0.000 description 2
- 229920002498 Beta-glucan Polymers 0.000 description 2
- 241000588747 Klebsiella pneumoniae Species 0.000 description 2
- 230000009471 action Effects 0.000 description 2
- 239000007864 aqueous solution Substances 0.000 description 2
- 108010019077 beta-Amylase Proteins 0.000 description 2
- 235000013361 beverage Nutrition 0.000 description 2
- 238000005119 centrifugation Methods 0.000 description 2
- 238000001816 cooling Methods 0.000 description 2
- 239000006071 cream Substances 0.000 description 2
- 229940079919 digestives enzyme preparation Drugs 0.000 description 2
- 238000010790 dilution Methods 0.000 description 2
- 239000012895 dilution Substances 0.000 description 2
- 230000035622 drinking Effects 0.000 description 2
- 235000013399 edible fruits Nutrition 0.000 description 2
- 239000003925 fat Substances 0.000 description 2
- -1 fatty acid ester Chemical class 0.000 description 2
- 239000000796 flavoring agent Substances 0.000 description 2
- 235000019634 flavors Nutrition 0.000 description 2
- 235000013312 flour Nutrition 0.000 description 2
- 235000020268 grain milk Nutrition 0.000 description 2
- 239000011630 iodine Substances 0.000 description 2
- 229910052740 iodine Inorganic materials 0.000 description 2
- 150000002632 lipids Chemical class 0.000 description 2
- 235000013372 meat Nutrition 0.000 description 2
- 235000015097 nutrients Nutrition 0.000 description 2
- 235000016709 nutrition Nutrition 0.000 description 2
- 239000003921 oil Substances 0.000 description 2
- 235000019198 oils Nutrition 0.000 description 2
- 235000008390 olive oil Nutrition 0.000 description 2
- 239000004006 olive oil Substances 0.000 description 2
- KJFMBFZCATUALV-UHFFFAOYSA-N phenolphthalein Chemical compound C1=CC(O)=CC=C1C1(C=2C=CC(O)=CC=2)C2=CC=CC=C2C(=O)O1 KJFMBFZCATUALV-UHFFFAOYSA-N 0.000 description 2
- 235000021395 porridge Nutrition 0.000 description 2
- 229920001592 potato starch Polymers 0.000 description 2
- 238000001799 protein solubilization Methods 0.000 description 2
- 230000007925 protein solubilization Effects 0.000 description 2
- 239000012460 protein solution Substances 0.000 description 2
- 238000000746 purification Methods 0.000 description 2
- 230000035484 reaction time Effects 0.000 description 2
- 238000000926 separation method Methods 0.000 description 2
- 239000007787 solid Substances 0.000 description 2
- 235000019640 taste Nutrition 0.000 description 2
- 125000000430 tryptophan group Chemical group [H]N([H])C(C(=O)O*)C([H])([H])C1=C([H])N([H])C2=C([H])C([H])=C([H])C([H])=C12 0.000 description 2
- FYGDTMLNYKFZSV-URKRLVJHSA-N (2s,3r,4s,5s,6r)-2-[(2r,4r,5r,6s)-4,5-dihydroxy-2-(hydroxymethyl)-6-[(2r,4r,5r,6s)-4,5,6-trihydroxy-2-(hydroxymethyl)oxan-3-yl]oxyoxan-3-yl]oxy-6-(hydroxymethyl)oxane-3,4,5-triol Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@H]1OC1[C@@H](CO)O[C@@H](OC2[C@H](O[C@H](O)[C@H](O)[C@H]2O)CO)[C@H](O)[C@H]1O FYGDTMLNYKFZSV-URKRLVJHSA-N 0.000 description 1
- OHVLMTFVQDZYHP-UHFFFAOYSA-N 1-(2,4,6,7-tetrahydrotriazolo[4,5-c]pyridin-5-yl)-2-[4-[2-[[3-(trifluoromethoxy)phenyl]methylamino]pyrimidin-5-yl]piperazin-1-yl]ethanone Chemical compound N1N=NC=2CN(CCC=21)C(CN1CCN(CC1)C=1C=NC(=NC=1)NCC1=CC(=CC=C1)OC(F)(F)F)=O OHVLMTFVQDZYHP-UHFFFAOYSA-N 0.000 description 1
- HMUNWXXNJPVALC-UHFFFAOYSA-N 1-[4-[2-(2,3-dihydro-1H-inden-2-ylamino)pyrimidin-5-yl]piperazin-1-yl]-2-(2,4,6,7-tetrahydrotriazolo[4,5-c]pyridin-5-yl)ethanone Chemical compound C1C(CC2=CC=CC=C12)NC1=NC=C(C=N1)N1CCN(CC1)C(CN1CC2=C(CC1)NN=N2)=O HMUNWXXNJPVALC-UHFFFAOYSA-N 0.000 description 1
- VZSRBBMJRBPUNF-UHFFFAOYSA-N 2-(2,3-dihydro-1H-inden-2-ylamino)-N-[3-oxo-3-(2,4,6,7-tetrahydrotriazolo[4,5-c]pyridin-5-yl)propyl]pyrimidine-5-carboxamide Chemical compound C1C(CC2=CC=CC=C12)NC1=NC=C(C=N1)C(=O)NCCC(N1CC2=C(CC1)NN=N2)=O VZSRBBMJRBPUNF-UHFFFAOYSA-N 0.000 description 1
- LDXJRKWFNNFDSA-UHFFFAOYSA-N 2-(2,4,6,7-tetrahydrotriazolo[4,5-c]pyridin-5-yl)-1-[4-[2-[[3-(trifluoromethoxy)phenyl]methylamino]pyrimidin-5-yl]piperazin-1-yl]ethanone Chemical compound C1CN(CC2=NNN=C21)CC(=O)N3CCN(CC3)C4=CN=C(N=C4)NCC5=CC(=CC=C5)OC(F)(F)F LDXJRKWFNNFDSA-UHFFFAOYSA-N 0.000 description 1
- WZFUQSJFWNHZHM-UHFFFAOYSA-N 2-[4-[2-(2,3-dihydro-1H-inden-2-ylamino)pyrimidin-5-yl]piperazin-1-yl]-1-(2,4,6,7-tetrahydrotriazolo[4,5-c]pyridin-5-yl)ethanone Chemical compound C1C(CC2=CC=CC=C12)NC1=NC=C(C=N1)N1CCN(CC1)CC(=O)N1CC2=C(CC1)NN=N2 WZFUQSJFWNHZHM-UHFFFAOYSA-N 0.000 description 1
- SOUXAAOTONMPRY-NSHDSACASA-N 2-[[(2s)-5-amino-5-oxo-2-(phenylmethoxycarbonylamino)pentanoyl]amino]acetic acid Chemical compound OC(=O)CNC(=O)[C@H](CCC(=O)N)NC(=O)OCC1=CC=CC=C1 SOUXAAOTONMPRY-NSHDSACASA-N 0.000 description 1
- YLZOPXRUQYQQID-UHFFFAOYSA-N 3-(2,4,6,7-tetrahydrotriazolo[4,5-c]pyridin-5-yl)-1-[4-[2-[[3-(trifluoromethoxy)phenyl]methylamino]pyrimidin-5-yl]piperazin-1-yl]propan-1-one Chemical compound N1N=NC=2CN(CCC=21)CCC(=O)N1CCN(CC1)C=1C=NC(=NC=1)NCC1=CC(=CC=C1)OC(F)(F)F YLZOPXRUQYQQID-UHFFFAOYSA-N 0.000 description 1
- 240000006439 Aspergillus oryzae Species 0.000 description 1
- 235000002247 Aspergillus oryzae Nutrition 0.000 description 1
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 1
- 235000007558 Avena sp Nutrition 0.000 description 1
- 241000194108 Bacillus licheniformis Species 0.000 description 1
- 241000194107 Bacillus megaterium Species 0.000 description 1
- 241000193407 Bacillus ohbensis Species 0.000 description 1
- 244000063299 Bacillus subtilis Species 0.000 description 1
- 235000014469 Bacillus subtilis Nutrition 0.000 description 1
- 239000004129 EU approved improving agent Substances 0.000 description 1
- 241000611354 Empedobacter Species 0.000 description 1
- 241000589565 Flavobacterium Species 0.000 description 1
- 241000193385 Geobacillus stearothermophilus Species 0.000 description 1
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 1
- IMQLKJBTEOYOSI-GPIVLXJGSA-N Inositol-hexakisphosphate Chemical compound OP(O)(=O)O[C@H]1[C@H](OP(O)(O)=O)[C@@H](OP(O)(O)=O)[C@H](OP(O)(O)=O)[C@H](OP(O)(O)=O)[C@@H]1OP(O)(O)=O IMQLKJBTEOYOSI-GPIVLXJGSA-N 0.000 description 1
- 241000758791 Juglandaceae Species 0.000 description 1
- 241000588748 Klebsiella Species 0.000 description 1
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 1
- 241001467578 Microbacterium Species 0.000 description 1
- 241000498617 Mucor javanicus Species 0.000 description 1
- 241001291960 Myroides Species 0.000 description 1
- AFCARXCZXQIEQB-UHFFFAOYSA-N N-[3-oxo-3-(2,4,6,7-tetrahydrotriazolo[4,5-c]pyridin-5-yl)propyl]-2-[[3-(trifluoromethoxy)phenyl]methylamino]pyrimidine-5-carboxamide Chemical compound O=C(CCNC(=O)C=1C=NC(=NC=1)NCC1=CC(=CC=C1)OC(F)(F)F)N1CC2=C(CC1)NN=N2 AFCARXCZXQIEQB-UHFFFAOYSA-N 0.000 description 1
- 240000007594 Oryza sativa Species 0.000 description 1
- 235000007164 Oryza sativa Nutrition 0.000 description 1
- 235000010627 Phaseolus vulgaris Nutrition 0.000 description 1
- 244000046052 Phaseolus vulgaris Species 0.000 description 1
- IMQLKJBTEOYOSI-UHFFFAOYSA-N Phytic acid Natural products OP(O)(=O)OC1C(OP(O)(O)=O)C(OP(O)(O)=O)C(OP(O)(O)=O)C(OP(O)(O)=O)C1OP(O)(O)=O IMQLKJBTEOYOSI-UHFFFAOYSA-N 0.000 description 1
- 241000589516 Pseudomonas Species 0.000 description 1
- 241000235402 Rhizomucor Species 0.000 description 1
- 241000235403 Rhizomucor miehei Species 0.000 description 1
- 241000303962 Rhizopus delemar Species 0.000 description 1
- 241001136275 Sphingobacterium Species 0.000 description 1
- 239000004376 Sucralose Substances 0.000 description 1
- 241000223257 Thermomyces Species 0.000 description 1
- 241000223258 Thermomyces lanuginosus Species 0.000 description 1
- 235000021307 Triticum Nutrition 0.000 description 1
- 244000098338 Triticum aestivum Species 0.000 description 1
- 241001327213 [Bacillus] clarkii Species 0.000 description 1
- 230000000172 allergic effect Effects 0.000 description 1
- FYGDTMLNYKFZSV-DZOUCCHMSA-N alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->4)-D-Glcp Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@@H](CO)O[C@H](O[C@@H]2[C@H](OC(O)[C@H](O)[C@H]2O)CO)[C@H](O)[C@H]1O FYGDTMLNYKFZSV-DZOUCCHMSA-N 0.000 description 1
- 125000003368 amide group Chemical group 0.000 description 1
- 235000001014 amino acid Nutrition 0.000 description 1
- 235000019270 ammonium chloride Nutrition 0.000 description 1
- 235000020244 animal milk Nutrition 0.000 description 1
- 239000003957 anion exchange resin Substances 0.000 description 1
- 229930002877 anthocyanin Natural products 0.000 description 1
- 235000010208 anthocyanin Nutrition 0.000 description 1
- 239000004410 anthocyanin Substances 0.000 description 1
- 150000004636 anthocyanins Chemical class 0.000 description 1
- 235000019606 astringent taste Nutrition 0.000 description 1
- 208000010668 atopic eczema Diseases 0.000 description 1
- 235000019658 bitter taste Nutrition 0.000 description 1
- 238000007664 blowing Methods 0.000 description 1
- 239000000872 buffer Substances 0.000 description 1
- 239000007853 buffer solution Substances 0.000 description 1
- 238000011088 calibration curve Methods 0.000 description 1
- 125000004432 carbon atom Chemical group C* 0.000 description 1
- 239000003729 cation exchange resin Substances 0.000 description 1
- 235000013339 cereals Nutrition 0.000 description 1
- 235000013351 cheese Nutrition 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 238000003776 cleavage reaction Methods 0.000 description 1
- 239000000701 coagulant Substances 0.000 description 1
- 239000000084 colloidal system Substances 0.000 description 1
- 239000000470 constituent Substances 0.000 description 1
- 238000010411 cooking Methods 0.000 description 1
- 238000004132 cross linking Methods 0.000 description 1
- 125000004122 cyclic group Chemical group 0.000 description 1
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 1
- 230000006240 deamidation Effects 0.000 description 1
- 230000003247 decreasing effect Effects 0.000 description 1
- 229910001873 dinitrogen Inorganic materials 0.000 description 1
- 239000003995 emulsifying agent Substances 0.000 description 1
- 230000001804 emulsifying effect Effects 0.000 description 1
- 239000000839 emulsion Substances 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 210000002615 epidermis Anatomy 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- 239000000835 fiber Substances 0.000 description 1
- 239000000706 filtrate Substances 0.000 description 1
- 238000004108 freeze drying Methods 0.000 description 1
- 239000008103 glucose Substances 0.000 description 1
- 238000000227 grinding Methods 0.000 description 1
- 239000001963 growth medium Substances 0.000 description 1
- 235000013402 health food Nutrition 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
- 230000002779 inactivation Effects 0.000 description 1
- 229910052500 inorganic mineral Inorganic materials 0.000 description 1
- 229940077844 iodine / potassium iodide Drugs 0.000 description 1
- 239000003456 ion exchange resin Substances 0.000 description 1
- 229920003303 ion-exchange polymer Polymers 0.000 description 1
- 235000004213 low-fat Nutrition 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 239000002609 medium Substances 0.000 description 1
- 239000012528 membrane Substances 0.000 description 1
- 238000009629 microbiological culture Methods 0.000 description 1
- 235000020124 milk-based beverage Nutrition 0.000 description 1
- 239000011707 mineral Substances 0.000 description 1
- 238000002156 mixing Methods 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 230000001254 nonsecretory effect Effects 0.000 description 1
- 235000020257 nut milk Nutrition 0.000 description 1
- 235000014571 nuts Nutrition 0.000 description 1
- 235000019629 palatability Nutrition 0.000 description 1
- 239000002245 particle Substances 0.000 description 1
- 239000000546 pharmaceutical excipient Substances 0.000 description 1
- 230000001766 physiological effect Effects 0.000 description 1
- 235000002949 phytic acid Nutrition 0.000 description 1
- 239000000467 phytic acid Substances 0.000 description 1
- 229940068041 phytic acid Drugs 0.000 description 1
- 239000000843 powder Substances 0.000 description 1
- 235000013406 prebiotics Nutrition 0.000 description 1
- 239000002244 precipitate Substances 0.000 description 1
- 230000008569 process Effects 0.000 description 1
- 238000003672 processing method Methods 0.000 description 1
- 235000009566 rice Nutrition 0.000 description 1
- 238000005185 salting out Methods 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 230000007017 scission Effects 0.000 description 1
- 230000003248 secreting effect Effects 0.000 description 1
- 241000894007 species Species 0.000 description 1
- 239000003381 stabilizer Substances 0.000 description 1
- 239000012086 standard solution Substances 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- BAQAVOSOZGMPRM-QBMZZYIRSA-N sucralose Chemical compound O[C@@H]1[C@@H](O)[C@@H](Cl)[C@@H](CO)O[C@@H]1O[C@@]1(CCl)[C@@H](O)[C@H](O)[C@@H](CCl)O1 BAQAVOSOZGMPRM-QBMZZYIRSA-N 0.000 description 1
- 235000019408 sucralose Nutrition 0.000 description 1
- 238000009210 therapy by ultrasound Methods 0.000 description 1
- 238000012546 transfer Methods 0.000 description 1
- 150000003626 triacylglycerols Chemical class 0.000 description 1
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 1
- 125000001493 tyrosinyl group Chemical group [H]OC1=C([H])C([H])=C(C([H])=C1[H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 description 1
- 238000001291 vacuum drying Methods 0.000 description 1
Classifications
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
- A23L2/00—Non-alcoholic beverages; Dry compositions or concentrates therefor; Their preparation
- A23L2/38—Other non-alcoholic beverages
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23C—DAIRY PRODUCTS, e.g. MILK, BUTTER OR CHEESE; MILK OR CHEESE SUBSTITUTES; MAKING THEREOF
- A23C11/00—Milk substitutes, e.g. coffee whitener compositions
- A23C11/02—Milk substitutes, e.g. coffee whitener compositions containing at least one non-milk component as source of fats or proteins
