CN107459555A - Oligopeptides, dense taste imparting agent, flavoring and preparation method and application - Google Patents
Oligopeptides, dense taste imparting agent, flavoring and preparation method and application Download PDFInfo
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- CN107459555A CN107459555A CN201710210265.8A CN201710210265A CN107459555A CN 107459555 A CN107459555 A CN 107459555A CN 201710210265 A CN201710210265 A CN 201710210265A CN 107459555 A CN107459555 A CN 107459555A
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- glu
- abu
- oligopeptides
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- 235000019640 taste Nutrition 0.000 title claims abstract description 24
- 108010038807 Oligopeptides Proteins 0.000 title claims abstract description 17
- 102000015636 Oligopeptides Human genes 0.000 title claims abstract description 17
- 238000002360 preparation method Methods 0.000 title claims abstract description 12
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 claims abstract description 12
- QWCKQJZIFLGMSD-UHFFFAOYSA-N alpha-aminobutyric acid Chemical class CCC(N)C(O)=O QWCKQJZIFLGMSD-UHFFFAOYSA-N 0.000 claims abstract description 11
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims abstract description 11
- 108090000790 Enzymes Proteins 0.000 claims abstract description 10
- 102000004190 Enzymes Human genes 0.000 claims abstract description 10
- 239000003795 chemical substances by application Substances 0.000 claims abstract description 10
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 claims abstract description 9
- 102000009127 Glutaminase Human genes 0.000 claims abstract description 7
- 108010073324 Glutaminase Proteins 0.000 claims abstract description 7
- FUZOZPRKGAXGOB-UHFFFAOYSA-N gamma-Glu-Abu Chemical compound CCC(C(O)=O)NC(=O)CCC(N)C(O)=O FUZOZPRKGAXGOB-UHFFFAOYSA-N 0.000 claims abstract description 7
- 108090000279 Peptidyltransferases Proteins 0.000 claims abstract description 6
- 230000009849 deactivation Effects 0.000 claims abstract description 6
- 239000000243 solution Substances 0.000 claims description 38
- 238000006243 chemical reaction Methods 0.000 claims description 17
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 17
- 239000007788 liquid Substances 0.000 claims description 16
- 150000001413 amino acids Chemical group 0.000 claims description 8
- 239000007864 aqueous solution Substances 0.000 claims description 6
- 238000010828 elution Methods 0.000 claims description 5
- -1 gamma-glutamyl amine Chemical class 0.000 claims description 5
- 238000004128 high performance liquid chromatography Methods 0.000 claims description 5
- UPCDLBPYWXOCOK-UHFFFAOYSA-N N-L-gamma-glutamyl-S-methyl-L-cysteine Natural products CSCC(C(O)=O)NC(=O)CCC(N)C(O)=O UPCDLBPYWXOCOK-UHFFFAOYSA-N 0.000 claims description 4
- SNCKGJWJABDZHI-ZKWXMUAHSA-N gamma-Glu-Ile Chemical compound CC[C@H](C)[C@@H](C(O)=O)NC(=O)CC[C@H](N)C(O)=O SNCKGJWJABDZHI-ZKWXMUAHSA-N 0.000 claims description 4
- RQNSKRXMANOPQY-BQBZGAKWSA-N gamma-Glu-Met Chemical compound CSCC[C@@H](C(O)=O)NC(=O)CC[C@H](N)C(O)=O RQNSKRXMANOPQY-BQBZGAKWSA-N 0.000 claims description 4
- 230000033228 biological regulation Effects 0.000 claims description 3
- JHFNSBBHKSZXKB-VKHMYHEASA-N Asp-Gly Chemical compound OC(=O)C[C@H](N)C(=O)NCC(O)=O JHFNSBBHKSZXKB-VKHMYHEASA-N 0.000 claims description 2
- OOULJWDSSVOMHX-WDSKDSINSA-N Cys-Met Chemical compound CSCC[C@@H](C(O)=O)NC(=O)[C@@H](N)CS OOULJWDSSVOMHX-WDSKDSINSA-N 0.000 claims description 2
- XUJNEKJLAYXESH-UWTATZPHSA-N D-Cysteine Chemical compound SC[C@@H](N)C(O)=O XUJNEKJLAYXESH-UWTATZPHSA-N 0.000 claims description 2
- FCQBDQYWNGUTPD-BQBZGAKWSA-N Gamma glutamyl ornithine Chemical compound NCCC[C@@H](C(O)=O)NC(=O)[C@@H](N)CCC(O)=O FCQBDQYWNGUTPD-BQBZGAKWSA-N 0.000 claims description 2
- SQBNIUOYNOKDTI-WHFBIAKZSA-N Gamma-glutamyl-Serine Chemical compound OC(=O)[C@@H](N)CCC(=O)N[C@@H](CO)C(O)=O SQBNIUOYNOKDTI-WHFBIAKZSA-N 0.000 claims description 2
- PABVKUJVLNMOJP-WHFBIAKZSA-N Glu-Cys Chemical compound OC(=O)CC[C@H](N)C(=O)N[C@@H](CS)C(O)=O PABVKUJVLNMOJP-WHFBIAKZSA-N 0.000 claims description 2
