GB2046567A - Ensilaging vegetable matter - Google Patents
Ensilaging vegetable matter Download PDFInfo
- Publication number
- GB2046567A GB2046567A GB8004578A GB8004578A GB2046567A GB 2046567 A GB2046567 A GB 2046567A GB 8004578 A GB8004578 A GB 8004578A GB 8004578 A GB8004578 A GB 8004578A GB 2046567 A GB2046567 A GB 2046567A
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- Prior art keywords
- bacteria
- activity
- enzymes
- glucides
- complex
- Prior art date
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- Granted
Links
- 235000013311 vegetables Nutrition 0.000 title claims description 50
- 241000894006 Bacteria Species 0.000 claims abstract description 52
- 102000004190 Enzymes Human genes 0.000 claims abstract description 41
- 108090000790 Enzymes Proteins 0.000 claims abstract description 41
- 238000000034 method Methods 0.000 claims abstract description 36
- 239000000203 mixture Substances 0.000 claims abstract description 35
- 230000008569 process Effects 0.000 claims abstract description 24
- 238000000855 fermentation Methods 0.000 claims abstract description 18
- 230000004151 fermentation Effects 0.000 claims abstract description 18
- 229920002472 Starch Polymers 0.000 claims abstract description 16
- 235000019698 starch Nutrition 0.000 claims abstract description 16
- 230000001461 cytolytic effect Effects 0.000 claims abstract description 14
- 239000008107 starch Substances 0.000 claims abstract description 14
- 241000588921 Enterobacteriaceae Species 0.000 claims abstract description 11
- OWEGMIWEEQEYGQ-UHFFFAOYSA-N 100676-05-9 Natural products OC1C(O)C(O)C(CO)OC1OCC1C(O)C(O)C(O)C(OC2C(OC(O)C(O)C2O)CO)O1 OWEGMIWEEQEYGQ-UHFFFAOYSA-N 0.000 claims abstract description 10
- GUBGYTABKSRVRQ-PICCSMPSSA-N Maltose Natural products O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@@H](CO)OC(O)[C@H](O)[C@H]1O GUBGYTABKSRVRQ-PICCSMPSSA-N 0.000 claims abstract description 10
- 230000020477 pH reduction Effects 0.000 claims abstract description 10
- 235000000346 sugar Nutrition 0.000 claims abstract description 10
- 235000013339 cereals Nutrition 0.000 claims abstract description 9
- 230000000977 initiatory effect Effects 0.000 claims abstract description 9
- 150000008163 sugars Chemical class 0.000 claims abstract description 9
- 241000588698 Erwinia Species 0.000 claims abstract description 7
- 241000531155 Pectobacterium Species 0.000 claims abstract description 7
- 230000000694 effects Effects 0.000 claims description 47
- 229940088598 enzyme Drugs 0.000 claims description 38
- 108010059892 Cellulase Proteins 0.000 claims description 26
- 229940106157 cellulase Drugs 0.000 claims description 23
- 239000001913 cellulose Substances 0.000 claims description 20
- 229920002678 cellulose Polymers 0.000 claims description 20
- 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 claims description 18
- 102000013142 Amylases Human genes 0.000 claims description 17
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- 230000001580 bacterial effect Effects 0.000 claims description 17
- 239000008103 glucose Substances 0.000 claims description 17
- 238000012360 testing method Methods 0.000 claims description 16
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- 230000002573 hemicellulolytic effect Effects 0.000 claims description 11
- 108010073178 Glucan 1,4-alpha-Glucosidase Proteins 0.000 claims description 8
- 244000052616 bacterial pathogen Species 0.000 claims description 8
- 230000015556 catabolic process Effects 0.000 claims description 8
- 239000003795 chemical substances by application Substances 0.000 claims description 8