- A23C11/10—Milk substitutes, e.g. coffee whitener compositions containing at least one non-milk component as source of fats or proteins containing or not lactose but no other milk components as source of fats, carbohydrates or proteins
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23C—DAIRY PRODUCTS, e.g. MILK, BUTTER OR CHEESE; MILK OR CHEESE SUBSTITUTES; MAKING THEREOF
- A23C11/00—Milk substitutes, e.g. coffee whitener compositions
- A23C11/02—Milk substitutes, e.g. coffee whitener compositions containing at least one non-milk component as source of fats or proteins
- A23C11/10—Milk substitutes, e.g. coffee whitener compositions containing at least one non-milk component as source of fats or proteins containing or not lactose but no other milk components as source of fats, carbohydrates or proteins
- A23C11/103—Milk substitutes, e.g. coffee whitener compositions containing at least one non-milk component as source of fats or proteins containing or not lactose but no other milk components as source of fats, carbohydrates or proteins containing only proteins from pulses, oilseeds or nuts, e.g. nut milk
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
- A23J3/00—Working-up of proteins for foodstuffs
- A23J3/14—Vegetable proteins
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
- A23J3/00—Working-up of proteins for foodstuffs
- A23J3/14—Vegetable proteins
- A23J3/16—Vegetable proteins from soybean
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
- A23J3/00—Working-up of proteins for foodstuffs
- A23J3/30—Working-up of proteins for foodstuffs by hydrolysis
- A23J3/32—Working-up of proteins for foodstuffs by hydrolysis using chemical agents
- A23J3/34—Working-up of proteins for foodstuffs by hydrolysis using chemical agents using enzymes
- A23J3/346—Working-up of proteins for foodstuffs by hydrolysis using chemical agents using enzymes of vegetable proteins
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
- A23L2/00—Non-alcoholic beverages; Dry compositions or concentrates therefor; Their preparation
- A23L2/52—Adding ingredients
- A23L2/66—Proteins
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/195—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/37—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from fungi
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23C—DAIRY PRODUCTS, e.g. MILK, BUTTER OR CHEESE; MILK OR CHEESE SUBSTITUTES; MAKING THEREOF
- A23C2220/00—Biochemical treatment
- A23C2220/10—Enzymatic treatment
Definitions
- the present invention relates to a material for vegetable protein food and drink and / or a processed product of vegetable protein food and drink, specifically, a method for producing processed vegetable milk. More specifically, the present invention relates to a processing technique for enhancing the dispersion stability and / or solubility of vegetable milks such as oat milk, black soybean milk, walnut milk, peanut milk, and coconut milk.
- soybean protein various modification treatments have been studied for the purpose of improving its existing characteristics and for providing foods having new taste characteristics.
- Patent Document 1 JP2000-50887A
- Patent Document 2 JP2008-283900A
- Patent Document 3 JP2015-159765A
- the soymilk is subjected to a deamidation treatment with a cation exchange resin and / or a phytic acid removal treatment with an anion exchange resin, so that a precipitate is formed on the coagulant. It is stated that it is less likely to occur.
- grain milk such as oat and black beans
- nut milk such as coconut, peanut, and walnut are being developed.
- oat milk has characteristics different from other grain milks in that it is rich in lipids, ⁇ -glucans, and minerals in addition to protein, and its high nutritional value is attracting attention.
- Patent Document 4 US6,451,361B1
- an auto-dispersion solution that solves the problem of high viscosity by treating an autosuspension with ⁇ -amylase and ⁇ -amylase and maintains a protein and ⁇ -glucan is provided. It is stated that it was obtained.
- Patent Document 5 (CN101991163A) describes that the prebiotic action of an auto-beverage is improved by producing maltooligosaccharide by treatment with ⁇ -amylase, ⁇ -amylase and transglucosidase.
- Black soybean milk is attracting attention because it contains black soybean epidermis components that are rich in components with various physiological effects such as anthocyanins.
- Patent Document 6 JP2006-230297A
- yellow soybean milk is added to black soymilk, and black soymilk solid content A and yellow soymilk solid content B are used for the purpose of suppressing astringency or bitterness derived from the skin portion of black soybean. It is described that a black soybean milk beverage having excellent palatability can be obtained by blending so that the content mass ratio (A: B) is 4: 6 to 6: 4.
- Walnut milk contains much more fat than protein.
- Patent Document 7 WO2019 / 104971A1
- walnut milk having a good texture and stability with low fat and high protein was obtained by separating and removing a part of fats and oils during the manufacturing process. Have been described.
- coconut milk is characterized by its unique aroma, so it may be treated for the purpose of improving the flavor.
- Patent Document 8 JP2008-09966A describes that a flavor improving effect can be obtained by containing sucralose in coconut milk.
- Vegetable milk has high nutritional value and high value as a health food, and processing methods are being studied from various viewpoints.
- the control of its dispersion stability and / or its solubility has been sufficiently studied.
- vegetable milk not only vegetable milk but also various vegetable protein foods and drinks and their materials, techniques for improving the dispersion stability and / or solubility thereof have not been sufficiently studied.
- the dispersion stability and / or solubility of vegetable protein foods and drinks and their materials will be improved in order to respond to the diversification of their uses. A technology that can be used is desired.
- An object of the present invention is to provide a processing technique for improving the dispersion stability and / or solubility of vegetable protein foods and drinks and their materials.
- the present inventor has found that treatment of a vegetable protein food or drink and its material with a protein deamidating enzyme can enhance the dispersion stability and / or solubility of the vegetable protein food or drink and its material. There is still room for improvement in the effect, and it is necessary to develop the effect even more efficiently. Therefore, as a result of further diligent studies by the present inventor, by treating the vegetable protein food and drink and its material with a combination of a protein deamidating enzyme and lipase and / or cyclodextrin glucanotransferase, the vegetable protein food and drink and its material are treated. It has been found that the dispersion stability and / or solubility of the material can be further enhanced. That is, the present invention provides the inventions of the following aspects.
- Item 1 Vegetable protein food and drink material and / or vegetable protein food and drink material and / or vegetable protein food and drink comprising the step of treating the vegetable protein food and drink material and / or the vegetable protein food and drink with a protein deamidating enzyme and lipase and / or cyclodextone lucanotransferase. Manufacturing method of processed products.
- Item 2. Item 2. The method for producing processed vegetable milk according to Item 1, wherein the vegetable protein food or drink material and / or the vegetable protein food or drink is vegetable milk.
- the processed vegetable product according to Item 1 or 2 wherein the vegetable protein food or drink material and / or the vegetable protein food or drink is selected from the group consisting of oat milk, black soybean milk, walnut milk, peanut milk, and coconut milk. How to make milk.
- Item 4. Item 2. The method for producing processed vegetable milk according to any one of Items 1 to 3, wherein the vegetable protein food / drink material and / or the vegetable protein food / drink is walnut milk and / or peanut milk, and lipase is used in the step. .. Item 5.
- the vegetable protein food and drink material and / or the vegetable protein food and drink is selected from the group consisting of oat milk, black soybean milk, peanut milk, and coconut milk, and cyclodexing glucanotransferase is used in the step. 3.
- the method for producing processed vegetable milk according to any one of 3. Item 7.
- Item 3. The method for producing processed vegetable milk according to Item 3 or 6, wherein the content of the coconut-derived component in the coconut milk is 10 to 70 w / v%.
- Item 6. The method for producing processed vegetable milk according to any one of Items 1 to 9, wherein the cyclodextrin glucanotransferase is used in an amount of 0.01 U or more per 1 g of the vegetable protein raw material.
- Item 11 A dispersion stability improver for walnut milk and / or peanut milk, which comprises a protein deamidating enzyme and lipase.
- a dispersion stability improver for oat milk which comprises a protein deamidating enzyme and cyclodextrin glucanotransferase.
- An agent for improving the solubility of vegetable milk selected from the group consisting of black soybean milk, peanut milk, and coconut milk, which comprises a protein deamidating enzyme and a cyclodextrin lucanotransferase.
- Item 14 A yield improver for coconut milk, which comprises a protein deamidating enzyme and cyclodextrin glucanotransferase.
- the method for producing vegetable protein food and drink material and / or vegetable protein food and drink processed product of the present invention is vegetable protein food and drink. It comprises treating the material and / or the vegetable protein food and drink with a protein deamidating enzyme and lipase and / or cyclodextone lucanotransferase.
- a protein deamidating enzyme and lipase and / or cyclodextone lucanotransferase the method for producing the vegetable protein food and drink material and / or the processed product of the vegetable protein food and drink of the present invention will be described in detail.
- Vegetable protein food and drink material and / or vegetable protein food and drink The vegetable protein food and drink material and / or vegetable protein food and drink used in the present invention is not particularly limited. Vegetable protein The food and drink material contains vegetable protein and is not intended to be eaten and / or eaten as it is, but is premised on cooking and is used as a material for food and drink. In addition, vegetable protein foods and drinks are those that are served as they are for eating and / or drinking. Specific examples of vegetable protein food and drink materials and / or vegetable protein food and drink (hereinafter collectively referred to as "vegetable protein food and drink material, etc.") include vegetable milk, vegetable cream, and the like. Examples thereof include vegetable substitute meat, vegetable substitute cheese, and vegetable protein solution. Among these vegetable protein food and drink materials, those having fluidity such as vegetable milk, vegetable cream, vegetable protein solution, etc. are preferably mentioned from the viewpoint of further improving the effect of the present invention. Vegetable milk is preferable.
- the vegetable edible portion which is a raw material of vegetable protein contained in vegetable protein food and drink materials is not particularly limited, and for example, wheat and rice.
- kinds, grains such as beans, and nuts and the like can be mentioned.
- oats, black beans, walnuts, peanuts, and coconuts are preferable from the viewpoint of further improving the effect of the present invention.
- the amount of water per 1 part by weight of vegetable protein raw material used for preparing vegetable protein food and drink materials is, for example, 0.5 to 40 parts by weight, 1 to 30 parts by weight, or 1.5 to 20 parts by weight. The weight part is mentioned.
- the method for producing processed vegetable milk of the present invention is characterized by comprising a step of treating vegetable milk with a protein deamidating enzyme and lipase and / or cyclodextrin glucanotransferase.
- a protein deamidating enzyme and lipase and / or cyclodextrin glucanotransferase are described in detail.
- the vegetable milk used in the present invention refers to a liquid in which crushed products of the edible part of a plant are dispersed in water.
- the edible portion of the plant can be crushed by any method such as squeezing and / or grinding, and these crushing methods can be preferably performed in water.
- the crushed material of the edible portion is dispersed, and the components derived from the edible portion exposed in water by extraction or the like are partially or completely dissolved, dispersed, and / or emulsified. good.
- the vegetable milk may be one in which the insoluble matter derived from the skin of the edible portion or the like is appropriately removed by any means such as centrifugal filtration, filtration, straining bag, sieve, etc., or the insoluble matter. May be contained in a dispersed state without being removed.
- the edible part of the plant used as the raw material of the vegetable milk used in the present invention is not particularly limited.
- the vegetable milk is preferably selected from the group consisting of oat milk, black soybean milk, walnut milk, peanut milk, and coconut milk.
- the auto milk used in the present invention is not particularly limited, and general auto milk can be used.
- oat milk include liquids obtained by filtering heat-treated oat slurry (for example, oat powder porridge, crushed oatmeal porridge, etc.).