- MFBYPDKTAJXHNI-VKHMYHEASA-N Gly-Cys Chemical compound [NH3+]CC(=O)N[C@@H](CS)C([O-])=O MFBYPDKTAJXHNI-VKHMYHEASA-N 0.000 claims description 2
- MYFMARDICOWMQP-UHFFFAOYSA-N L-L-gamma-Glutamylleucine Natural products CC(C)CC(C(O)=O)NC(=O)CCC(N)C(O)=O MYFMARDICOWMQP-UHFFFAOYSA-N 0.000 claims description 2
- AQAKHZVPOOGUCK-UHFFFAOYSA-N L-L-gamma-Glutamylvaline Natural products CC(C)C(C(O)=O)NC(=O)CCC(N)C(O)=O AQAKHZVPOOGUCK-UHFFFAOYSA-N 0.000 claims description 2
- ZUKPVRWZDMRIEO-VKHMYHEASA-N L-cysteinylglycine Chemical compound SC[C@H]([NH3+])C(=O)NCC([O-])=O ZUKPVRWZDMRIEO-VKHMYHEASA-N 0.000 claims description 2
- RITKHVBHSGLULN-WHFBIAKZSA-N L-gamma-glutamyl-L-cysteine Chemical compound OC(=O)[C@@H](N)CCC(=O)N[C@@H](CS)C(O)=O RITKHVBHSGLULN-WHFBIAKZSA-N 0.000 claims description 2
- ACIJGUBIMXQCMF-UHFFFAOYSA-N N-L-gamma-glutamyl-glycine Natural products OC(=O)C(N)CCC(=O)NCC(O)=O ACIJGUBIMXQCMF-UHFFFAOYSA-N 0.000 claims description 2
- 108010047857 aspartylglycine Proteins 0.000 claims description 2
- 108010016616 cysteinylglycine Proteins 0.000 claims description 2
- WQXXXVRAFAKQJM-WHFBIAKZSA-N gamma-Glu-Ala Chemical compound OC(=O)[C@H](C)NC(=O)CC[C@H](N)C(O)=O WQXXXVRAFAKQJM-WHFBIAKZSA-N 0.000 claims description 2
- ACIJGUBIMXQCMF-BYPYZUCNSA-N gamma-Glu-Gly Chemical compound OC(=O)[C@@H](N)CCC(=O)NCC(O)=O ACIJGUBIMXQCMF-BYPYZUCNSA-N 0.000 claims description 2
- MYFMARDICOWMQP-YUMQZZPRSA-N gamma-Glu-Leu Chemical compound CC(C)C[C@@H](C(O)=O)NC(=O)CC[C@H](N)C(O)=O MYFMARDICOWMQP-YUMQZZPRSA-N 0.000 claims description 2
- AQAKHZVPOOGUCK-XPUUQOCRSA-N gamma-Glu-Val Chemical compound CC(C)[C@@H](C(O)=O)NC(=O)CC[C@H](N)C(O)=O AQAKHZVPOOGUCK-XPUUQOCRSA-N 0.000 claims description 2
- BBAYFIRFVORJLJ-UHFFFAOYSA-N gamma-Glutamyl-alpha-ornitine Natural products NCCCC(C(O)=O)NC(=O)CCC(N)C(O)=O BBAYFIRFVORJLJ-UHFFFAOYSA-N 0.000 claims description 2
- 108010064169 gamma-glutamyl-leucine Proteins 0.000 claims description 2
- 108010068906 gamma-glutamylcysteine Proteins 0.000 claims description 2
- 108010067681 gamma-glutamylornithine Proteins 0.000 claims description 2
- GWNXFCYUJXASDX-UHFFFAOYSA-N gamma-glutamylthreonine Chemical compound CC(O)C(C(O)=O)NC(=O)CCC(N)C(O)=O GWNXFCYUJXASDX-UHFFFAOYSA-N 0.000 claims description 2
- 108010032395 gamma-glutamylvaline Proteins 0.000 claims description 2
- DVCSNHXRZUVYAM-BQBZGAKWSA-N leu-asp Chemical compound CC(C)C[C@H](N)C(=O)N[C@H](C(O)=O)CC(O)=O DVCSNHXRZUVYAM-BQBZGAKWSA-N 0.000 claims description 2
- GOJUJUVQIVIZAV-UHFFFAOYSA-N 2-amino-4,6-dichloropyrimidine-5-carbaldehyde Chemical group NC1=NC(Cl)=C(C=O)C(Cl)=N1 GOJUJUVQIVIZAV-UHFFFAOYSA-N 0.000 claims 1
- 239000002253 acid Substances 0.000 claims 1
- 239000012295 chemical reaction liquid Substances 0.000 claims 1
- 150000002825 nitriles Chemical class 0.000 claims 1
- 235000013305 food Nutrition 0.000 abstract description 2
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 abstract 3
- WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 abstract 2
- 239000000796 flavoring agent Substances 0.000 description 21
- 235000019634 flavors Nutrition 0.000 description 21
- 125000002642 gamma-glutamyl group Chemical group 0.000 description 12
- 238000011156 evaluation Methods 0.000 description 10
- 230000001953 sensory effect Effects 0.000 description 10
- 239000012071 phase Substances 0.000 description 8
- 235000014347 soups Nutrition 0.000 description 8
- 241000287828 Gallus gallus Species 0.000 description 7
- 230000000694 effects Effects 0.000 description 7
- 238000004458 analytical method Methods 0.000 description 6
- 239000000463 material Substances 0.000 description 6
- 239000000523 sample Substances 0.000 description 6
- XBJFCYDKBDVADW-UHFFFAOYSA-N acetonitrile;formic acid Chemical compound CC#N.OC=O XBJFCYDKBDVADW-UHFFFAOYSA-N 0.000 description 5
- 239000000203 mixture Substances 0.000 description 5
- 235000019605 sweet taste sensations Nutrition 0.000 description 5
- 150000001875 compounds Chemical class 0.000 description 4
- 238000000855 fermentation Methods 0.000 description 4
- 230000004151 fermentation Effects 0.000 description 4