- 238000006731 degradation reaction Methods 0.000 claims description 8
- 230000000593 degrading effect Effects 0.000 claims description 8
- 241000588912 Pantoea agglomerans Species 0.000 claims description 7
- 239000000654 additive Substances 0.000 claims description 6
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- 235000001727 glucose Nutrition 0.000 claims description 6
- FBPFZTCFMRRESA-FSIIMWSLSA-N D-Glucitol Natural products OC[C@H](O)[C@H](O)[C@@H](O)[C@H](O)CO FBPFZTCFMRRESA-FSIIMWSLSA-N 0.000 claims description 4
- FBPFZTCFMRRESA-KVTDHHQDSA-N D-Mannitol Chemical compound OC[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)CO FBPFZTCFMRRESA-KVTDHHQDSA-N 0.000 claims description 4
- SQUHHTBVTRBESD-UHFFFAOYSA-N Hexa-Ac-myo-Inositol Natural products CC(=O)OC1C(OC(C)=O)C(OC(C)=O)C(OC(C)=O)C(OC(C)=O)C1OC(C)=O SQUHHTBVTRBESD-UHFFFAOYSA-N 0.000 claims description 4
- 229930006000 Sucrose Natural products 0.000 claims description 4
- CZMRCDWAGMRECN-UGDNZRGBSA-N Sucrose Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 CZMRCDWAGMRECN-UGDNZRGBSA-N 0.000 claims description 4
- PYMYPHUHKUWMLA-WDCZJNDASA-N arabinose Chemical compound OC[C@@H](O)[C@@H](O)[C@H](O)C=O PYMYPHUHKUWMLA-WDCZJNDASA-N 0.000 claims description 4
- PYMYPHUHKUWMLA-UHFFFAOYSA-N arabinose Natural products OCC(O)C(O)C(O)C=O PYMYPHUHKUWMLA-UHFFFAOYSA-N 0.000 claims description 4
- SRBFZHDQGSBBOR-UHFFFAOYSA-N beta-D-Pyranose-Lyxose Natural products OC1COC(O)C(O)C1O SRBFZHDQGSBBOR-UHFFFAOYSA-N 0.000 claims description 4
- 235000013681 dietary sucrose Nutrition 0.000 claims description 4
- 229960000367 inositol Drugs 0.000 claims description 4
- 235000010355 mannitol Nutrition 0.000 claims description 4
- CDAISMWEOUEBRE-UHFFFAOYSA-N scyllo-inosotol Natural products OC1C(O)C(O)C(O)C(O)C1O CDAISMWEOUEBRE-UHFFFAOYSA-N 0.000 claims description 4
- 239000000600 sorbitol Substances 0.000 claims description 4
- 229960004793 sucrose Drugs 0.000 claims description 4
- FBPFZTCFMRRESA-JGWLITMVSA-N D-glucitol Chemical compound OC[C@H](O)[C@@H](O)[C@H](O)[C@H](O)CO FBPFZTCFMRRESA-JGWLITMVSA-N 0.000 claims description 3
- 229930195725 Mannitol Natural products 0.000 claims description 3
- 241001465754 Metazoa Species 0.000 claims description 3
- WQZGKKKJIJFFOK-VFUOTHLCSA-N beta-D-glucose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-VFUOTHLCSA-N 0.000 claims description 3
- GUBGYTABKSRVRQ-QUYVBRFLSA-N beta-maltose Chemical compound OC[C@H]1O[C@H](O[C@H]2[C@H](O)[C@@H](O)[C@H](O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@@H]1O GUBGYTABKSRVRQ-QUYVBRFLSA-N 0.000 claims description 3
- CDAISMWEOUEBRE-GPIVLXJGSA-N inositol Chemical compound O[C@H]1[C@H](O)[C@@H](O)[C@H](O)[C@H](O)[C@@H]1O CDAISMWEOUEBRE-GPIVLXJGSA-N 0.000 claims description 3
- 239000000594 mannitol Substances 0.000 claims description 3
- 241000209140 Triticum Species 0.000 claims description 2
- 235000021307 Triticum Nutrition 0.000 claims description 2
- -1 and amygdaline Chemical compound 0.000 claims description 2
- 230000000717 retained effect Effects 0.000 claims description 2
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 2
- 150000001720 carbohydrates Chemical class 0.000 claims 1
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- 238000004321 preservation Methods 0.000 abstract description 13
- 239000005418 vegetable material Substances 0.000 abstract 2
- 241000588914 Enterobacter Species 0.000 abstract 1
- 230000002538 fungal effect Effects 0.000 abstract 1
- JVTAAEKCZFNVCJ-UHFFFAOYSA-N lactic acid Chemical compound CC(O)C(O)=O JVTAAEKCZFNVCJ-UHFFFAOYSA-N 0.000 description 23
- 238000011282 treatment Methods 0.000 description 15