- the amount of water with respect to 1 part by weight of the auto is, for example, 0.5 to 20 parts by weight, 1 to 15 parts by weight, or 2 to 10 parts by weight, preferably 3 to 8 parts by weight. It is preferably 4 to 6 parts by weight, more preferably 4.5 to 5.5 parts by weight.
- the temperature of the heat treatment include 83 to 100 ° C, preferably 85 to 96 ° C, and more preferably 88 to 93 ° C.
- the number of meshes of the sieve used for filtering the heat-treated autoslurry may be such that the coarse insoluble fibers of the auto can be removed, and examples thereof include 50 to 70 meshes, preferably 55 to 65 meshes.
- the black soymilk used in the present invention is not particularly limited, and general black soymilk (black soymilk) can be used.
- black soybean milk include a slurry of heated black soybeans (for example, a slurry obtained by crushing heat-treated black soybeans with skin in water (preferably hot water)) and a heat-treated product of black soybean slurry (for example, unheated). Heat-treated products of slurry products obtained by crushing black beans with skin in water), diluted products thereof, pH-adjusted products thereof and the like can be mentioned.
- the heat treatment temperature for black beans or slurry is not particularly limited, and examples thereof include 48 ° C. and boiling temperature ° C.. Examples of the temperature of the hot water include 80 to 95 ° C.
- the content of the black soybean-derived component in the black soybean milk is, for example, 0.5 to 25 w / v%, 1 to 20 w / v%, 2 to 15 w / v%, preferably 3 to 10 w / v%, and more preferably 4. -8w / v%, more preferably 5-7w / v%.
- the content of black soybean protein in black soybean milk is, for example, 0.1 to 10 w / v%, 0.2 to 8 w / v%, 0.4 to 6 w / v%, 0.8 to 4 w / v%, preferably 0.8 to 4 w / v%.
- the pH (25 ° C.) of the black soybean milk is, for example, 5.5 to 6.5, preferably 5.8 to 6.2.
- the walnut milk used in the present invention is not particularly limited, and general walnut milk can be used.
- walnut milk include heat-treated walnut slurry (for example, a heat-treated product of peeled walnut slurry or a water-diluted product thereof).
- the temperature of the heat treatment include 83 to 100 ° C, preferably 85 to 96 ° C, and more preferably 88 to 93 ° C.
- the amount of water per 1 part by weight of walnut in walnut milk is, for example, 0.5 to 20 parts by weight, 1 to 15 parts by weight, 1.5 to 10 parts by weight, preferably 2 to 8 parts by weight, and more preferably 3. 5 parts by weight, more preferably 3.5 to 4.5 parts by weight.
- the peanut milk used in the present invention is not particularly limited, and general peanut milk can be used.
- peanut milk include heat-treated peanut slurries (eg, boiled products of peeled roasted peanut slurries or water dilutions thereof).
- the temperature of the heat treatment include 90 ° C. to boiling temperature, preferably 95 ° C. to boiling temperature, and more preferably boiling temperature.
- the content of the peanut-derived component in the peanut milk is, for example, 0.5 to 25 w / v%, 1 to 20 w / v%, 2 to 15 w / v%, preferably 4 to 12 w / v%, and more preferably 6 to.
- the content of peanut protein in peanut milk is, for example, 0.1 to 10 w / v%, 0.2 to 8 w / v%, 0.4 to 6 w / v%, 0.8 to 4 w / v%, preferably 0.8 to 4 w / v%. Is 1.2 to 3 w / v%, more preferably 1.5 to 2.5 w / v%, still more preferably 1.8 to 2.2 w / v%.
- the pH (25 ° C.) of the peanut milk is, for example, 5.5 to 6.5, preferably 5.8 to 6.2.
- the coconut milk used in the present invention is not particularly limited, and general coconut milk can be used.
- Examples of coconut milk are crushed and / or shredded coconut slurries (eg, raw coconut endosperm or copra (dried mature fruit endosperm)) ground in water (preferably warm water).
- the slurry obtained in the above process or a water-diluted product thereof) can be mentioned.
- Examples of the temperature of the hot water include 40 to 60 ° C.
- Examples of the content of coconut-derived components in coconut milk include 10 to 70 w / v%, 20 to 60 w / v%, preferably 30 to 50 w / v%, and more preferably 35 to 45 w / v%, and coconut.
- the protein content in milk is, for example, 0.1 to 10 w / v%, 0.2 to 5 w / v%, 0.3 to 3 w / v%, preferably 0.5 to 2 w / v%, and more preferably 0.5 to 2 w / v%. 1 to 1.5 w / v% can be mentioned.
- the pH (25 ° C.) of the coconut milk is, for example, 5.5 to 6.5, preferably 5.8 to 6.2.
- These vegetable milks may be used alone or in combination of two or more.
- Protein deamidating enzyme used in the present invention is an enzyme having an action of decomposing an amide group-containing side chain of a protein without cleavage of a peptide bond and cross-linking of the protein, and the type and origin thereof. Is not particularly limited.
- Examples of protein deamidating enzymes are Chryseobacterium, Flavobacterium, Empedobacter, disclosed in JP2000-50887A, JP2001-218590A, WO2006 / 075772A1.
- protein deamidating enzymes derived from the genus Sphingobacterium, Aureobacterium or Myroides, and protein glutaminase derived from the genus Chryseobacterium.
- protein deamidating enzymes one type may be used alone, or a plurality of types may be used in combination.
- protein deamidating enzymes from the viewpoint of further improving the dispersion stability and / or solubility of the above-mentioned vegetable protein food and drink materials, or from the viewpoint of further improving the yield of coconut milk.
- protein deamidating enzymes derived from the genus Chryseobacterium more preferably protein glutaminase derived from the genus Chryseobacterium, and even more preferably protein glutaminase derived from the Chryseobacterium proteinicum species. ..
- the protein deamidating enzyme can be prepared from the culture solution of the microorganism from which the above protein deamidating enzyme is derived.
- Specific preparation methods include a method of recovering protein deamidating enzyme from the above-mentioned microbial culture solution or cells.
- the enzyme can be separated and / or purified after collecting the cells from the culture solution by filtration, centrifugation or the like in advance, if necessary.
- the cells were recovered from the culture solution in advance as needed, and then the cells were crushed by pressure treatment, ultrasonic treatment, etc. to expose the enzyme.
- the enzyme can be separated and / or purified.
- a known protein separation and / or purification method can be used without particular limitation, and for example, a centrifugation method, a UF concentration method, a salting out method, an ion exchange resin, or the like can be used.
- Various chromatographic methods using the above can be mentioned.
- the separated and / or purified enzyme can be pulverized by a drying method such as freeze-drying or vacuum drying to prepare an enzyme preparation, and an excipient and / or a drying aid suitable for the drying method can be used. It can also be powdered using.
- a commercially available enzyme preparation can be used for the protein deamidating enzyme, and an example of a preferable commercially available product is the protein glutaminase "Amano" 500 manufactured by Amano Enzyme Co., Ltd.
- the titer of the enzyme preparation containing the protein deamidating enzyme used in the present invention is not particularly limited, but is, for example, 10 to 50,000 U, preferably 100 to 10000 U, more preferably 200 to 800 U / g, still more preferably 300 to 700 U / g. g, more preferably 400 to 600 U / g, still more preferably 450 to 550 U / g.
- the amount of the protein deamidating enzyme used is not particularly limited, but the amount used per 1 g of vegetable protein in vegetable protein food and drink materials is, for example, 0.01 U or more, preferably 0.1 U or more, more preferably 0. .5 U or more, more preferably 0.8 U or more, and 25 U or less.
- the amount of the protein amide enzyme used per 1 g of the vegetable protein raw material used for the vegetable protein food and drink material is, for example, 0.006 U or more, preferably 0.012 U or more, more preferably 0.024 U or more, still more preferable. Is 0.036U or more, more preferably 0.06U or more, and 10U or less.
- the autoprotein of the protein deamidating enzyme is used from the viewpoint of further enhancing the dispersion stability and / or solubility of the automilk, preferably from the viewpoint of further enhancing the dispersion stability.
- the amount used per 1 g is 0.1 U or more, 0.5 U or more, 1 U or more, preferably 1.5 U or more, more preferably 2 U or more, still more preferably 2.5 U or more, still more preferably 3 U or more, still more. It is preferably 4U or more, and particularly preferably 4.5U or more.
- the upper limit of the range of the amount of the protein deamidating enzyme used per 1 g of autoprotein is not particularly limited, and examples thereof include 25 U or less.
- suitable examples of the upper limit of the range of use of the protein deamidating enzyme per 1 g of autoprotein include, for example, 22 U or less, preferably 17 U or less, more preferably 14 U or less, still more preferably 10 U or less, and one layer. It is preferably 8U or less, and even more preferably 6U or less.
- the amount of protein deamidating enzyme used per 1 g of oat milk used for oat milk when the material for vegetable protein food and drink is oat milk is, for example, 0.06 U or more, and the dispersion stability of oat milk is mentioned. And / or from the viewpoint of further enhancing the solubility, preferably 0.18 U or more, more preferably 0.24 U or more, still more preferably 0.3 U or more, still more preferably 0, from the viewpoint of further enhancing the dispersion stability. It is .36U or more, more preferably 0.48U or more, and particularly preferably 0.54U or more.
- the upper limit of the range of the amount of the protein deamidating enzyme used per 1 g of auto is not particularly limited, and examples thereof include 5 U or less.
- suitable examples of the upper limit of the range of use of the protein deamidating enzyme per 1 g of auto are, for example, 4 or less, preferably 3 U or less, more preferably 2 U or less, still more preferably 1.5 U or less. More preferably, it is 1 U or less, and particularly preferably 0.7 U or less.
- the amount of the protein deamidating enzyme used per 1 g of black soybean protein is 0.1 U or more, 0.5 U or more, preferably 1 U or more, more preferably 1.5 U or more, and further. 2U or more is preferable, and 2.5U or more is more preferable.
- the upper limit of the range of the amount of the protein deamidating enzyme used per 1 g of black soybean protein is not particularly limited, and examples thereof include 25 U or less. Since the present invention is excellent in the effect of improving dispersion stability and / or solubility, the effect can be effectively obtained without using a large amount of protein deamidating enzyme. From this point of view, suitable examples of the upper limit of the range of use of the protein deamidating enzyme per 1 g of black soybean protein include, for example, 20 U or less, preferably 15 U or less, more preferably 10 U or less, still more preferably 5 U or less, and one layer. Preferred is 3U or less.
- the amount of protein deamidating enzyme used per 1 g of black soybean milk used for black soybean milk when the material for vegetable protein food and drink is black soybean milk is, for example, 0.05 U or more, and the dispersion stability of black soybean milk is mentioned.
- / or from the viewpoint of further enhancing the solubility preferably further enhancing the solubility (particularly, further increasing the amount of solute molecules exhibiting absorption at a wavelength of 280 nm), preferably 0.1 U or more, more preferably. Is 0.25U or more, more preferably 0.4U or more, more preferably 0.55U or more, still more preferably 0.7U or more, and particularly preferably 0.85U or more.
- the upper limit of the range of the amount of the protein deamidating enzyme used per 1 g of black soybean is not particularly limited, and examples thereof include 10 U or less. Since the present invention is excellent in the effect of improving dispersion stability and / or solubility, the effect can be effectively obtained without using a large amount of protein deamidating enzyme. From this point of view, as a preferable example of the upper limit of the amount of the protein deamidating enzyme used per 1 g of black soybean, for example, 8 U or less, preferably 6 U or less, more preferably 4 U or less, still more preferably 3 U or less, still more preferable. Is 2U or less, more preferably 1U or less.
- the walnut protein of the protein deamidating enzyme is used from the viewpoint of further enhancing the dispersion stability and / or solubility of the walnut milk, preferably from the viewpoint of further enhancing the dispersion stability.
- the amount used per 1 g is 0.1 U or more, 0.5 U or more, 1 U or more, preferably 1.5 U or more, more preferably 2 U or more, still more preferably 2.5 U or more, still more preferably 3 U or more, still more. It is preferably 4U or more, and particularly preferably 5U or more.
- the upper limit of the range of the amount of the protein deamidating enzyme used per 1 g of walnut protein is not particularly limited, and examples thereof include 25 U or less.
- suitable examples of the upper limit of the range of use of the protein deamidating enzyme per 1 g of walnut protein include, for example, 22 U or less, preferably 17 U or less, more preferably 14 U or less, still more preferably 12 U or less, and one layer. It is preferably 9 U or less, more preferably 7 U or less, and particularly preferably 6 U or less.
- the amount of the protein deamidating enzyme used per 1 g of walnut used in walnut milk is, for example, 0.05 U or more, and the dispersion stability of walnut milk is mentioned. And / or from the viewpoint of further enhancing the solubility, preferably 0.1 U or more, more preferably 0.25 U or more, still more preferably 0.4 U or more, still more preferably 0, from the viewpoint of further enhancing the dispersion stability. It is .55U or more, more preferably 0.7U or more, and particularly preferably 0.85U or more.
- the upper limit of the range of the amount of the protein deamidating enzyme used per 1 g of walnut is not particularly limited, and examples thereof include 10 U or less.
- the present invention is excellent in the effect of improving dispersion stability and / or solubility, the effect can be effectively obtained without using a large amount of protein deamidating enzyme.
- the upper limit of the usage range of the protein deamidating enzyme per 1 g of walnut for example, 8 U or less, preferably 6 U or less, more preferably 4 U or less, still more preferably 3 U or less, still more preferable. Is 2U or less, more preferably 1.5U or less.
- Vegetable protein When the food and drink material is peanut milk, 1 g of peanut protein, a protein deamidating enzyme, from the viewpoint of further enhancing the dispersion stability and / or solubility of the peanut milk, preferably further enhancing the solubility.
- the amount used per unit is 0.05 U or more, preferably 0.1 U or more, more preferably 0.2 U or more, still more preferably 0.4 U or more, still more preferably 0.6 U or more, still more preferably 0.8 U. As mentioned above, 0.9U or more is particularly preferable.