- JVTAAEKCZFNVCJ-UHFFFAOYSA-N lactic acid Chemical compound CC(O)C(O)=O JVTAAEKCZFNVCJ-UHFFFAOYSA-N 0.000 description 4
- 235000013555 soy sauce Nutrition 0.000 description 4
- 102100035650 Extracellular calcium-sensing receptor Human genes 0.000 description 3
- 101710159793 Extracellular calcium-sensing receptor Proteins 0.000 description 3
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 3
- 235000019606 astringent taste Nutrition 0.000 description 3
- 238000000034 method Methods 0.000 description 3
- LPUQAYUQRXPFSQ-DFWYDOINSA-M monosodium L-glutamate Chemical class [Na+].[O-]C(=O)[C@@H](N)CCC(O)=O LPUQAYUQRXPFSQ-DFWYDOINSA-M 0.000 description 3
- 235000013923 monosodium glutamate Nutrition 0.000 description 3
- 150000003839 salts Chemical class 0.000 description 3
- 239000011780 sodium chloride Substances 0.000 description 3
- 241000193744 Bacillus amyloliquefaciens Species 0.000 description 2
- 244000046052 Phaseolus vulgaris Species 0.000 description 2
- 235000010627 Phaseolus vulgaris Nutrition 0.000 description 2
- 238000010811 Ultra-Performance Liquid Chromatography-Tandem Mass Spectrometry Methods 0.000 description 2
- 240000008042 Zea mays Species 0.000 description 2
- 235000005824 Zea mays ssp. parviglumis Nutrition 0.000 description 2
- 235000002017 Zea mays subsp mays Nutrition 0.000 description 2
- 239000000556 agonist Substances 0.000 description 2
- 239000007795 chemical reaction product Substances 0.000 description 2
- 235000005822 corn Nutrition 0.000 description 2
- 230000003247 decreasing effect Effects 0.000 description 2
- 238000000132 electrospray ionisation Methods 0.000 description 2
- 238000005516 engineering process Methods 0.000 description 2
- 238000002474 experimental method Methods 0.000 description 2
- 235000013312 flour Nutrition 0.000 description 2
- 239000012530 fluid Substances 0.000 description 2
- RWSXRVCMGQZWBV-WDSKDSINSA-N glutathione Chemical compound OC(=O)[C@@H](N)CCC(=O)N[C@@H](CS)C(=O)NCC(O)=O RWSXRVCMGQZWBV-WDSKDSINSA-N 0.000 description 2
- 238000000703 high-speed centrifugation Methods 0.000 description 2
- 239000002054 inoculum Substances 0.000 description 2
- 239000004310 lactic acid Substances 0.000 description 2
- 235000014655 lactic acid Nutrition 0.000 description 2
- 239000007791 liquid phase Substances 0.000 description 2
- 239000006199 nebulizer Substances 0.000 description 2
- 230000035790 physiological processes and functions Effects 0.000 description 2
- 238000004451 qualitative analysis Methods 0.000 description 2
- 230000000638 stimulation Effects 0.000 description 2
- 239000000126 substance Substances 0.000 description 2
- 239000006228 supernatant Substances 0.000 description 2
- 235000012976 tarts Nutrition 0.000 description 2
- 238000012360 testing method Methods 0.000 description 2
- 235000015099 wheat brans Nutrition 0.000 description 2
- 244000063299 Bacillus subtilis Species 0.000 description 1
- 241000196324 Embryophyta Species 0.000 description 1
- 101710159104 Flavor peptide Proteins 0.000 description 1
- 108010024636 Glutathione Proteins 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- VVLXCWVSSLFQDS-UHFFFAOYSA-N N-L-gamma-glutamyl-L-tyrosine Natural products OC(=O)C(N)CCC(=O)NC(C(O)=O)CC1=CC=C(O)C=C1 VVLXCWVSSLFQDS-UHFFFAOYSA-N 0.000 description 1
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 1
- 229910021529 ammonia Inorganic materials 0.000 description 1
- QGZKDVFQNNGYKY-UHFFFAOYSA-N ammonia Natural products N QGZKDVFQNNGYKY-UHFFFAOYSA-N 0.000 description 1
- 230000001093 anti-cancer Effects 0.000 description 1
- 235000019632 basic taste sensations Nutrition 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 235000019658 bitter taste Nutrition 0.000 description 1
- 239000012496 blank sample Substances 0.000 description 1
- 238000009835 boiling Methods 0.000 description 1
- 210000000481 breast Anatomy 0.000 description 1
- 230000003197 catalytic effect Effects 0.000 description 1
- 150000001768 cations Chemical class 0.000 description 1
- 230000001413 cellular effect Effects 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 238000010668 complexation reaction Methods 0.000 description 1