- 230000002255 enzymatic effect Effects 0.000 description 14
- 239000004310 lactic acid Substances 0.000 description 12
- 235000014655 lactic acid Nutrition 0.000 description 12
- 239000000758 substrate Substances 0.000 description 11
- BDAGIHXWWSANSR-UHFFFAOYSA-N methanoic acid Natural products OC=O BDAGIHXWWSANSR-UHFFFAOYSA-N 0.000 description 10
- 240000004658 Medicago sativa Species 0.000 description 9
- 235000010624 Medicago sativa Nutrition 0.000 description 9
- 230000007423 decrease Effects 0.000 description 9
- 238000006460 hydrolysis reaction Methods 0.000 description 9
- 239000000047 product Substances 0.000 description 9
- 230000007062 hydrolysis Effects 0.000 description 8
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 6
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 6
- FERIUCNNQQJTOY-UHFFFAOYSA-N Butyric acid Chemical compound CCCC(O)=O FERIUCNNQQJTOY-UHFFFAOYSA-N 0.000 description 6
- 230000006872 improvement Effects 0.000 description 6
- 238000010348 incorporation Methods 0.000 description 6
- 229910052757 nitrogen Inorganic materials 0.000 description 6
- OSWFIVFLDKOXQC-UHFFFAOYSA-N 4-(3-methoxyphenyl)aniline Chemical compound COC1=CC=CC(C=2C=CC(N)=CC=2)=C1 OSWFIVFLDKOXQC-UHFFFAOYSA-N 0.000 description 5
- 108010084185 Cellulases Proteins 0.000 description 5
- 102000005575 Cellulases Human genes 0.000 description 5
- 230000008901 benefit Effects 0.000 description 5
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- 102000006995 beta-Glucosidase Human genes 0.000 description 5
- 235000019253 formic acid Nutrition 0.000 description 5
- 150000004676 glycans Chemical class 0.000 description 5
- 229920001282 polysaccharide Polymers 0.000 description 5
- 239000005017 polysaccharide Substances 0.000 description 5
- 240000005979 Hordeum vulgare Species 0.000 description 4
- 235000007340 Hordeum vulgare Nutrition 0.000 description 4
- 239000002253 acid Substances 0.000 description 4
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- 238000004519 manufacturing process Methods 0.000 description 4
- 230000000050 nutritive effect Effects 0.000 description 4
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- CURLTUGMZLYLDI-UHFFFAOYSA-N Carbon dioxide Chemical compound O=C=O CURLTUGMZLYLDI-UHFFFAOYSA-N 0.000 description 2
- GUBGYTABKSRVRQ-CUHNMECISA-N D-Cellobiose 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)OC(O)[C@H](O)[C@H]1O GUBGYTABKSRVRQ-CUHNMECISA-N 0.000 description 2
- 108010082495 Dietary Plant Proteins Proteins 0.000 description 2
- 240000008042 Zea mays Species 0.000 description 2
- 235000002017 Zea mays subsp mays Nutrition 0.000 description 2
- 229940025131 amylases Drugs 0.000 description 2
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- 125000001547 cellobiose group Chemical group 0.000 description 2
- 230000001413 cellular effect Effects 0.000 description 2
- 239000000470 constituent Substances 0.000 description 2
- XBDQKXXYIPTUBI-UHFFFAOYSA-N dimethylselenoniopropionate Natural products CCC(O)=O XBDQKXXYIPTUBI-UHFFFAOYSA-N 0.000 description 2
- 125000002791 glucosyl group Chemical group C1([C@H](O)[C@@H](O)[C@H](O)[C@H](O1)CO)* 0.000 description 2
- 230000036541 health Effects 0.000 description 2
- 239000001257 hydrogen Substances 0.000 description 2
- 229910052739 hydrogen Inorganic materials 0.000 description 2
- 239000012528 membrane Substances 0.000 description 2
- 238000006116 polymerization reaction Methods 0.000 description 2
- IUVKMZGDUIUOCP-BTNSXGMBSA-N quinbolone Chemical compound O([C@H]1CC[C@H]2[C@H]3[C@@H]([C@]4(C=CC(=O)C=C4CC3)C)CC[C@@]21C)C1=CCCC1 IUVKMZGDUIUOCP-BTNSXGMBSA-N 0.000 description 2