- the upper limit of the range of the amount of the protein deamidating enzyme used per 1 g of peanut protein is not particularly limited, and examples thereof include 25 U or less.
- the present invention is excellent in the effect of improving dispersion stability and / or solubility, the effect can be effectively obtained without using a large amount of protein deamidating enzyme.
- the upper limit of the usage range of the protein deamidating enzyme per 1 g of peanut protein for example, 20 U or less, preferably 15 U or less, more preferably 10 U or less, still more preferably 5 U or less, and more. More preferably, 3U or less can be mentioned.
- the amount of protein deamidating enzyme used per 1 g of peanuts used for peanut milk when the material for vegetable protein food and drink is peanut milk is, for example, 0.05 U or more, and the dispersion stability of peanut milk is mentioned. And / or from the viewpoint of further enhancing the solubility, preferably further enhancing the solubility, preferably 0.01 U or more, more preferably 0.05 U or more, still more preferably 0.09 U or more, still more preferably 0. 13U or more, more preferably 0.17U or more, and particularly preferably 0.21U or more.
- the upper limit of the range of the amount of the protein deamidating enzyme used per 1 g of peanuts is not particularly limited, and examples thereof include 10 U or less.
- the present invention is excellent in the effect of improving dispersion stability and / or solubility, the effect can be effectively obtained without using a large amount of protein deamidating enzyme.
- the upper limit of the usage range of the protein deamidating enzyme per 1 g of peanuts for example, 5 U or less, preferably 3 U or less, more preferably 2 U or less, still more preferably 1 U or less, still more preferable.
- the material for vegetable protein food and drink is coconut milk
- coconut milk from the viewpoint of further enhancing the dispersion stability and / or solubility of the protein deamidating enzyme coconut milk, preferably further enhancing the solubility (particularly at a wavelength of 280 nm).
- the amount of the protein deamidating enzyme used per 1 g of coconut protein is 0.1 U or more, 0. .5 U or more, preferably 1 U or more, more preferably 1.5 U or more, still more preferably 2 U or more, still more preferably 2.5 U or more.
- the upper limit of the range of the amount of the protein deamidating enzyme used per 1 g of coconut protein is not particularly limited, and examples thereof include 25 U or less. Since the present invention is excellent in the effect of improving dispersion stability and / or solubility, the effect can be effectively obtained without using a large amount of protein deamidating enzyme. From this point of view, as a preferable example of the upper limit of the usage range of the protein deamidating enzyme per 1 g of coconut protein, for example, 20 U or less, preferably 15 U or less, more preferably 10 U or less, still more preferably 5 U or less, and more. More preferably, 3U or less can be mentioned.
- the amount of protein deamidating enzyme used per 1 g of coconut used in coconut milk when the material for vegetable protein food and drink is coconut milk is, for example, 0.006 U or more, and the dispersion stability of coconut milk is mentioned. And / or from the viewpoint of further increasing the solubility, preferably further increasing the solubility (in particular, further increasing the amount of solute molecules exhibiting absorption at a wavelength of 280 nm), or further improving the yield of coconut milk. From the viewpoint of making the protein, preferably 0.012 U or more, more preferably 0.024 U or more, still more preferably 0.036 U or more, still more preferably 0.06 U or more, still more preferably 0.07 or more.
- the upper limit of the range of the amount of the protein deamidating enzyme used per 1 g of coconut is not particularly limited, but is preferably 0.6 U or less. Since the present invention is excellent in the effect of improving dispersion stability and / or solubility, the effect can be effectively obtained without using a large amount of protein deamidating enzyme. From this point of view, as a preferable example of the upper limit of the usage range of the protein deamidating enzyme per 1 g of coconut, for example, 0.45 U or less, preferably 0.3 U or less, more preferably 0.15 U or less, still more preferable. Is 0.09U or less.
- benzyloxycarbonyl-L-glutaminylglycine (Z-Gln-Gly) is used as a substrate, and the amount of the enzyme that liberates 1 ⁇ mol of ammonia per minute is 1 unit (1U).
- Lipase used in the present invention is particularly limited in its type and origin as long as it is an enzyme that hydrolyzes ester bonds constituting lipids, specifically, an enzyme that decomposes triglycerides and exhibits an activity to release fatty acids.
- Rhizopus include the genus Rhizopus, such as Rhizopus delemar and Rhizopus oryzae, Rhizopus arriz, Rhizopus arrhizus, Rhizopus arrhizus.
- genus Aspergillus such as Aspergillus niger
- genus Mucor such as Mucor javanicus, Mucor miehei, eg Rhizopus; RhizoMucor mieehei, etc .
- Thermomyces for example, Thermomyces lanuginosus, etc .
- Pseudomonas Rhizopus, Rhizopus, Rhizopus, Rhizopus, Rhizopus, Rhizopus, Rhizopus, Rhizopus, Rhizopus, Rhizopus, Rhizopus, Rhizopus, Rhizopus, Rhizopus, Rhizopus, Rhizopus, Rhizopus, Rhizopus, Rhizopus, Rhizopus, Rhizopus, Rhizopus, Rhizopus, Rhizopus, Rhizopus, Rhizopus, Rhizopus, Rhizopus, Rhizopus, Rhizopus, Rhizopus, Rhizopus, Rhizopus, Rhizopus, Rhizopus, Rhizopus, Rhizopus, Rhizopus, Rhizopus,
- 1,3-position specific lipase is preferable from the viewpoint of further improving the dispersion stability and / or solubility of vegetable milk.
- the genus Rhizopus (preferably Rhizopus oryzae) and the genus Rhizopus (preferably Rhizopus oryzae) are particularly preferable from the viewpoint of significantly improving the dispersion stability and / or solubility of vegetable milk.
- Derived lipase More specifically, among these lipases, the genus Rhizopus (preferably Rhizopus oryzae) and the genus Rhizopus (preferably) are particularly preferable from the viewpoint of significantly improving the dispersion stability of vegetable milk, particularly walnut milk.
- Lipase derived from Rhizopus oryzalis significantly improves the solubility of vegetable milk, especially walnut milk and peanut milk (particularly significantly increases the amount of solute molecules that exhibit absorption at a wavelength of 280 nm). From the viewpoint, a lipase derived from the genus Rhizopus (preferably Rhizopus oryzae) is particularly preferable.
- Lipase can be prepared from the culture solution of the microorganism from which the above lipase is derived.
- the specific preparation method is the same as the above-mentioned preparation method for protein deamidating enzyme.
- lipase DF lipase DF
- lipase MHA lipase MHA
- Amano lipase 10SD manufactured by Amano Enzyme Co., Ltd.
- a preferable example when lipase is used is a case where walnut milk and / or peanut milk is treated as a vegetable protein food or drink material, and a more preferable example is the dispersion stability of walnut milk. It may be used for the purpose of improving and / or for the purpose of improving the solubility of peanut milk (particularly, increasing the amount of solute molecules exhibiting absorption at a wavelength of 280 nm).
- the amount of lipase used is not particularly limited, but examples of the amount used per 1 g of vegetable protein raw material used for vegetable protein food and drink materials include 0.5 U or more. From the viewpoint of further improving the dispersion stability and / or solubility of the vegetable milk, the amount used per 1 g of the vegetable protein raw material used for the vegetable protein food and drink material of lipase is preferably 1 U or more. .. In particular, when a lipase derived from the genus Risops (preferably Risops oryzae) is used as the lipase, the amount used per 1 g of the plant protein raw material used for the vegetable protein food and drink material is the dispersion stability of the vegetable milk and the dispersion stability.
- Risops preferably Risops oryzae
- Vegetable protein The amount used per 1 g of plant protein raw material used for food and drink materials is more preferably 1 U or more, further preferably 1 U or more, from the viewpoint of further improving the dispersion stability and / or solubility of plant milk. Is 3U or more, more preferably 4U or more, and even more preferably 5U or more.
- the upper limit of the range of the amount of vegetable protein used per 1 g of the vegetable protein raw material used for the vegetable protein food and drink material of lipase is not particularly limited, and examples thereof include 1000 U or less, 800 U or less, or 550 U or less.
- a lipase derived from the genus Rhizopus preferably Rhizopus oryzae
- the dispersion stability and / or the solubility can be improved extremely efficiently, so that excellent dispersion stability and excellent dispersion stability even when used in a small amount can be achieved. / Or the effect of improving solubility can be obtained.
- the upper limit of the range of use per 1 g of vegetable protein raw material used for vegetable protein food and drink materials when lipase derived from the genus Rhizopus (preferably Rhizopus oryzae) is used as lipase For example, 1000 U or less, preferably 500 U or less, more preferably 300 U or less, and more preferably 200 U or less.
- the dispersion stability and / or the solubility, particularly the dispersion stability can be improved extremely efficiently, so that the dispersion stability and / or the excellent dispersion stability and / or even when used in a small amount can be improved.
- solubility particularly dispersion stability.
- the upper limit of the usage range per 1 g of the vegetable protein raw material used for the vegetable protein food and drink material when the lipase derived from the genus Mucor is used as the lipase for example, 50 U or less is preferable. Is 30 U or less, more preferably 15 U or less, still more preferably 9 U or less, still more preferably 7 U or less.
- the ratio between the amount of the protein amide enzyme used and the amount of lipase used is determined according to the amount of each enzyme used, but it has the effect of improving the dispersion stability and / or solubility of vegetable protein food and drink materials and the like. From the viewpoint of further enhancing, the ratio of the amount of lipase used per 1 U of protein deamidating enzyme is preferably 1 U or more.
- the dispersion stability and / or solubility of vegetable milk is further improved as the ratio of the amount of lipase used per 1 U of protein deamidating enzyme.
- the ratio of the amount of lipase used per 1 U of protein deamidating enzyme is more preferably 2 U from the viewpoint of further improving the dispersion stability and / or solubility of vegetable milk. Above, more preferably 5U or more.
- the upper limit of the range of the ratio of the amount of lipase used per 1 U of protein deamidating enzyme is not particularly limited, and examples thereof include 200 U or less.
- a lipase derived from the genus Rhizopus preferably Rhizopus oryzae
- a suitable example of the upper limit of the range of the amount of lipase used per 1 U of protein deamidating enzyme is preferably 100 U from the same viewpoint as above. Hereinafter, it is more preferably 90 U or less, still more preferably 80 U or less.
- a suitable example of the upper limit of the range of the amount of lipase used per 1 U of protein deamidating enzyme is preferably 50 U or less, more preferably 30 U or less from the same viewpoint as above. , More preferably 15 U or less, still more preferably 9 U or less, still more preferably 7 U or less.
- olive oil is used as a substrate, and the amount of enzyme that causes an increase of 1 micromolar fatty acid per minute is 1 unit (1U).
- Cyclodextrin lucanotransferase used in the present invention acts on ⁇ -1,4-glucan and is a cyclic ⁇ -1,4-glucan due to its intramolecular transfer activity (CD). As long as it is an enzyme that produces glucan, its type and origin are not particularly limited.
- cyclodex string lucanotransferases examples include the genus Bacillus, such as Bacillus stearothermophilus, Bacillus megaterium, Bacillus cyclans, Bacillus cyclus ), Bacillus ohbensis, Bacillus clarkii; genus Klebsiella, for example, Klebsiella pneumoniae; from the genus Klebsiella pneumoniae; Cyclodex string lucanotransferase of. These cyclodextrin glucanotransferases may be used alone or in combination of two or more.
- cyclodextrine lucanotransferases from the viewpoint of further improving the dispersion stability and / or solubility of vegetable protein food and drink materials, it is preferably derived from the genus Bacillus, more preferably the genus Bacillus, that is, Geobacillus. Cyclodextrin lucanotransferases derived from the genus (Geobacillus), more preferably thermophilic Bacillus stearomophilus or Geobacillus stearomophilus.
- Cyclodextrin lucanotransferase can be prepared from the culture medium of the microorganism from which the above cyclodextrin lucanotransferase is derived.
- the specific preparation method is the same as the above-mentioned preparation method for protein deamidating enzyme.
- a commercially available product can be used as the cyclodextrin glucanotransferase, and an example of a preferable commercially available product is Contizyme manufactured by Amano Enzyme Co., Ltd.
- a preferable example of the case of using the cyclodex ring lucanotransferase includes the case of treating auto milk, black soybean milk, peanut milk, and / or coconut milk as a vegetable protein food and drink material.
- Preferred examples are when used for the purpose of improving the dispersion stability of automilk, and when used for the purpose of improving the solubility of black soybean milk (particularly, increasing the amount of solute molecules exhibiting absorption at a wavelength of 280 nm).
- the amount of cyclodextrin lucanotransferase used is not particularly limited, and examples of the amount used per 1 g of vegetable protein raw material used for vegetable protein food and drink materials include 0.01 U or more and 1000 U or less.
- the amount of cyclodex ring lucanotransferase used per 1 g of oat milk used for oat milk is 0.01 U or more, and the dispersion stability of oat milk and / Alternatively, from the viewpoint of further enhancing the solubility, preferably further enhancing the dispersion stability, preferably 0.05 U or more, more preferably 0.1 U or more, still more preferably 0.2 U or more, still more preferably 0.3 U. As mentioned above, 0.4U or more is more preferable.
- oat milk is a milk containing a particularly large amount of starch among vegetable milks
- dispersion stability tends to be improved by using a large amount of ⁇ -amylase as a protein deamidating enzyme.
- the amount of cyclodextrin lucanotransferase used is relatively small because the dispersion stability can be improved exceptionally efficiently by treating the protein deamidextrin in combination with cyclodextrin lucanotransferase. Even so, an excellent effect of improving dispersion stability can be obtained.
- a suitable example of the upper limit of the range of the amount of cyclodextrin glucanotransferase used per 1 g of the vegetable protein raw material used for the vegetable protein food and drink material is 2 U or less, preferably 1 U or less. It is preferably 0.5 U or less, more preferably 0.3 U or less.
- the amount of cyclodextrin glucanotransferase used per 1 g of black soybean milk used for black soybean milk is 0.01 U or more, and the dispersion stability of black soybean milk and /
- the amount is preferably 0.05 U or more, more preferably 0. .1U or more, more preferably 0.2U or more, still more preferably 0.3U or more, still more preferably 0.4U or more.