- 230000007423 decrease Effects 0.000 description 1
- 230000007812 deficiency Effects 0.000 description 1
- 238000001035 drying Methods 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 235000021107 fermented food Nutrition 0.000 description 1
- 238000004108 freeze drying Methods 0.000 description 1
- 238000007710 freezing Methods 0.000 description 1
- 230000008014 freezing Effects 0.000 description 1
- OWQDWQKWSLFFFR-WDSKDSINSA-N gamma-Glu-Glu Chemical compound OC(=O)[C@@H](N)CCC(=O)N[C@H](C(O)=O)CCC(O)=O OWQDWQKWSLFFFR-WDSKDSINSA-N 0.000 description 1
- VVLXCWVSSLFQDS-QWRGUYRKSA-N gamma-Glu-Tyr Chemical compound OC(=O)[C@@H](N)CCC(=O)N[C@H](C(O)=O)CC1=CC=C(O)C=C1 VVLXCWVSSLFQDS-QWRGUYRKSA-N 0.000 description 1
- 229960003180 glutathione Drugs 0.000 description 1
- PCHJSUWPFVWCPO-UHFFFAOYSA-N gold Chemical compound [Au] PCHJSUWPFVWCPO-UHFFFAOYSA-N 0.000 description 1
- 239000010931 gold Substances 0.000 description 1
- 229910052737 gold Inorganic materials 0.000 description 1
- 239000004519 grease Substances 0.000 description 1
- 235000019668 heartiness Nutrition 0.000 description 1
- 229910001385 heavy metal Inorganic materials 0.000 description 1
- 230000003993 interaction Effects 0.000 description 1
- 150000002500 ions Chemical class 0.000 description 1
- 230000002503 metabolic effect Effects 0.000 description 1
- 229910021645 metal ion Inorganic materials 0.000 description 1
- 244000005700 microbiome Species 0.000 description 1
- 239000000178 monomer Substances 0.000 description 1
- 239000004223 monosodium glutamate Substances 0.000 description 1
- 235000012149 noodles Nutrition 0.000 description 1
- 231100000614 poison Toxicity 0.000 description 1
- 238000004321 preservation Methods 0.000 description 1
- 239000000047 product Substances 0.000 description 1
- 230000035807 sensation Effects 0.000 description 1
- 235000019615 sensations Nutrition 0.000 description 1
- 210000000697 sensory organ Anatomy 0.000 description 1
- 230000002195 synergetic effect Effects 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 238000004885 tandem mass spectrometry Methods 0.000 description 1
- 239000003440 toxic substance Substances 0.000 description 1
- 238000004704 ultra performance liquid chromatography Methods 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K5/00—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof
- C07K5/04—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof containing only normal peptide links
- C07K5/10—Tetrapeptides
- C07K5/1021—Tetrapeptides with the first amino acid being acidic
-
- 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
- A23L27/00—Spices; Flavouring agents or condiments; Artificial sweetening agents; Table salts; Dietetic salt substitutes; Preparation or treatment thereof
- A23L27/20—Synthetic spices, flavouring agents or condiments
- A23L27/21—Synthetic spices, flavouring agents or condiments containing amino acids
- A23L27/22—Synthetic spices, flavouring agents or condiments containing amino acids containing glutamic acids
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23V—INDEXING SCHEME RELATING TO FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES AND LACTIC OR PROPIONIC ACID BACTERIA USED IN FOODSTUFFS OR FOOD PREPARATION
- A23V2200/00—Function of food ingredients
Abstract
The invention discloses oligopeptides, dense taste imparting agent, flavoring and preparation method and application.The oligopeptides γ Glu γ Glu γ Glu Abu of the present invention have good stability, and the savoury of food particularly flavouring is remarkably improved under 60 100mg/kg concentration.Specifically preparation process is：It is soluble in water after glutamine is mixed with 2 aminobutyric acids, add solution quality 0.001 0.4%（w/w）Glutaminase or γ-glutamate transpeptidase, the pH to 7.0 10.0 of solution is adjusted with 10 mol/l sodium hydroxide solution, is reacted 3 12 hours at 25 50 DEG C, afterwards between 4 mol/L hydrochloric acid readjustment pH to 7 ~ 8,90 DEG C of min of enzyme deactivation 10.