- 238000011160 research Methods 0.000 description 2
- HDTRYLNUVZCQOY-UHFFFAOYSA-N α-D-glucopyranosyl-α-D-glucopyranoside Natural products OC1C(O)C(O)C(CO)OC1OC1C(O)C(O)C(O)C(CO)O1 HDTRYLNUVZCQOY-UHFFFAOYSA-N 0.000 description 1
- RFCYHWZKRUEYHZ-KYWOWLQSSA-N 1h-indole;(2r,3s,4r)-2,3,4,5-tetrahydroxypentanal Chemical compound C1=CC=C2NC=CC2=C1.OC[C@@H](O)[C@H](O)[C@@H](O)C=O RFCYHWZKRUEYHZ-KYWOWLQSSA-N 0.000 description 1
- KUWPCJHYPSUOFW-YBXAARCKSA-N 2-nitrophenyl beta-D-galactoside Chemical compound O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@H]1OC1=CC=CC=C1[N+]([O-])=O KUWPCJHYPSUOFW-YBXAARCKSA-N 0.000 description 1
- 229920000945 Amylopectin Polymers 0.000 description 1
- 229920000856 Amylose Polymers 0.000 description 1
- 108010082340 Arginine deiminase Proteins 0.000 description 1
- 235000021537 Beetroot Nutrition 0.000 description 1
- 229920002134 Carboxymethyl cellulose Polymers 0.000 description 1
- 102000016938 Catalase Human genes 0.000 description 1
- 108010053835 Catalase Proteins 0.000 description 1
- 229920003043 Cellulose fiber Polymers 0.000 description 1
- SHZGCJCMOBCMKK-UHFFFAOYSA-N D-mannomethylose Natural products CC1OC(O)C(O)C(O)C1O SHZGCJCMOBCMKK-UHFFFAOYSA-N 0.000 description 1
- 229920001353 Dextrin Polymers 0.000 description 1
- 239000004375 Dextrin Substances 0.000 description 1
- 101710121765 Endo-1,4-beta-xylanase Proteins 0.000 description 1
- 239000001828 Gelatine Substances 0.000 description 1
- UFHFLCQGNIYNRP-UHFFFAOYSA-N Hydrogen Chemical compound [H][H] UFHFLCQGNIYNRP-UHFFFAOYSA-N 0.000 description 1
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 description 1
- PNNNRSAQSRJVSB-UHFFFAOYSA-N L-rhamnose Natural products CC(O)C(O)C(O)C(O)C=O PNNNRSAQSRJVSB-UHFFFAOYSA-N 0.000 description 1
- GUBGYTABKSRVRQ-QKKXKWKRSA-N Lactose Natural products OC[C@H]1O[C@@H](O[C@H]2[C@H](O)[C@@H](O)C(O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@H]1O GUBGYTABKSRVRQ-QKKXKWKRSA-N 0.000 description 1
- 241000209082 Lolium Species 0.000 description 1
- OFOBLEOULBTSOW-UHFFFAOYSA-L Malonate Chemical compound [O-]C(=O)CC([O-])=O OFOBLEOULBTSOW-UHFFFAOYSA-L 0.000 description 1
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- 235000010627 Phaseolus vulgaris Nutrition 0.000 description 1
- HDTRYLNUVZCQOY-WSWWMNSNSA-N Trehalose Natural products O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@H](O)[C@@H](O)[C@@H](O)[C@@H](CO)O1 HDTRYLNUVZCQOY-WSWWMNSNSA-N 0.000 description 1
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- 235000016383 Zea mays subsp huehuetenangensis Nutrition 0.000 description 1
- 239000008351 acetate buffer Substances 0.000 description 1
- 150000007513 acids Chemical class 0.000 description 1
- 230000003113 alkalizing effect Effects 0.000 description 1
- HDTRYLNUVZCQOY-LIZSDCNHSA-N alpha,alpha-trehalose Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 HDTRYLNUVZCQOY-LIZSDCNHSA-N 0.000 description 1
- WQZGKKKJIJFFOK-DVKNGEFBSA-N alpha-D-glucose Chemical compound OC[C@H]1O[C@H](O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-DVKNGEFBSA-N 0.000 description 1
- 238000013459 approach Methods 0.000 description 1
- DLRVVLDZNNYCBX-ZZFZYMBESA-N beta-melibiose Chemical compound O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@@H]1OC[C@@H]1[C@@H](O)[C@H](O)[C@@H](O)[C@H](O)O1 DLRVVLDZNNYCBX-ZZFZYMBESA-N 0.000 description 1
- 239000006227 byproduct Substances 0.000 description 1
- 239000001569 carbon dioxide Substances 0.000 description 1
- 229910002092 carbon dioxide Inorganic materials 0.000 description 1
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- 235000010948 carboxy methyl cellulose Nutrition 0.000 description 1