- the upper limit of the range of use of cyclodextrin glucanotransferase per 1 g of black soybean is not particularly limited, but suitable examples include 10 U or less, 5 U or less, 3 U or less, 2 U or less, 1 U or less, or 0.5 U or less. ..
- the amount of cyclodextrin glucanotransferase used per 1 g of peanut milk used in the peanut milk is, for example, 0.05 U or more, and the dispersion stability of the peanut milk and the dispersion stability of the peanut milk are mentioned.
- the solubility preferably 0.1 U or more, more preferably 1 U or more, still more preferably 10 U or more, still more preferably 20 or more, still more preferably. 30U or more, particularly preferably 35U or more.
- the upper limit of the range of use of cyclodextrin glucanotransferase per 1 g of peanuts is not particularly limited, but suitable examples include 1000 U or less, 100 U or less, 80 U or less, 60 U or less, 50 U or less, or 45 U or less.
- the amount of cyclodextone lucanotransferase used per 1 g of coconut used in coconut milk is, for example, 0.05 U or more, and the dispersion stability of coconut milk and / Or from the viewpoint of further increasing the solubility, preferably further increasing the solubility, or further increasing the yield of coconut milk, preferably 0.1 U or more, more preferably 1 U or more, still more preferably 10 U or more. , More preferably 20 or more, even more preferably 30 U or more, and particularly preferably 35 U or more.
- the upper limit of the range of use of cyclodextrin glucanotransferase per 1 g of coconut is not particularly limited, but suitable examples include 1000 U or less, 100 U or less, 80 U or less, 60 U or less, 50 U or less, or 45 U or less.
- the ratio between the amount of the protein amide enzyme used and the amount of the cyclodextrin glucanotransferase used is determined according to the amount of each enzyme used, but from the viewpoint of further enhancing the effect of improving the texture of vegetable milk, Preferably, the ratio of the amount of cyclodextrin lucanotransferase used per 1 U of protein deamidextrin is 0.05 U or more and 1000 U or less.
- the ratio of the amount of cyclodextrin lucanotransferase used per 1U of protein deamidextrin is from the viewpoint of further enhancing the dispersion stability and / or solubility of black soybean milk. From the viewpoint of further enhancing the solubility (particularly, further increasing the amount of solute molecules exhibiting absorption at a wavelength of 280 nm), preferably 0.1 U or more, more preferably 0.15 U or more, still more preferably 0. .3U or more, more preferably 0.4U or more.
- the upper limit of the range of the ratio of the amount of cyclodextrin lucanotransferase used per 1 U of protein deamidating enzyme when the vegetable protein food or drink material is black soybean milk is not particularly limited, but as a suitable example, 10 U or less and 5 U.
- 3U or less, 2U or less, 1U or less, or 0.5U or less may be mentioned.
- the ratio of the amount of cyclodextrin lucanotransferase used per 1 U of protein deamidextrin is from the viewpoint of further enhancing the dispersion stability and / or solubility of peanut milk. From the viewpoint of further enhancing the solubility, preferably 1 U or more, more preferably 10 U or more, still more preferably 30 U or more, still more preferably 50 U or more, still more preferably 60 U or more.
- the upper limit of the ratio range of the amount of cyclodextrin lucanotransferase used per 1 U of protein deamidextrin when the vegetable protein food or drink material is peanut milk is not particularly limited, but as a suitable example, 1000 U or less, 200 U
- 150 U or less, 90 U or less, or 70 U or less may be mentioned.
- the ratio of the amount of cyclodextrin lucanotransferase used per 1 U of protein deamidextrin is from the viewpoint of further enhancing the dispersion stability and / or solubility of coconut milk. From the viewpoint of further increasing the solubility, or further increasing the yield of coconut milk, preferably 10 U or more, preferably 100 U or more, more preferably 300 U or more, still more preferably 500 U or more.
- the upper limit of the range of the ratio of the amount of cyclodextrin glucanotransferase used per 1 U of protein deamidating enzyme is not particularly limited, but suitable examples thereof include 1000 U or less, 800 U or less, or 600 U or less.
- the amount of enzyme that reduces the blue iodine coloration of starch by 1% per minute is 1 unit (1U) using potato starch as a substrate.
- the dispersion stability is preferably improved from the viewpoint of further enhancing the dispersion stability and / or the solubility of the oat milk.
- ⁇ -amylase can be used in combination with the above enzymes.
- ⁇ -amylase is not particularly limited, but for example, the genus Aspergillus, for example, Aspergillus oryzae, Aspergillus niger, etc .; the genus Bacillus, for example, Bacillus.
- ⁇ -amylases derived from Bacillus amyloliquefaciens, Bacillus subtilis, Bacillus licheniformis, etc. are mentioned, and ⁇ -amylase derived from the genus Bacillus is preferable.
- Preferred is ⁇ -amylase derived from Bacillus amyloliquefaciens species.
- the amount of ⁇ -amylase used for example, 0.05 U or more, preferably 0.1 U or more, 0.5 U or more, or 1 U or more per 1 g of auto.
- the upper limit of the range of the amount of ⁇ -amylase used is not particularly limited, and examples thereof include 50 U or less. Since the present invention is excellent in the dispersion stability and / or solubility improving effect of oat milk, particularly the dispersibility improving effect, a large amount of ⁇ -amylase that assists the dispersion stability and / or solubility of oat milk is used. The effect can be effectively obtained without using it.
- suitable examples of the upper limit of the amount range of ⁇ -amylase used are, for example, 10 U or less, preferably 5 U or less, more preferably 4 U or less, still more preferably 3 U or less, still more preferably 2 U or less. Will be.
- soluble starch is used as a substrate, and the amount of enzyme that brings about an increase in reducing power equivalent to 10 mg of glucose in 30 minutes is 1 unit (1 U).
- Protein deamide enzyme, and lipase and / or cyclodexstring lucanotransferase, or vegetable protein such as food and drink materials, protein deamide enzyme, lipase and / or cyclodexstring lucanotransferase, and other enzymes.
- the enzyme treatment reaction can proceed.
- the heating temperature (enzyme treatment reaction temperature) of the composition of the vegetable protein food or drink material is not particularly limited, and a person skilled in the art depends on the optimum temperature of the enzyme used and / or the thermal characteristics of the vegetable protein food or drink material or the like. Can be appropriately determined, and examples thereof include 40 to 70 ° C.
- the heating temperature of the oat milk composition is preferably 50 to 70 ° C, more preferably 55 to 65 ° C, and even more preferably 58 to 62 ° C. °C is mentioned.
- the heating temperature of the black soybean milk composition is preferably 40 to 60 ° C., more preferably 45 to 55 ° C., still more preferably 48 to 52 ° C.
- the heating temperature of the walnut milk composition is preferably 40 to 60 ° C, more preferably 45 to 55 ° C, still more preferably 48 to 52 ° C.
- the heating temperature of the peanut milk composition is preferably 40 to 60 ° C, more preferably 45 to 55 ° C, still more preferably 48 to 52 ° C.
- the heating temperature of the coconut milk composition is preferably 40 to 60 ° C, more preferably 45 to 55 ° C, still more preferably 48 to 52 ° C.
- the enzyme treatment reaction time of the composition such as vegetable protein food and drink material is not particularly limited and may be appropriately determined according to the charging scale and the like of the composition, but for example, 0.5 hours or more, preferably 1 hour or more. Can be mentioned.
- the upper limit of the range of the enzyme treatment reaction time is not particularly limited, and examples thereof include 24 hours or less, 12 hours or less, 8 hours or less, or 6 hours or less.
- the enzyme treatment reaction can be terminated by enzyme deactivation treatment with high heat.
- the enzyme deactivation treatment temperature is, for example, 85 ° C. or higher, preferably 90 ° C. or higher, and the enzyme deactivation treatment time is, for example, 5 to 25 minutes, preferably 10 to 20 minutes.
- the composition such as vegetable protein food and drink material is obtained as processed vegetable milk by performing post-treatment such as filtration as necessary.
- the number of meshes of the sieve used for filtering the composition such as vegetable protein food and drink material after the completion of the enzyme treatment is, for example, 80 to 120 mesh, preferably 85 to 115 mesh, more preferably 90 to 110 mesh, and further. Preferred are 95-105 meshes.
- the processed vegetable protein food and drink material can be obtained as a food and drink material having improved dispersion stability and / or dissolution stability as compared with the vegetable protein food and drink material before enzyme treatment.
- the processed automilk can be obtained as a milk having improved dispersion stability and / or dissolution stability, preferably dispersion stability, as compared with the automilk before the enzyme treatment;
- the processed black soybean milk is an enzyme.
- the processed walnut milk can be obtained as a milk having improved dispersion stability and / or dissolution stability, preferably dispersion stability as compared with the walnut milk before the enzyme treatment; the processed peanut milk is the peanut milk before the enzyme treatment.
- the combination of a protein deamidating enzyme with a lipase and / or cyclodextrin lucanotransferase can improve the dispersion stability and / or solubility of vegetable protein food and drink materials.
- the present invention comprises the use of an enzyme agent containing a protein deamidase and lipase for the production of a dispersion stability enhancer for walnut milk and / or peanut milk; including a protein deamide enzyme and a cyclodexing lucanotransferase.
- enzyme preparations for the production of dispersion stability enhancers for automilk and selection from the group consisting of black bean milk, peanut milk, and coconut milk for enzyme preparations including protein deamidase and cyclodextone lucanotransferase.
- solubility-enhancing agents for vegetable milks which include protein deamidating enzymes and lipases, dispersion stability improving agents for walnut milk and / or peanut milk; protein deamidating enzymes and cyclodextrin.
- Dissolution of vegetable milk selected from the group consisting of black soybean milk, peanut milk, and coconut milk, which comprises a gluconotransferase, a dispersion stability enhancer for automilk; and a protein deamidating enzyme and a cyclodexing lucanotransferase. It also provides a sex improver.
- improving the solubility of vegetable protein food and drink materials includes at least one of increasing the amount of solute molecules exhibiting absorption at a wavelength of 280 nm and increasing the amount of dissolved protein.
- the combination of the protein deamidextrin with cyclodextrin glucanotransferase not only further improves the solubility, but also reduces the amount of filter media increased by the use of the protein deamidextrin, and the processed coconut.
- the yield of milk can be improved.
- the present invention comprises the use of an enzyme agent comprising a protein deamidating enzyme and cyclodextrin lucanotransferase for the production of a coconut milk yield improving agent, and comprising a protein deamidating enzyme and a cyclodextrin lucanotransferase. Also provided are coconut milk yield improvers.
- protein deamidating enzyme protein glutaminase
- the activity of protein deamidating enzyme was measured by the following method. (1) To 1 ml of 0.2 M phosphate buffer (pH 6.5) containing 30 mM Z-Gln-Gly, 0.1 ml of an aqueous solution containing a protein deamidating enzyme was added, and the mixture was incubated at 37 ° C. for 10 minutes, and then 0. The reaction was stopped by adding 1 ml of 4M TCA solution.
- the activity of the protein deamidating enzyme was calculated from the following formula, with the amount of the enzyme producing 1 ⁇ mol of ammonia per minute as 1 unit (1 U).
- the amount of the reaction solution is 2.1
- the amount of the enzyme solution is 0.1
- Df is the dilution ratio of the enzyme solution.
- 17.03 is the molecular weight of ammonia.
- the activity of lipase was measured by the following method. Olive oil 75mL and emulsion (polyvinyl alcohol I test solution or polyvinyl alcohol) I. Polyvinyl alcohol II test solution) Put 225 mL in the container of the emulsifier and intermittently rotate at 14500 rpm for 10 minutes (3 minutes 20 seconds rotation ⁇ 3 minutes 20 seconds stop ⁇ 3 minutes 20 seconds) while cooling to 10 ° C or lower. Rotation for seconds ⁇ Stop for 3 minutes and 20 seconds ⁇ Rotation for 3 minutes and 20 seconds) The substrate solution was obtained by stirring and emulsifying. This substrate solution was left in a cold place (5 to 10 ° C.) for 1 hour, and was used after confirming that the oil layer did not separate.
- the activity of cyclodextrin glucanotransferase was measured by the following method. 1.0 g of potato starch was weighed, 20 mL of water was added, and 5 mL of sodium hydroxide test solution (1 mol / L) was gradually added with stirring to form a paste. After heating in a boiling water bath for 3 minutes with stirring, 25 mL of water was added. After cooling, the pH was adjusted to 5.5 with an acetic acid test solution (1 mol / L), and water was added to make 100 mL, which was used as a substrate solution. Weigh 10 mL of the substrate solution, heat at 40 ° C. for 10 minutes, add 1 mL of sample solution, shake immediately, heat at 40 ° C.
- the dispersion stability and solubility of the processed vegetable milk prepared in the following test examples were evaluated by the instability index by LUMiSizer651, A280, soluble protein concentration and the like.
- the instability index by LUMiSizer651 is an index based on the behavior of particles in the centrifuge, and is used as an evaluation index of "dispersion stability".
- A280 represents the total amount of a solute molecule exhibiting absorption at a wavelength of 280 nm, for example, a protein having an aromatic amino acid (tyrosine, tryptophan) residue, and is used as an evaluation index of "solubility".
- the soluble protein concentration represents a value measured by the Lowry method, that is, the amount of protein having a tyrosine residue, a tryptophan residue, and / or a cysteine residue, and is used as an evaluation index of "solubility". Details such as measurement conditions for each evaluation item will be described in each test example.
- Test Example 1 Preparation of black soybean milk 1300 mL of water was added to 208.5 g of black soybeans, kept warm in an electric oven (50 ° C.) for 4 hours, then heated to 100 ° C. on a stove and boiled for about 5 seconds. Further, 160 mL of hot water at 90 ° C. was added and treated with a colloidal mill for 40 minutes to prepare a black soybean slurry. The black soybean slurry was cooled to room temperature, 2000 mL of water was added, and the pH was adjusted to 6.0 (25 ° C.) using 0.5 M citric acid.
- black soybean milk (pH 6.0, 25 ° C.) having a black soybean-derived component content of 5.56 w / v% and a protein content of 2 w / v%.
- the obtained black soybean milk was subdivided into beakers in 500 ml increments with stirring.