Description
Technical field
The present invention relates to peptide with flavor effect and preparation method thereof, and in particular to has the γ-Glutamyl Peptide of savoury
And preparation method thereof.
Background technology
γ-Glutamyl Peptide deposit extensively with a variety of animals and plants and fermented food, be a kind of safety is natural, the food of safety into
Point.Its primary structure of common glutathione is γ-Glu-Cys-Gly, is a kind of typical γ-Glutamyl Peptide.Modern study
Show that metabolic activity and the physiological function of γ-Glutamyl Peptide and organism are relevant, most of γ-Glutamyl Peptide has calm in addition
Depressurize, fatigue of releiving, anticancer removing toxic substances, complexation heavy metal ion, maintain cellular metal ions balance etc. physiological function.
In recent years, it has been found that γ-Glutamyl Peptide also has stronger flavor characteristic.Japanese aginomoto strain formula meeting in 2002
Society is disclosed by exploring the diversified compound with CaSR agonist activities, finds to assign with more excellent dense taste
Effect, the dense taste imparting effect particularly with preceding taste type, and has excellent stability, can simplicity and produce at low cost
The material for being capable of imparting body taste, there is provided the dense taste imparting agent comprising the material, and with other there is CaSR to swash the material
The combinations of substances of dynamic agent activity uses the compound dense taste imparting agent formed.Include γ-Glu-Abu (L- gamma-glutamyls-L-2-2-
Aminobutyric acid) dense taste imparting agent, and the material with other there is the combinations of substances of CaSR agonist activities to use to form
Compound dense taste imparting agent (number of patent application 201080024054.1).
Most of γ-Glutamyl Peptide under low consistency conditions has slight astringent taste, with the raising of concentration, γ-paddy ammonia
Acyl peptide starts that primary taste is presented.Such as γ-Glu-Glu have delicate flavour, γ-Glu-tyr bitter taste when concentration is 10mmol/L
Threshold value is twice of its astringent taste threshold value.In delicate flavour solution, γ-Glutamyl Peptide has savoury, and threshold value is also being decreased obviously.With
People further appreciate that scholar has found that γ-Glutamyl Peptide has the feature of savoury material to flavor peptide：1. base in aqueous
This insipidness or only slight taste (astringent taste or tart flavour)；2. increasing can be cooperateed with other taste compounds in system
Effect acts on, and is added in the solution system containing delicate flavour material, will not change the basic taste sensation intensity of solution, but can coordinate each
Kind taste, dramatically increase dense sense (kokumi)；3. compared with pure water solution, threshold value is decreased obviously in delicate flavour solution.
Table 1 has reported γ-Glutamyl Peptide flavor characteristic and threshold value list
So far, there is not yet γ-Glu- γ-Glu- γ-Glu-Abu have the report of dense taste.
The content of the invention
It is an object of the invention to overcome deficiencies of the prior art, there is provided one kind utilizes glutamine enzymatic synthesis
The preparation method of γ-Glutamyl Peptide.
The purpose of the present invention is achieved through the following technical solutions.
A kind of oligopeptides, its amino acid sequence are γ-Glu- γ-Glu- γ-Glu-Abu.
Dense taste imparting agent provided by the invention, combined by the oligopeptides and more than one following peptide：γ-Glu-
X-Gly (X represents amino acid or amino acid derivativges), γ-Glu-Val-Y (Y represents amino acid or amino acid derivativges), γ-
Glu-Abu、γ-Glu-Ala、γ-Glu-Gly、γ-Glu-Cys、γ-Glu-Met、γ-Glu-Thr、γ-Glu-Val、γ-
Glu-Orn、Asp-Gly、Cys-Gly、Cys-Met、Glu-Cys、Gly-Cys、Leu-Asp、D-Cys、γ-Glu-Met(O)、
γ-Glu-γ-Glu-Val、γ-Glu-Val-NH2、γ-Glu-Val-ol、γ-Glu-Ser、γ-Glu-Tau、γ-Glu-
Cys (S-Me) (O), γ-Glu-Leu, γ-Glu-Ile, γ-Glu-t-Leu and γ-Glu-Cys (S-Me).