- 239000008112 carboxymethyl-cellulose Substances 0.000 description 1
- 229940105329 carboxymethylcellulose Drugs 0.000 description 1
- 238000010909 chemical acidification Methods 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 230000000295 complement effect Effects 0.000 description 1
- 150000004695 complexes Chemical class 0.000 description 1
- 150000001875 compounds Chemical class 0.000 description 1
- 235000005822 corn Nutrition 0.000 description 1
- 235000013365 dairy product Nutrition 0.000 description 1
- 235000019425 dextrin Nutrition 0.000 description 1
- 235000019621 digestibility Nutrition 0.000 description 1
- 150000002016 disaccharides Chemical class 0.000 description 1
- 230000008030 elimination Effects 0.000 description 1
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- 230000007247 enzymatic mechanism Effects 0.000 description 1
- 230000002550 fecal effect Effects 0.000 description 1
- 239000007789 gas Substances 0.000 description 1
- 229920000159 gelatin Polymers 0.000 description 1
- 235000019322 gelatine Nutrition 0.000 description 1
- 238000003306 harvesting Methods 0.000 description 1
- 229920001519 homopolymer Polymers 0.000 description 1
- 150000002431 hydrogen Chemical class 0.000 description 1
- 230000001788 irregular Effects 0.000 description 1
- 238000009533 lab test Methods 0.000 description 1
- 239000008101 lactose Substances 0.000 description 1
- 230000002101 lytic effect Effects 0.000 description 1
- 230000014759 maintenance of location Effects 0.000 description 1
- 235000009973 maize Nutrition 0.000 description 1
- 235000013622 meat product Nutrition 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- HEBKCHPVOIAQTA-UHFFFAOYSA-N meso ribitol Natural products OCC(O)C(O)C(O)CO HEBKCHPVOIAQTA-UHFFFAOYSA-N 0.000 description 1
- 230000002503 metabolic effect Effects 0.000 description 1
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- 230000004048 modification Effects 0.000 description 1
- 235000013379 molasses Nutrition 0.000 description 1
- 239000000178 monomer Substances 0.000 description 1
- 150000002823 nitrates Chemical class 0.000 description 1
- 229920001542 oligosaccharide Polymers 0.000 description 1
- 150000002482 oligosaccharides Chemical class 0.000 description 1
- 150000007524 organic acids Chemical class 0.000 description 1
- 235000005985 organic acids Nutrition 0.000 description 1
- 239000001814 pectin Substances 0.000 description 1
- 229920001277 pectin Polymers 0.000 description 1
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- 239000000843 powder Substances 0.000 description 1
- 102000004169 proteins and genes Human genes 0.000 description 1
- 108090000623 proteins and genes Proteins 0.000 description 1
- 239000002994 raw material Substances 0.000 description 1
- 230000035484 reaction time Effects 0.000 description 1
- HEBKCHPVOIAQTA-ZXFHETKHSA-N ribitol Chemical compound OC[C@H](O)[C@H](O)[C@H](O)CO HEBKCHPVOIAQTA-ZXFHETKHSA-N 0.000 description 1
- NGFMICBWJRZIBI-UJPOAAIJSA-N salicin Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@H]1OC1=CC=CC=C1CO NGFMICBWJRZIBI-UJPOAAIJSA-N 0.000 description 1
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Classifications
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23K—FODDER
- A23K30/00—Processes specially adapted for preservation of materials in order to produce animal feeding-stuffs
- A23K30/10—Processes specially adapted for preservation of materials in order to produce animal feeding-stuffs of green fodder
- A23K30/15—Processes specially adapted for preservation of materials in order to produce animal feeding-stuffs of green fodder using chemicals or microorganisms for ensilaging