- ⁇ A280> The processed black soybean milk was centrifuged at 16000 rpm for 10 minutes, and the supernatant was filtered through a 0.45 ⁇ m membrane filter to measure the absorbance at 280 nm.
- Test Example 2 (1) Preparation of walnut milk 350 g of walnut was immersed in a 1 w / w% sodium hydroxide solution and heated (70 ° C. or higher) for 10 minutes with stirring. The sodium hydroxide solution was discarded, the skin was peeled, washed with water, and drained. 1000 ml of hot water (80 ° C.) was added to 300 g of the obtained peeled walnut and treated with a colloidal mill for 30 minutes to obtain a walnut slurry. After heating the walnut slurry at 90 ° C.
- the walnut slurry was cooled to 50 ° C., and the volumetric flask was adjusted to 1500 g with warm water to prepare walnut milk (the total amount of water per 1 part by weight of the peeled walnut was 4 parts by weight).
- the prepared walnut milk was divided into small portions with stirring.
- ⁇ A280> The processed walnut milk was centrifuged at 14000 rpm for 10 minutes, the supernatant was diluted 50-fold, and the absorbance at 280 nm was measured.
- ⁇ Instability index> The instability index was measured using LumiSizer 651 under the conditions of 4000 rpm (RCA 2100 g), 25 ° C., 865 nm, 300 profiles, Interval 10s, and light factor 1.
- Test Example 3 (1) Preparation of peanut milk 1400 mL (0.8 w / v%) of salt water was added to 350 g of shelled peanuts and boiled for 5 minutes. It was cooled and drained to remove foreign matter (skin, etc.). In an electric oven, the peeled peanuts were roasted at 150 ° C. for 40 minutes and cooled to remove foreign matter. 300 g of the obtained peanuts were weighed, 1800 mL of warm water (50 ° C.) was added, and the mixture was treated with a colloidal mill for 40 minutes to obtain a peanut slurry.
- peanut milk (pH 6.0) having a peanut-derived component content of 8 w / v% and a protein content of 2 w / v% was prepared.
- the prepared peanut milk was divided into 500 ml portions with stirring.
- ⁇ Protein solubilization rate> The percentage of soluble protein (% by weight) when the total protein of the processed peanut milk was 100% by weight was determined.
- Test Example 4 Preparation of coconut milk 1500 g of coconut meat (endosperm of mature coconut fruit) is chopped into 1 cm squares with a kitchen knife, 2000 mL of warm water (50 ° C) is added to this, and colloid is separated while separating the filter with a 100-mesh filter.
- the coconut slurry was prepared by treating with a mill for 120 minutes.
- the separated filter medium is returned to the coconut slurry, adjusted to pH 6.0 (25 ° C) with 0.5 M citric acid, and then volumetrically increased to 3750 mL with warm water (50 ° C) to increase the content of coconut-derived components to 40 w / v%.
- coconut milk with a protein content of 1.2 w / v% was prepared.
- the prepared coconut milk was divided into 500 ml portions with stirring.
- ⁇ A280> The processed coconut milk was centrifuged at 16000 g for 10 minutes, the supernatant was diluted 100-fold, and the absorbance at 280 nm was measured.
- Test Example 5 Further, when protein glutaminase and cyclodextrin lucanotransferase were added to oat milk (the total amount of water per 1 part by weight of oat was about 5 parts by weight) and treated, the solubility of oat milk was improved, and in Test Example 3. It was also confirmed that the solubility of peanut milk was improved by adding protein glutaminase and lipase to the prepared peanut milk and treating it.
Landscapes
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Engineering & Computer Science (AREA)
- Food Science & Technology (AREA)
- Polymers & Plastics (AREA)
- Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- Nutrition Science (AREA)
- Organic Chemistry (AREA)
- Oil, Petroleum & Natural Gas (AREA)
- Medicinal Chemistry (AREA)
- Gastroenterology & Hepatology (AREA)
- Biophysics (AREA)
- General Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Mycology (AREA)
- Coloring Foods And Improving Nutritive Qualities (AREA)
- Non-Alcoholic Beverages (AREA)
- Dairy Products (AREA)
Abstract
Description
項2. 前記植物性タンパク質飲食品素材及び/又は植物性タンパク質飲食品が植物性ミルクである、項1に記載の加工植物性ミルクの製造方法。
項3. 前記植物性タンパク質飲食品素材及び/又は植物性タンパク質飲食品が、オートミルク、黒豆ミルク、クルミミルク、ピーナッツミルク、及びココナッツミルクからなる群より選択される、項1又は2に記載の加工植物性ミルクの製造方法。
項4. 前記植物性タンパク質飲食品素材及び/又は植物性タンパク質飲食品がクルミミルク及び/又はピーナッツミルクであり、前記工程においてリパーゼを用いる、項1~3のいずれかに記載の加工植物性ミルクの製造方法。
項5. 前記リパーゼがリゾパス属又はムコール属由来のリパーゼである、項4に記載の加工植物性ミルクの製造方法。
項6. 前記植物性タンパク質飲食品素材及び/又は植物性タンパク質飲食品が、オートミルク、黒豆ミルク、ピーナッツミルク、及びココナッツミルクからなる群より選択され、前記工程においてシクロデキストリングルカノトランスフェラーゼを用いる、項1~3のいずれかに記載の加工植物性ミルクの製造方法。
項7. 前記ココナッツミルク中のココナッツ由来成分含有量が、10~70w/v%である、項3又は6に記載の加工植物性ミルクの製造方法。
項8. 前記タンパク質脱アミド酵素を植物性タンパク質1g当たり0.01U以上用いる、項1~7のいずれかに記載の加工植物性ミルクの製造方法。
項9. 前記リパーゼを、植物タンパク質原料1g当たり0.5U以上用いる、項1~8のいずれかに記載の加工植物性ミルクの製造方法。
項10. 前記シクロデキストリングルカノトランスフェラーゼを、植物性タンパク質原料1g当たり0.01U以上用いる、項1~9のいずれかに記載の加工植物性ミルクの製造方法。
項11. タンパク質脱アミド酵素及びリパーゼを含む、クルミミルク及び/又はピーナッツミルクの分散安定性向上剤。
項12. タンパク質脱アミド酵素及びシクロデキストリングルカノトランスフェラーゼを含む、オートミルクの分散安定性向上剤。
項13. タンパク質脱アミド酵素及びシクロデキストリングルカノトランスフェラーゼを含む、黒豆ミルク、ピーナッツミルク、及びココナッツミルクからなる群より選択される植物性ミルクの溶解性向上剤。
項14. タンパク質脱アミド酵素及びシクロデキストリングルカノトランスフェラーゼを含む、ココナッツミルクの収率向上剤。
本発明の植物性タンパク質飲食品素材及び/又は植物性タンパク質飲食品の加工物の製造方法は、植物性タンパク質飲食品素材及び/又は植物性タンパク質飲食品を、タンパク質脱アミド酵素及びリパーゼ及び/又はシクロデキストリングルカノトランスフェラーゼで処理する工程を含むことを特徴とする。以下、本発明の植物性タンパク質飲食品素材及び/又は植物性タンパク質飲食品の加工物の製造方法について詳述する。
本発明で用いられる植物性タンパク質飲食品素材及び/又は植物性タンパク質飲食品としては特に限定されるものではない。植物性タンパク質飲食品素材は、植物性タンパク質を含み、そのまま喫食及び/又は喫飲に供されるものではなく、調理を前提としており、飲食品の材料として用いられるものをいう。また、植物性タンパク質飲食品は、そのまま喫食及び/又は喫飲に供されるものをいう。植物性タンパク質飲食品素材及び/又は植物性タンパク質飲食品(以下において、これらをまとめて「植物性タンパク質飲食品素材等」と記載する。)の具体例としては、植物性ミルク、植物性クリーム、植物性代替肉、植物性代替チーズ、植物性タンパク質溶液等が挙げられる。これらの植物性タンパク質飲食品素材等の中でも、本発明の効果をより一層向上させる観点から、好ましくは植物性ミルク、植物性クリーム、植物性タンパク質溶液等の流動性を有するものが挙げられ、より好ましくは植物性ミルクが挙げられる。
本発明で用いられるタンパク質脱アミド酵素としては、ペプチド結合の切断及びタンパク質の架橋を伴わずタンパク質のアミド基含有側鎖を分解する作用を示す酵素であれば、その種類及び由来等は特に限定されない。タンパク質脱アミド酵素の例として、JP2000-50887A、JP2001-218590A、WO2006/075772A1に開示された、クリセオバクテリウム(Chryseobacterium)属、フラボバクテリウム(Flavobacterium)属、エンペドバクター(Empedobacter)属、スフィンゴバクテリウム(Sphingobacterium)属、アウレオバクテリウム(Aureobacterium)属又はミロイデス(Myroides)属由来のタンパク質脱アミド酵素、及びクリセオバクテリウム属由来のプロテイングルタミナーゼの市販品が挙げられる。これらのタンパク質脱アミド酵素としては、1種を単独で用いてもよいし、複数種を組み合わせて用いてもよい。
本発明で用いられるリパーゼとしては、脂質を構成するエステル結合を加水分解する酵素、具体的にはトリグリセリドを分解して脂肪酸を遊離する活性を示す酵素であれば、その種類及び由来等は特に限定されない。リパーゼの例として、リゾプス(Rhizopus)属、例えばリゾプス・デレマー(Rhizopus delemar)及びリゾプス・オリゼ(Rhizopus oryzae)、リゾプス・アリズス(Rhizopus arrhizus)、リゾプス・ニベウス(Rhizopus niveus)、リゾプス・ジャバニクス(Rhizopus javenicus)等;アスペルギルス(Aspergillus)属、例えばアスペルギルス・ニガ(Aspergillus niger)等;ムコール(Mucor)属、例えばムコール・ヤバニカス(Mucor javanicus)、ムコール・ミエヘイ(Mucor miehei)等;リゾムコール(Rhizomucor)属、例えばリゾムコール・ミエヘイ(RhizoMucor miehei)等;サーモミセス(Thermomyces)属、例えばサーモミセス・ラヌギノサス(Thermomyces lanuginosus)等;シュードモナス(Pseudomonas)属、ジオトリケム(Geotrichum)属;ペニシリウム(Penicillium)属;キャンディダ(Candida)属等由来のリパーゼが挙げられる。これらのリパーゼは、1種を単独で用いてもよいし、複数種を組み合わせて用いてもよい。
本発明で用いられるシクロデキストリングルカノトランスフェラーゼとしては、α-1,4-グルカンに作用し、その分子内転移活性により環状α-1,4-グルカンであるシクロデキストリン(CD)を生成させる酵素であれば、その種類及び由来等は特に限定されない。シクロデキストリングルカノトランスフェラーゼの例として、バシラス(Bacillus)属、例えばバシラス・ステアロサーモフィラス(Bacillus stearothermophilus)、バシラス・メガテリウム(Bacillus megaterium)、バシラス・サイクランス(Bacillus circulans)、バシラス・マセランス(Bacillus macerans)、バシラス・オーベンシス(Bacillus ohbensis)、バシラス・クラーキ(Bacillus clarkii);クレブシエラ(klebsiella)属、例えばクレブシエラ・ニューモニア(Klebsiella pneumoniae);サーモアナエロバクター(Thremoanaerobactor)属;ブレビバクテリウム(Brevibacterium) 属等由来のシクロデキストリングルカノトランスフェラーゼが挙げられる。これらのシクロデキストリングルカノトランスフェラーゼは、1種を単独で用いてもよいし、複数種を組み合わせて用いてもよい。
本発明の製造方法においては、植物性タンパク質飲食品素材等がオートミルクである場合、オートミルクの分散安定性及び/又は溶解性をより一層高める観点から、好ましくは分散安定性をより一層高める観点から、上記の酵素と共に、α-アミラーゼを併用することができる。
植物性タンパク質飲食品素材等をタンパク質脱アミド酵素とリパーゼ及び/又はシクロデキストリングルカノトランスフェラーゼで処理する工程においては、上記の植物性タンパク質飲食品素材等にタンパク質脱アミド酵素とリパーゼ及び/又はシクロデキストリングルカノトランスフェラーゼ、必要に応じて上記の植物性タンパク質飲食品素材等にとリパーゼ及び/又はシクロデキストリングルカノトランスフェラーゼと他の酵素とを添加することで、植物性タンパク質飲食品素材等、タンパク質脱アミド酵素、並びにリパーゼ及び/又はシクロデキストリングルカノトランスフェラーゼ、又は、植物性タンパク質飲食品素材等、タンパク質脱アミド酵素、リパーゼ及び/又はシクロデキストリングルカノトランスフェラーゼ、並びに他の酵素を含む植物性タンパク質飲食品素材等組成物を調製し、当該植物性タンパク質飲食品素材等組成物を加熱状態で維持することで、酵素処理反応を進行させることができる。