A kind of flavoring containing the oligopeptides, it contains γ-Glu- γ-Glu- γ-Glu- more than 60 weight mg/kg
Abu。
A kind of flavoring containing the oligopeptides, contain more than 60 weight mg/kg
γ-Glu-γ-Glu-γ-Glu-Abu。
A kind of flavoring containing the oligopeptides, contain more than 500 weight mg/kg
γ-Glu-γ-Glu-γ-Glu-Abu。
The preparation method of the oligopeptides, it is specifically：Glutamine and free 2-amino-butyric acid, mol ratio 1-2:1, it is dissolved in
Solution is obtained in water, regulation reaction pH is 7.0-10.0, adds glutaminase or gamma-glutamyl amine transpeptidase 0.02-1% (w/
W), reacted 3-12 hours at 25-50 DEG C, afterwards between 4mol/L hydrochloric acid readjustment pH to 7~8,90 DEG C of enzyme deactivation 10min, obtain richness
The γ of-the Glu- containing γ-Glu-Abu reaction solution.Using 5 μm of 4.6x250mm analytical columns of XSelect HSS T3, mobile phase A liquid
For 0.1% (V/V) formic acid-aqueous solution；Mobile phase B liquid is 0.1% (V/V) formic acid-acetonitrile solution, and column temperature is 40 DEG C, and flow velocity is
1mL/min, the μ L of sample size 10 of reaction solution, gradient elution is carried out to reaction solution using high performance liquid chromatography, the 2nd peak is widow
Peptide γ-Glu- γ-Glu-Abu.
Further, the concentration of the solution GLN and free 2-amino-butyric acid is in 400-1000mmol/L.
The present invention compared with prior art, has the following advantages that：
1) present invention firstly discloses γ-Glu- γ-Glu- γ-Glu-Abu to have savoury characteristic.
2) make public for the first time and utilize glutaminase or gamma-glutamyl amine transpeptidase catalytic preparation of gamma-Glu- γ-Glu-
γ-Glu-Abu。
Brief description of the drawings
Fig. 1 is that 2-amino-butyric acid adds contrast difference figure of the glutaminase to flavor characteristic with glutamine mixture；
Fig. 2 is the liquid chromatogram of mixture after example 1 reacts；
Fig. 3 is γ-Glu- γ-Glu- γ-Glu-Abu flavor specificity analysis；
Fig. 4 is γ-Glu- γ-Glu- γ-Glu-Abu second order mses figure；
Fig. 5 a, Fig. 5 b are flavor synergistic effects of the γ-Glu- γ-Glu-Abu to soy sauce and chicken soup respectively.
Embodiment
Specifically implement to make further citing, but implementation of the invention and guarantor to the present invention below in conjunction with accompanying drawing and example
Protect not limited to this.
Embodiment 1
400mM glutamine and 400mM2- aminobutyric acids are dissolved in 100g water, the pH value of solution is adjusted to 10.0, adds
Enter 0.4g glutaminases (Japanese Tian Ye Co., Ltd., vigor 100GTU/g), react 12h respectively at 25 DEG C, after use 4mol/
After L hydrochloric acid readjustment pH to 7.0,90 DEG C of enzyme deactivation 10min, sensory evaluation is carried out to product flavor characteristic, flavor is special before and after it reacts
Property such as Fig. 1.
As seen from Figure 1, after reaction terminates, savoury, delicate flavour and the saline taste of reaction solution all significantly improve, and sweet taste significantly drops
It is low.Glutamine is in sweet taste, and solution GLN content reduces after reaction, causes the sweet taste of reaction solution to weaken.
HPLC liquid phases carry out quantitative flavor analysis to reaction product：Analytical column：XSelect HSS T3 5μm 4.6x
250mm；Mobile phase：A liquid：0.1% (V/V) formic acid-aqueous solution；B liquid：0.1% (V/V) formic acid-acetonitrile solution；Column temperature：40 DEG C,
Flow velocity：1mL/min.The μ L of sample size 10.Its liquid chromatogram is shown in Fig. 2, and it is as shown in table 2 that mobile phase carries out graded elution.
Table 2
| Time/min | 0 | 5 | 10 | 15 | 20 |
| A/% | 90 | 80 | 20 | 90 | 90 |
In Fig. 2, compareed with standard items, empirical tests, appearance time be peak 3 corresponding to 5.577 be not γ-Glu- γ-
Glu- γ-Glu-Abu, are collected to peak 3, and freeze-drying obtains γ-Glu- γ-Glu- γ-Glu-Abu monomer.Weigh
0.01g γ-Glu- γ-Glu- γ-Glu-Abu, and 0.5g salt and 0.3g monosodium glutamates, are dissolved in 100g water, and and blank
Sample (0.5g salt and 0.3g monosodium glutamates are dissolved in 100g water) carries out sensory evaluation.Sensory evaluation experiment has sense organ to comment by 30-41 year
7 males of valency experience and 9 women compositions, Analyses Methods for Sensory Evaluation Results are shown in Fig. 3.
As seen from Figure 3,0.01g γ-Glu- γ-Glu- γ-Glu-Abu sample is added compared with the control, solution
Delicate flavour and saline taste significantly improve.