- A23K30/18—Processes specially adapted for preservation of materials in order to produce animal feeding-stuffs of green fodder using chemicals or microorganisms for ensilaging using microorganisms or enzymes
Landscapes
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Microbiology (AREA)
- Polymers & Plastics (AREA)
- Zoology (AREA)
- Animal Husbandry (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Engineering & Computer Science (AREA)
- Food Science & Technology (AREA)
- Enzymes And Modification Thereof (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Fodder In General (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
Abstract
A process for the preservation of vegetable material by lactic acidification which comprises admixing the vegetable material prior to ensilaging the same, with bacteria capable of initiating lactic fermentation, and enzymes and/or bacteria adapted to degrade higher glucides into fermentable sugars used by the bacteria initiating the lactic fermentation. The enzymes comprise a defined cellulolytic complex of fungal origin. The bacteria comprise Gram -ve bacteria belonging to the family of Enterobacteriaceae type Erwinia or Pectobacterium, group Herbicola, of the new species Enterobacter agglomerons, which breaks down starch, but not maltose. This composition with an enzyme and/or bacteria base, is incorporated on a cereal support.
Description
SPECIFICATION
Process and product for preserving fresh vegetables and moist byproducts of the Agro-alimentary industry try
The present invention is related to an improved process for preserving and valorizing fresh vegetables so as to allow the same to be consumed in an appetizing form in successive amounts, as the need arises, after harvesting said vegetables. The invention also relates to a composition or product for carrying out said process
On account of the importance of the problems raised by the preservation of fresh vegetables, considerable research work has been conducted with a view to resolving the same by devising an appropriate technique; this research work has encountered a certain number of obstacles difficult to overcome.
The technique of ensilaging is based on the principle of preserving fresh vegetables during a more or less extended period of time within a closed, tight enclosure in an acid environment or medium with a view to preventing the proliferation of putrifying alkalizing and gas-producing germs; these germs will not develop in an acid medium. A satisfactory ensilaging method is difficult to devise, since a great number of obstacles are encountered when endeavouring to put such method to practical use, the most difficult problems to be overcome being the formation of fermentation products which are dangerous to the health of animals orthe health of man when the meat and dairy products are consumed by the latter.
The mechanism to be devised is as follows: allowing the lactic bacteria contained in the medium to produce lactic acid from available soluble sugars, in such a manner that the pH of the medium may be thus lowered to a value of about 4. However in many cases the vegetables to be ensilaged do not contain a sufficient amount of fermentable sugars, and the proliferation only of the lactic bacteria, which are contained in the medium is insufficient, the pH thus not being lowered rapidly enough to the required value 4, while butyric and anaerobic bacteria develop and convert the residual sugars into butyric and acetic acid, carbon dioxide and hydrogen, the proteins being degraded into ammoniacal and other metabolic phases.