上述の通り、タンパク質脱アミド酵素とリパーゼ及び/又はシクロデキストリングルカノトランスフェラーゼとの組み合わせは、植物性タンパク質飲食品素材の分散安定性及び/又は溶解性を向上できる。したがって、本発明は、タンパク質脱アミド酵素及びリパーゼを含む酵素剤の、クルミミルク及び/又はピーナッツミルクの分散安定性向上剤の製造のための使用;タンパク質脱アミド酵素及びシクロデキストリングルカノトランスフェラーゼを含む酵素剤の、オートミルクの分散安定性向上剤の製造のための使用;及びタンパク質脱アミド酵素及びシクロデキストリングルカノトランスフェラーゼを含む酵素剤の、黒豆ミルク、ピーナッツミルク、及びココナッツミルクからなる群より選択される植物性ミルクの溶解性向上剤の製造のための使用も提供し、タンパク質脱アミド酵素及びリパーゼを含む、クルミミルク及び/又はピーナッツミルクの分散安定性向上剤;タンパク質脱アミド酵素及びシクロデキストリングルカノトランスフェラーゼを含む、オートミルクの分散安定性向上剤;及びタンパク質脱アミド酵素及びシクロデキストリングルカノトランスフェラーゼを含む、黒豆ミルク、ピーナッツミルク、及びココナッツミルクからなる群より選択される植物性ミルクの溶解性向上剤も提供する。
以下の試験例において使用した酵素の詳細については、次の通りである。
(1)30mM Z-Gln-Glyを含む0.2Mリン酸バッファー(pH6.5)1mlにタンパク質脱アミド酵素を含む水溶液0.1mlを添加して、37℃、10分間インキュベートした後、0.4M TCA溶液を1ml加えて反応を停止した。ブランクとして、30mM Z-Gln-Glyを含む0.2Mリン酸バッファー(pH6.5)1mlに0.4M TCA溶液を1ml加え、さらにタンパク質脱アミド酵素を含む水溶液0.1mlを添加して、37℃で10分間インキュベートした。
(2)(1)で得られた溶液についてアンモニアテストワコー(和光純薬)を用い、反応液中に生じたアンモニア量の測定を行った。アンモニア標準液(塩化アンモニウム)を用いて作成したアンモニア濃度と吸光度(630nm)との関係を表す検量線より、反応液中のアンモニア濃度を求めた。
(3)タンパク質脱アミド酵素の活性を、1分間に1μmolのアンモニアを生成する酵素量を1単位(1U)とし、以下の式から算出した。式中、反応液量は2.1、酵素溶液量は0.1、Dfは酵素溶液の希釈倍率である。また、17.03はアンモニアの分子量である。
オリブ油75mL及び乳化液(ポリビニルアルコールI試液又はポリビニルアルコール
I・ポリビニルアルコールII試液)225mLを乳化器の容器に入れ、10℃以下に冷却
しながら、毎分14500回転で間欠的に10分間(3分20秒回転→3分20秒停止→3分20秒回転→3分20秒停止→3分20秒回転)撹拌して乳化させたものを基質溶液とした。この基質溶液は、冷所(5~10℃)で1時間放置し、油層が分離しないことを確認した後、使用した。基質溶液5mLに緩衝液(pH7.0のリン酸緩衝液(0.1mol/L))4mLを加えて振り混ぜ、37℃で10分間加温した後、試料液1mLを加えて直ちに振り混ぜ、37℃で20分間加温した。この液にエタノール(95)/アセトン混液(体積比で1/1)10mLを加えて振り混ぜた後、0.05mol/L水酸化ナトリウム溶液10mLを加え、更にエタノール(95)/アセトン混液(体積比で1/1)10mLを加えて振り混ぜ、検液とした。別に基質溶液5mLに検液の場合と同一の緩衝液4mLを加えて振り混ぜ、37℃で30分間加温し、エタノール(95)/アセトン混液(体積比で1/1)10mLを加えた後、試料液1mLを加えて振り混ぜ、0.05mol/L水酸化ナトリウム溶液10mLを加え、更にエタノール(95)/アセトン混液(体積比で1/1)10mLを加えて振り混ぜ、比較液とした。検液及び比較液に指示薬としてフェノールフタレイン試液2滴を加えて直ちに窒素ガスを液面に吹き付けながら0.05mol/L塩酸でpH10.0まで滴定した。本条件下、1分間に1マイクロモルの脂肪酸の増加をもたらす酵素量を1単位(1U)とし次式より算出した。
バレイショデンプン1.0gを量り、水20mLを加え、水酸化ナトリウム試液(1mol/L)5mLを撹拌しながら徐々に加えて糊状とした。撹拌しながら沸騰水浴中で3分間加熱した後、水25mLを加えた。冷後、酢酸試液(1mol/L)でpH5.5に調整し、水を加えて100mLとしたものを基質溶液とした。基質溶液10mLを量り、40℃で10分間加温し、試料液1mLを加えて直ちに振り混ぜ、40℃で10分間加温した後、この液1mLを量り、塩酸試液(0.1mol/L)10mLに加えて直ちに振り混ぜた。この液1mLを量り、ヨウ素・ヨウ化カリウム試液(0.4mmol/L)10mLを加えて振り混ぜ、検液とした。別に試料液の代わりに水を用いて検液の調製と同様に操作し、比較液とした。検液及び比較液につき、波長660nmにおける吸光度を測定する。本条件下、1分間にデンプンの青色ヨウ素呈色を1%減少させる酵素量を1単位(1U)とした。
以下の試験例において調製した加工植物性ミルクの分散安定性及び溶解性は、LUMiSizer651による不安定指数、A280、可溶性タンパク質濃度等により評価した。LUMiSizer651による不安定指数は、遠心中の粒子の挙動に基づく指数であり、「分散安定性」の評価指標とする。A280は波長280nmにおいて吸収を示す溶質分子、例えば、芳香族アミノ酸(チロシン、トリプトファン)残基を有するタンパク質の総量を表し、「溶解性」の評価指標とする。可溶性タンパク質濃度はLowry法による測定値、つまりチロシン残基、トリプトファン残基、及び/又はシステイン残基を有するタンパク質の量を表し、「溶解性」の評価指標とする。それぞれの評価項目の測定条件等の詳細については、各試験例で述べる。
(1)黒豆ミルクの調製
黒豆208.5gに水を1300mL加え、電気オーブン(50℃)で4時間保温し、その後、コンロで100℃まで加熱し、5秒程度煮沸した。さらに90℃の熱水を160mL加え、コロイドミルで40分間処理して黒豆スラリーを調製した。黒豆スラリーを室温まで冷却し、水を2000mL加え、0.5Mクエン酸を用いてpH6.0(25℃)に調整した。さらに、黒豆スラリーに水を加えて3750mLまでメスアップし、黒豆由来成分含有量5.56w/v%、タンパク質含有量2w/v%の黒豆ミルク(pH6.0、25℃)を得た。得られた黒豆ミルクは撹拌しながら500mlずつビーカーへ小分けした。
500mlの黒豆ミルクに、表2に示す酵素を表示の量で投入し、50℃で6時間反応させた。90℃、15分間処理で酵素失活処理を行った後、ミキサーで5分間撹拌し、加工黒豆ミルクを得た。
得られた加工黒豆ミルクについて、pH(25℃)及びA280を測定した。結果を表2に示す。
加工黒豆ミルクを16000rpmで10分間遠心し、上清を0.45μmメンブランフィルターでろ過して、280nmの吸光度を測定した。
(1)クルミミルクの調製
クルミ350gを1w/w%水酸化ナトリウム溶液に漬け、10分間加熱(70℃以上)撹拌した。水酸化ナトリウム溶液を棄て、皮を剥き、水洗いし、水切りを行った。得られた皮剥きクルミ300gに湯(80℃)を1000ml添加し、コロイドミルで30分間処理してクルミスラリーとした。クルミスラリーを90℃で15分間加熱した後、50℃まで冷却し、温水で1500gまでメスアップし、クルミミルク(皮むきクルミ1重量部に対する水の総量は4重量部)を調製した。調製したクルミミルクは、撹拌しながら小分けした。
表3に示す酵素を、表示の量で投入し、50℃で3時間反応させた。90℃で15分間、酵素失活処理を行った後、かき混ぜ、篩(100メッシュ)でろ過し、加工クルミミルクを得た。
得られた加工クルミミルクについて、A280及び不安定指数を測定した。結果を表3に示す。
加工クルミミルクを14000rpmで10分間遠心し、上清を50倍に希釈し、280nmの吸光度を測定した。
LUMiSizer 651を用い、4000rpm(RCA 2100g)、25℃、865nm、300 profiles、Interval 10s、light factor 1の条件で、不安定指数を測定した。
(1)ピーナッツミルクの調製
殻取りピーナッツ350gに塩水1400mL(0.8w/v%)を入れ、5分間煮沸処理した。冷却して水切りし、異物(皮など)を除去した。電気オーブンで、皮取りピーナッツを150℃で40分間ローストし、冷却して異物を除去した。得られたピーナッツを300g秤量し、温水(50℃)を1800mL加え、コロイドミルで40分間処理してピーナッツスラリーを得た。ピーナッツスラリーに水を1700mL添加し、5分間煮沸し、室温まで冷却後、pH6.0(0.5Mクエン酸)に調整し、温水で3750mLまでメスアップした。これによって、ピーナッツ由来成分含有量8w/v%、タンパク質含有量2w/v%のピーナッツミルク(pH6.0)を調製した。調製したピーナッツミルクは、撹拌しながら500mlずつ小分けした。
表4に示す酵素を、表示の量で投入し、50℃で1時間、3時間、又は6時間反応させた。90℃で15分間、酵素失活処理を行った後、かき混ぜ、篩(100メッシュ)でろ過し、加工ピーナッツミルクを得た。
得られた加工ピーナッツミルクについて、pH(25℃)、可溶性タンパク濃度(mg/mL)、及びタンパク質可溶化率(%)を測定した。結果を表4に示す。
加工ピーナッツミルクを遠心(16000×g、10分)し、上清のろ液(0.45μmフィルター)を用いて、Lowry法により可溶性タンパク質濃度を測定した。
加工ピーナッツミルクの全タンパク質を100重量%とした場合の、可溶性タンパク質の割合(重量%)を求めた。
(1)ココナッツミルクの調製
ココナッツミート(ココナッツの成熟果の胚乳)1500gを包丁で1センチ角に刻み、これに温水(50℃)を2000mL加え、100-メッシュフィルターで濾物を分離しながらコロイドミルで120分間処理し、ココナッツスラリーを調製した。分離した濾物をココナッツスラリーに戻し、0.5Mクエン酸でpH6.0(25℃)に調整後、温水(50℃)で3750mLまでメスアップすることで、ココナッツ由来成分含有量40w/v%、タンパク質含有量1.2w/v%のココナッツミルクを調製した。調製したココナッツミルクは、撹拌しながら500mlずつ小分けした。
500mlのココナッツミルクに、表5に示す酵素を表示の量で投入し、50℃で6時間反応させた。90℃で15分間、酵素失活処理を行った後、ミキサーで5分間かき混ぜ、フィルター(100-メッシュ)でろ過し、加工ココナッツミルクを得た。
得られた加工ココナッツミルクについて、pH(25℃)、A280及び収率(%)を測定した。結果を表5に示す。
加工ココナッツミルクを16000gで10分間遠心し、上清を100倍に希釈し、280nmの吸光度を測定した。
上記(2)の酵素失活処理後のココナッツミルク組成物500mlの体積を100%とした場合の、当該ココナッツミルク組成物をフィルター(100-メッシュ)で濾物を除去した後の加工ココナッツミルクの相対体積(%)を、収率として導出した。
また、オートミルク(オート1重量部に対する水の総量は約5重量部)にプロテイングルタミナーゼ及びシクロデキストリングルカノトランスフェラーゼを加えて処理すると、オートミルクの溶解性が向上したこと、及び、試験例3で調製したピーナッツミルクにプロテイングルタミナーゼ及びリパーゼを加えて処理すると、ピーナッツミルクの溶解性が向上したことも確認した。
Claims (14)
- 植物性タンパク質飲食品素材及び/又は植物性タンパク質飲食品を、タンパク質脱アミド酵素とリパーゼ及びシクロデキストリングルカノトランスフェラーゼからなる群より選択される少なくとも1種の酵素とで処理する工程を含む、植物性タンパク質飲食品素材及び/又は植物性タンパク質飲食品の加工物の製造方法。
- 前記植物性タンパク質飲食品素材及び/又は植物性タンパク質飲食品が植物性ミルクである、請求項1に記載の製造方法。
- 前記植物性タンパク質飲食品素材及び/又は植物性タンパク質飲食品が、オートミルク、黒豆ミルク、クルミミルク、ピーナッツミルク、及びココナッツミルクからなる群より選択される、請求項1に記載の製造方法。
- 前記植物性タンパク質飲食品素材及び/又は植物性タンパク質飲食品がクルミミルク及び/又はピーナッツミルクであり、前記工程においてリパーゼを用いる、請求項1に記載の製造方法。
- 前記リパーゼがリゾプス属及びムコール属由来のリパーゼからなる群より選択される、請求項4に記載の製造方法。
- 前記植物性タンパク質飲食品素材及び/又は植物性タンパク質飲食品が、オートミルク、黒豆ミルク、ピーナッツミルク、及びココナッツミルクからなる群より選択され、前記工程においてシクロデキストリングルカノトランスフェラーゼを用いる、請求項1に記載の製造方法。
- 前記ココナッツミルク中のココナッツ由来成分含有量が、10~70w/v%である、請求項2に記載の製造方法。
- 前記タンパク質脱アミド酵素を植物性タンパク質1g当たり0.01U以上用いる、請求項1に記載の製造方法。
- 前記リパーゼを、植物性タンパク質原料1g当たり0.5U以上用いる、請求項1に記載の製造方法。
- 前記シクロデキストリングルカノトランスフェラーゼを、植物性タンパク質原料1g当たり0.01U以上用いる、請求項1に記載の製造方法。
- タンパク質脱アミド酵素及びリパーゼを含む、クルミミルク及び/又はピーナッツミルクの分散安定性向上剤。
- タンパク質脱アミド酵素及びシクロデキストリングルカノトランスフェラーゼを含む、オートミルクの分散安定性向上剤。
- タンパク質脱アミド酵素及びシクロデキストリングルカノトランスフェラーゼを含む、黒豆ミルク、ピーナッツミルク、及びココナッツミルクからなる群より選択される植物性ミルクの溶解性向上剤。
- タンパク質脱アミド酵素及びシクロデキストリングルカノトランスフェラーゼを含む、ココナッツミルクの収率向上剤。
Priority Applications (4)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
CN202180074583.0A CN116367729A (zh) | 2020-11-05 | 2021-11-04 | 提高分散稳定性和/或溶解性的加工植物性奶的制造方法 |
EP21889228.9A EP4241571A1 (en) | 2020-11-05 | 2021-11-04 | Method for producing processed plant-based milk having increased dispersion stability and/or solubility |
JP2022560807A JPWO2022097675A1 (ja) | 2020-11-05 | 2021-11-04 | |
US18/251,846 US20240099322A1 (en) | 2020-11-05 | 2021-11-04 | Method for producing processed plant-based milk having increased dispersion stability and/or solubility |
Applications Claiming Priority (2)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
CN202011222558.6A CN114521593A (zh) | 2020-11-05 | 2020-11-05 | 提高分散稳定性和/或溶解性的加工植物性奶的制造方法 |
CN202011222558.6 | 2020-11-05 |
Publications (1)
Publication Number | Publication Date |
---|---|
WO2022097675A1 true WO2022097675A1 (ja) | 2022-05-12 |
Family
ID=81457094
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
PCT/JP2021/040557 WO2022097675A1 (ja) | 2020-11-05 | 2021-11-04 | 分散安定性及び/又は溶解性を高めた加工植物性ミルクの製造方法 |
Country Status (5)
Country | Link |
---|---|
US (1) | US20240099322A1 (ja) |
EP (1) | EP4241571A1 (ja) |
JP (1) | JPWO2022097675A1 (ja) |
CN (2) | CN114521593A (ja) |
WO (1) | WO2022097675A1 (ja) |
Cited By (3)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
WO2023214553A1 (ja) * | 2022-05-06 | 2023-11-09 | 天野エンザイム株式会社 | 植物性タンパク質含有液状組成物の食感改善剤 |
WO2024004848A1 (ja) * | 2022-06-28 | 2024-01-04 | 天野エンザイム株式会社 | 植物性飲食品の糖類低減用酵素剤 |
GB2625604A (en) * | 2022-12-20 | 2024-06-26 | Britvic Soft Drinks Ltd | Beverage formulation |
Citations (23)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JPH0698704A (ja) * | 1992-06-19 | 1994-04-12 | Rhone Poulenc Inc | 食品に使用するための食物繊維組成物 |