UPLC-MS/MS carries out qualitative analysis to reaction product：Including：An Agilent 1290 series UPLC
System (Agilent Technologies) is used for each γ-Glu-peptides, with an elec-trospray
Ionization (ESI) mass spectrometer system (Q-TOF MS/MS, Bruker Daltonics) carries out qualitative analysis.Chromatographic column is：
Agilent ZORBAX RRHD SB-C18(2.1x50mm,1.8μm).Sample size is 5 μ L.Liquid-phase condition is：Solution A is
0.1% formic acid-the aqueous solution, and solution B are 0.1% formic acid-acetonitrile solution, and gradient elution program is：0-10%B, 0-5.0min；
10-15%B, 5.0-10.0min；Then 100%B, 10.0-12.0min.MS conditions：Ionization (ionization)：Cation
Pattern；Drying gas (dry gas)：10L/min at 350 DEG C；Nebulizer (nebulizer pressure)：25psig；
Fragmentor (capillary voltage)：30V.UPLC-MS/MS analyses, its testing result such as Fig. 4 are carried out to peak 3.
As shown in Figure 4, its primary structure is γ-Glu- γ-Glu- γ-Glu-Abu.
Embodiment 2
Fresh Grade Breast is put into 15 times of weight clear water, 60min is incubated after boiling, freezing dispels noodle soup grease, filters to obtain chicken
Soup.The salt of addition chicken soup 0.5% (% is to account for chicken soup mass percent, similarly hereinafter), 0.01% γ-Glu- γ-Glu- γ of addition-
Glu-Abu evaluates its flavor characteristic variations in chicken soup.Sensory evaluation is tested by 30-41 year 7 men for having sensory evaluation experience
Property and 9 women composition, Analyses Methods for Sensory Evaluation Results shows, adds 0.01% γ-Glu- γ-Glu- γ-Glu- γ-Abu chicken
Sensation, delicate flavour, sweet taste and the savoury of the chicken soup of soup are significantly increased, and see Fig. 5 b.
Soy sauce is commercially available extra large day Gold Label soy, adds 0.01% (mass percent, similarly hereinafter) γ-Glu- γ-Glu- respectively
γ-Glu-Abu are in soy sauce.Sensory evaluation experiment is made up of by 30-41 year 7 males and 9 women of sensory evaluation experience,
Analyses Methods for Sensory Evaluation Results shows that the saline taste for adding 0.01% γ-Glu- γ-Glu- γ-Glu- γ-Abu soy sauce decreases,
But delicate flavour, sweet taste and savoury increase are obvious, see Fig. 5 a.
Embodiment 3
By bacillus amyloliquefaciens (Bacillus amyloliquefaciens) SWJS22 (Chinese microorganism strain preservations
Administration committee's common micro-organisms center, deposit number CGMCCNo.8425) fermentation medium is inoculated in 1% inoculum concentration
(composition of fermentation medium is：4% dregs of beans, 2% wheat bran, 2% corn flour) in, 37~39 DEG C of fermented and cultured 30h.By zymotic fluid
In 4 DEG C, high speed centrifugation 10min under the conditions of 10000r/min, supernatant, i.e. glutaminase crude enzyme liquid are filtered to obtain.
600mM glutamine and 300mM 2-amino-butyric acids are dissolved in 100g water, the pH value of solution is adjusted to 7.0, adds
Enter 1g crude enzyme liquids, after 50 DEG C are reacted 3h respectively, after adjusting back pH to 7.0 with 4mol/L hydrochloric acid, 90 DEG C of enzyme deactivation 10min, obtain richness
γ-Glu- the γ of-the Glu- containing γ-Glu-Abu reaction solution.Using 5 μm of 4.6x250mm analytical columns of XSelect HSS T3, stream
Dynamic phase A liquid is 0.1% (V/V) formic acid-aqueous solution；Mobile phase B liquid is 0.1% (V/V) formic acid-acetonitrile solution, and column temperature is 40 DEG C,
Flow velocity is 1mL/min, the μ L of sample size 10 of reaction solution, and gradient elution, the 3rd peak are carried out to reaction solution using high performance liquid chromatography
As oligopeptides γ-Glu- γ-Glu- γ-Glu-Abu.
Embodiment 4
With 1% inoculum concentration Bacillus subtillis ATCC 6633 is inoculated in into fermentation medium, and (fermentation medium forms
For：4% dregs of beans, 2% wheat bran, 2% corn flour) in, 37~39 DEG C of fermented and cultured 48h.By zymotic fluid in 4 DEG C, 10000r/min
Under the conditions of high speed centrifugation 10min, filter to obtain supernatant, i.e. gamma-glutamyl amine transpeptidase crude enzyme liquid.
600mM glutamine and 400mM2- aminobutyric acids are dissolved in 100g water, respectively the pH value of regulation solution to 8.0,
1g gamma-glutamyl amine transpeptidase crude enzyme liquids are added, after 40 DEG C are reacted 6h respectively, after adjusting back pH to 7.0 with 4mol/L hydrochloric acid, 90
DEG C enzyme deactivation 10min, obtain the reaction solution rich in γ-Glu- γ-Glu- γ-Glu-Abu.Using the μ of XSelect HSS T3 5
M4.6x250mm analytical columns, mobile phase A liquid are 0.1% (V/V) formic acid-aqueous solution；Mobile phase B liquid be 0.1% (V/V) formic acid-
Acetonitrile solution, column temperature are 40 DEG C, flow velocity 1mL/min, the μ L of sample size 10 of reaction solution, using high performance liquid chromatography to reaction solution
Gradient elution is carried out, the 3rd peak is oligopeptides γ-Glu- γ-Glu- γ-Glu-Abu.
Table 3
a:Tart flavour (mg/L), b:Savoury solution ph is transferred to 6.5
Table 3 shows that stimulation of the γ-Glutamyl Peptide in different solutions is in taste threshold value, and % is the mass percent for accounting for water.By
Table 3 is visible, and γ-Glu- γ-Glu- γ-Glu-Abu and lactic acid have stronger flavor interaction, add monosodium glutamate and lactic acid can be bright
The aobvious stimulation for reducing γ-Glu- γ-Glu- γ-Glu-Abu is in taste threshold value.
Claims (8)
1. a kind of oligopeptides, it is characterised in that its amino acid sequence is γ-Glu- γ-Glu- γ-Glu-Abu.
2. dense taste imparting agent, it is characterised in that oligopeptides and more than one following peptide combine as described in claim 1：
γ-Glu-X-Gly、γ-Glu-Val-Y、γ-Glu-Abu、γ-Glu-Ala、γ-Glu-Gly、γ-Glu-Cys、γ-Glu-
Met、γ-Glu-Thr、γ-Glu-Val、γ-Glu-Orn、Asp-Gly、Cys-Gly、Cys-Met、Glu-Cys、Gly-Cys、
Leu-Asp、D-Cys、γ-Glu-Met(O)、γ-Glu-γ-Glu-Val、γ-Glu-Val-NH2、γ-Glu-Val-ol、
γ-Glu-Ser、γ-Glu-Tau、γ-Glu-Cys(S-Me)(O)、γ-Glu-Leu、γ-Glu-Ile、γ-Glu-t-Leu
With γ-Glu-Cys (S-Me)；X, Y represents amino acid or amino acid derivativges.
A kind of 3. flavoring containing oligopeptides described in claim 1, it is characterised in that the γ containing more than 60 weight mg/kg-
Glu-γ-Glu-γ-Glu-Abu。
4. a kind of flavoring containing dense taste imparting agent described in claim 2, it is characterised in that contain more than 60 weight mg/kg
γ-Glu- γ-Glu- γ-Glu-Abu.
5. the flavoring according to claim 3 or 4, it is characterised in that the γ-Glu- γ containing more than 500 weight mg/kg-
Glu-γ-Glu-Abu。
6. the preparation method of oligopeptides described in claim 1, it is characterised in that glutamine and free 2-amino-butyric acid, mol ratio are
1-2:1, soluble in water to obtain solution, regulation reaction pH is 7.0-10.0, adds glutaminase or gamma-glutamyl amine transpeptidase
0.02-1%（w/w）, reacted 3-12 hours at 25-50 DEG C, between the rear pH to 7 ~ 8 with 4 mol/L hydrochloric acid readjustment, 90 DEG C of enzyme deactivations 10
Min, obtain oligopeptides-Glu- containing γ γ-Glu- γ-Glu-Abu reaction solutions.
7. preparation method according to claim 6, it is characterised in that：Using 5 μm of 4.6x of XSelect HSS T3
250mm analytical columns, mobile phase A liquid are 0.1%（V/V）Formic acid-the aqueous solution；Mobile phase B liquid is 0.1% (V/V) formic acid-second
Nitrile solution, column temperature are 40 DEG C, and flow velocity is 1 mL/min, the μ L of sample size 10 of reaction solution, using high performance liquid chromatography to reaction
Liquid carries out gradient elution, and the 3rd peak is oligopeptides γ-Glu- γ-Glu- γ-Glu-Abu.
8. preparation method according to claim 6, it is characterised in that the solution GLN and free 2- amino fourth
The concentration of acid is in 400-1000mmol/L.
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| US11659854B2 (en) | 2017-07-13 | 2023-05-30 | Fuji Oil Holdings Inc. | Method for imparting body taste to food |
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| CN100999746A (en) * | 2006-12-19 | 2007-07-18 | 南京工业大学 | Process of synthesizing gamma-D-glutamine acyl L-tryptophane by enzyme method |
| CN102481006A (en) * | 2009-04-01 | 2012-05-30 | 味之素株式会社 | Use of peptide for imparting body taste |
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2017
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| CN100999746A (en) * | 2006-12-19 | 2007-07-18 | 南京工业大学 | Process of synthesizing gamma-D-glutamine acyl L-tryptophane by enzyme method |
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| US11659854B2 (en) | 2017-07-13 | 2023-05-30 | Fuji Oil Holdings Inc. | Method for imparting body taste to food |
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