JPH11318373A (ja) * | 1998-05-15 | 1999-11-24 | Kao Corp | 食品の呈味改善方法 |
JP2000050887A (ja) | 1998-06-04 | 2000-02-22 | Amano Pharmaceut Co Ltd | 新規蛋白質脱アミド酵素、それをコ―ドする遺伝子、その製造法並びにその用途 |
JP2000513231A (ja) * | 1996-07-01 | 2000-10-10 | ノボ ノルディスク アクティーゼルスカブ | ベーキングにおけるデアミダーゼの利用 |
JP2001218590A (ja) | 1999-12-03 | 2001-08-14 | Amano Enzyme Inc | 新規蛋白質脱アミド酵素、それを生産する微生物、それをコードする遺伝子、その製造法及び用途 |
US6451361B1 (en) | 2001-05-29 | 2002-09-17 | Agri-Nutrients Technology Group, Inc. | Alkali metal magnesium phosphate hydrate buffering feed mineral |
WO2006075772A1 (ja) | 2005-01-13 | 2006-07-20 | Ajinomoto Co., Inc. | 乳製品及びその製造方法 |
JP2006230297A (ja) | 2005-02-25 | 2006-09-07 | Yakult Honsha Co Ltd | 黒豆豆乳飲料及びその製造方法 |
JP2008099676A (ja) | 2006-09-22 | 2008-05-01 | Sanei Gen Ffi Inc | ココナッツミルク含有飲食品及びその風味向上方法 |
JP2008283900A (ja) | 2007-05-17 | 2008-11-27 | Sakamoto Yakuhin Kogyo Co Ltd | 豆乳の分散安定剤 |
CN101991163A (zh) | 2009-08-10 | 2011-03-30 | 爱之味股份有限公司 | 具有治疗高脂血症、高血糖症和改善肠胃道的低聚糖燕麦饮品 |
JP2012034654A (ja) * | 2010-08-10 | 2012-02-23 | T Hasegawa Co Ltd | 飲食品の呈味改善剤 |
WO2012117879A1 (ja) * | 2011-02-28 | 2012-09-07 | 天野エンザイム株式会社 | 蒸しパンの品質改良剤及びその用途 |
JP2015159765A (ja) | 2014-02-27 | 2015-09-07 | マルサンアイ株式会社 | 豆乳の改質方法 |
JP2015216846A (ja) * | 2014-05-14 | 2015-12-07 | 長谷川香料株式会社 | 大豆食品の風味付与剤 |
JP2016502868A (ja) * | 2013-01-11 | 2016-02-01 | インポッシブル フーズ インコーポレイテッド | コアセルベートを含む、乳成分非含有チーズ代替品 |
JP2016506732A (ja) * | 2013-02-05 | 2016-03-07 | オートリー エービー | 液状のエンバクベース |
WO2017009100A1 (en) * | 2015-07-13 | 2017-01-19 | Dsm Ip Assets B.V. | Use of peptidylarginine deiminase to solubilize proteins or to reduce their foaming tendency |
WO2017154992A1 (ja) * | 2016-03-10 | 2017-09-14 | 味の素株式会社 | 植物蛋白質含有食品の製造方法 |
WO2019104971A1 (zh) | 2017-11-30 | 2019-06-06 | 深圳市聚尘科技有限公司 | 一种核桃乳饮料的制备工艺 |
WO2020171105A1 (ja) * | 2019-02-21 | 2020-08-27 | 天野エンザイム株式会社 | ナッツミルクの凝集防止 |
WO2020171106A1 (ja) * | 2019-02-21 | 2020-08-27 | 天野エンザイム株式会社 | 植物性ミルクの凝集防止 |
WO2020176469A1 (en) * | 2019-02-26 | 2020-09-03 | Amano Enzyme Usa Co., Ltd. | Stable protein formulations |
-
2020
- 2020-11-05 CN CN202011222558.6A patent/CN114521593A/zh active Pending
-
2021
- 2021-11-04 WO PCT/JP2021/040557 patent/WO2022097675A1/ja active Application Filing
- 2021-11-04 CN CN202180074583.0A patent/CN116367729A/zh active Pending
- 2021-11-04 EP EP21889228.9A patent/EP4241571A1/en active Pending
- 2021-11-04 JP JP2022560807A patent/JPWO2022097675A1/ja active Pending
- 2021-11-04 US US18/251,846 patent/US20240099322A1/en active Pending
Patent Citations (23)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JPH0698704A (ja) * | 1992-06-19 | 1994-04-12 | Rhone Poulenc Inc | 食品に使用するための食物繊維組成物 |
JP2000513231A (ja) * | 1996-07-01 | 2000-10-10 | ノボ ノルディスク アクティーゼルスカブ | ベーキングにおけるデアミダーゼの利用 |
JPH11318373A (ja) * | 1998-05-15 | 1999-11-24 | Kao Corp | 食品の呈味改善方法 |
JP2000050887A (ja) | 1998-06-04 | 2000-02-22 | Amano Pharmaceut Co Ltd | 新規蛋白質脱アミド酵素、それをコ―ドする遺伝子、その製造法並びにその用途 |
JP2001218590A (ja) | 1999-12-03 | 2001-08-14 | Amano Enzyme Inc | 新規蛋白質脱アミド酵素、それを生産する微生物、それをコードする遺伝子、その製造法及び用途 |
US6451361B1 (en) | 2001-05-29 | 2002-09-17 | Agri-Nutrients Technology Group, Inc. | Alkali metal magnesium phosphate hydrate buffering feed mineral |
WO2006075772A1 (ja) | 2005-01-13 | 2006-07-20 | Ajinomoto Co., Inc. | 乳製品及びその製造方法 |
JP2006230297A (ja) | 2005-02-25 | 2006-09-07 | Yakult Honsha Co Ltd | 黒豆豆乳飲料及びその製造方法 |
JP2008099676A (ja) | 2006-09-22 | 2008-05-01 | Sanei Gen Ffi Inc | ココナッツミルク含有飲食品及びその風味向上方法 |
JP2008283900A (ja) | 2007-05-17 | 2008-11-27 | Sakamoto Yakuhin Kogyo Co Ltd | 豆乳の分散安定剤 |
CN101991163A (zh) | 2009-08-10 | 2011-03-30 | 爱之味股份有限公司 | 具有治疗高脂血症、高血糖症和改善肠胃道的低聚糖燕麦饮品 |
JP2012034654A (ja) * | 2010-08-10 | 2012-02-23 | T Hasegawa Co Ltd | 飲食品の呈味改善剤 |
WO2012117879A1 (ja) * | 2011-02-28 | 2012-09-07 | 天野エンザイム株式会社 | 蒸しパンの品質改良剤及びその用途 |
JP2016502868A (ja) * | 2013-01-11 | 2016-02-01 | インポッシブル フーズ インコーポレイテッド | コアセルベートを含む、乳成分非含有チーズ代替品 |
JP2016506732A (ja) * | 2013-02-05 | 2016-03-07 | オートリー エービー | 液状のエンバクベース |
JP2015159765A (ja) | 2014-02-27 | 2015-09-07 | マルサンアイ株式会社 | 豆乳の改質方法 |
JP2015216846A (ja) * | 2014-05-14 | 2015-12-07 | 長谷川香料株式会社 | 大豆食品の風味付与剤 |
WO2017009100A1 (en) * | 2015-07-13 | 2017-01-19 | Dsm Ip Assets B.V. | Use of peptidylarginine deiminase to solubilize proteins or to reduce their foaming tendency |
WO2017154992A1 (ja) * | 2016-03-10 | 2017-09-14 | 味の素株式会社 | 植物蛋白質含有食品の製造方法 |
WO2019104971A1 (zh) | 2017-11-30 | 2019-06-06 | 深圳市聚尘科技有限公司 | 一种核桃乳饮料的制备工艺 |
WO2020171105A1 (ja) * | 2019-02-21 | 2020-08-27 | 天野エンザイム株式会社 | ナッツミルクの凝集防止 |
WO2020171106A1 (ja) * | 2019-02-21 | 2020-08-27 | 天野エンザイム株式会社 | 植物性ミルクの凝集防止 |
WO2020176469A1 (en) * | 2019-02-26 | 2020-09-03 | Amano Enzyme Usa Co., Ltd. | Stable protein formulations |
Non-Patent Citations (1)
Title |
---|
KATUTOSHI ARA, TADASHI YOSHIMATSU, MIYUKI OJIMA, SHUJI KAWAI, KAZUYOSHI OKUBO: "Effect of Enzymatic Treatment on Sensory Taste of Soymilk", JOURNAL OF THE JAPANESE SOCIETY FOR FOOD SCIENCE AND TECHNOLOGY, vol. 50, no. 1, 15 January 2003 (2003-01-15), JP , pages 13 - 21, XP009536429, ISSN: 1341-027X, DOI: 10.3136/nskkk.50.13 * |
Cited By (3)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
WO2023214553A1 (ja) * | 2022-05-06 | 2023-11-09 | 天野エンザイム株式会社 | 植物性タンパク質含有液状組成物の食感改善剤 |
WO2024004848A1 (ja) * | 2022-06-28 | 2024-01-04 | 天野エンザイム株式会社 | 植物性飲食品の糖類低減用酵素剤 |
GB2625604A (en) * | 2022-12-20 | 2024-06-26 | Britvic Soft Drinks Ltd | Beverage formulation |
Also Published As
Publication number | Publication date |
---|---|
EP4241571A1 (en) | 2023-09-13 |
JPWO2022097675A1 (ja) | 2022-05-12 |
CN116367729A (zh) | 2023-06-30 |
US20240099322A1 (en) | 2024-03-28 |
CN114521593A (zh) | 2022-05-24 |
Similar Documents
Publication | Publication Date | Title |
---|---|---|
WO2022097675A1 (ja) | 分散安定性及び/又は溶解性を高めた加工植物性ミルクの製造方法 | |
CN113826703B (zh) | 一种燕麦乳饮料的制备方法 | |
RU2616802C2 (ru) | Жидкая овсяная основа | |
EP0671883B1 (en) | Method for stabilizing rice bran and rice bran products | |
TWI441600B (zh) | 具有治療高血脂症、高血糖症及改善腸胃道機能的寡醣燕麥飲品及其三酵微分解製造方法 | |
WO2022071418A1 (ja) | 加工植物性ミルクの製造方法 | |
EP1309249A2 (en) | Soy protein product and process for its manufacture | |
JP5682697B1 (ja) | 植物性分離蛋白およびその製造法 | |
CA1198700A (en) | Enzyme for decomposition of a high molecular carbohydrate, the isolated high molecular carbohydrate, a method for selection of a microorganism producing such enzyme and a method for production of such enzyme | |
KR20200065928A (ko) | 귀리분말 제조방법 | |
WO2022092242A1 (ja) | 香りが増強された植物性タンパク質飲食品の加工物の製造方法 | |
WO2022092241A1 (ja) | 食感が向上した植物性タンパク質加工物の製造方法 | |
KR20170057448A (ko) | 면류의 제조방법 및 면용 분리 개량제 | |
JP2814300B2 (ja) | 酵素変性蛋白と方法 | |
WO2022059754A1 (ja) | 加工ひよこ豆ミルクの製造方法 | |
CA3121259A1 (en) | A process for preparation of cereal fractions | |
KR20040104509A (ko) | 비소화성 올리고당 함량이 낮은 대두 단백질 농축물 및그의 제조방법 | |
WO2022059755A1 (ja) | 加工ココナッツミルクの製造方法 | |
JPS6234379B2 (ja) | ||
WO2020226166A1 (ja) | 粉末状植物性蛋白素材の製造法 | |
FR2578396A1 (fr) | Produits alimentaires a base de lait de soja et leur procede de preparation | |
JP5118032B2 (ja) | γ−アミノ酪酸又はγ−アミノ酪酸含有組成物の製造方法 | |
WO2005055735A1 (ja) | 改良大豆7sたん白及びその製造法 | |
WO2024053745A1 (ja) | 加工植物性タンパク質含有組成物の製造方法 | |
JP2015119699A (ja) | 植物性分離蛋白およびその製造法 |
Legal Events
Date | Code | Title | Description |
---|---|---|---|
121 | Ep: the epo has been informed by wipo that ep was designated in this application |
Ref document number: 21889228 Country of ref document: EP Kind code of ref document: A1 |
|
ENP | Entry into the national phase |
Ref document number: 2022560807 Country of ref document: JP Kind code of ref document: A |
|
WWE | Wipo information: entry into national phase |
Ref document number: 18251846 Country of ref document: US |
|
NENP | Non-entry into the national phase |
Ref country code: DE |
|
ENP | Entry into the national phase |
Ref document number: 2021889228 Country of ref document: EP Effective date: 20230605 |