Various approaches have been devised with a view to overcoming these drawbacks. More particularly, according to one known process, a chemical acidification is effected by adding various acids.
However this known method may be dangerous under certain conditions. According to another known method, a biological acidification is effected by adding highly glucidolytic bacteria. However this
biological acidification process has been found to be difficult to carry out in practice.
According to other known methods, a raw material
having a high contentofglucide, such as molasses, is added to the ensilaged material. The results obtained when carrying out such methods in practice are not consistent, and the process involves considerable expense.
French Patent specification No. 2 361 828 discloses a process of preserving and valorizing fresh vegetables by lactic acidification, which comprises adding to the vegetables, prior to ensilaging the same, bacteria capable of initiating lactic fermentation, and adding a degradation agent for degrading higher glucides into fermentable sugars which are adapted to be used by the bacteria that initiate the lactic fermentation. This degradation agent is constituted by gram+ bacteria which initiate the fermentation of starch, glucose, mannitol (mannite), rahmnose, saccharose, amygdaline, arabinose, while not initiating the fermentation of maltose, inositol and sorbitol; the bacteria areVP+, oxydase+, catalase+, nitrates, urea-, indol- and H2S- bacteria.Said degradation agent may also comprise one or more enzymes capable of splitting polysaccharides, especially starches, pentosames and other complex polysaccharides, so as to produce fermentable sugars. More particularly, according to the abovementioned patent specification, a hemicellulolytic complex of fungic origin the main activity of which is a galactomannanasic activity and which has secondary xylanase, amylase and pectylase activities, as well as an amylase may be added to the fodder with a view to obtaining the formation of the maltose necessary for the production of lactic acid by the bacteria.
French Patent specification No. 2 390 908 discloses an improvement to the process according to
French specification No 2 361 828. In the latter specification the enzyme is exoamylase of fungic origin which does not completely degrade starch, whereas the amylase used in accordance with
French Specification No. 2,390,908 is an amylase of bacterial origin.
This enzyme (endoamyalase) acts on the liquefied starches and produces mainly alpha-D maltose and a small amountofalpha-D glucose said amylase being active in the pH range comprised between 5 and 8.
French specification No 2 390 908 also discloses the use of amyloglucosidase which is substantially more active with respect to the amylose and amylopectin chains for producing alpha-D glucose. The enzymatic composition according to said specification also comprises a hemicellulolytic complex of fungic origin which acts on the polysaccaric constituents of the cellular membranes and the dextrins in the pH range comprised between 5.5 and 8.
Patent Application No: 34183/77 (Serial No the contents of which are incorporated herein by reference, claims priority from the French
Applications from which the aforementioned French
Patent Specifications derive and describes and claims processes and compositions as hereinbefore discussed.
The present invention is aimed at providing an improved process and an improved product for ensilaging vegetables, the improvement residing inter alia in the provision of a novel enzymatic composition and in the provision of a novel bacterial composition. The enzymatic composition contains in addition to the enzymes indicated hereinabove a cellulolytic or cellulase complex capable of splitting the beta links (1--3) and (1-4) of the polysaccharides which are not attacked by the prior enzymatic com
position.
The above-mentioned complex is a cellulolytic complex of fungic origin which degrades the natural cellulose and the other polysaccharides contained in the cellular membranes.
This enzyme is active in the pH range comprised between 2 and 5. A synergy phenomenon exists
between the cellulolytic complex and the hemicellulolytic complex, as regards the degradation of the vegetable structures.
On account of the environment of the cellulose in the vegetable its hydrolysis requires a plurality of enzymes, or one single enzyme having a plurality of functions, to wit:
- hydrolysis of the amorphous zones,
- swelling of the crystalline regions and disrup
ture of the hydrogen links so as to produce linear' molecules, - hydrolysis of cellobiose to produce glucose,
- transglucosylation of disaccharides and oligosaccharides, as well as disrupture of the irregular links of cellulose and its primary hydrolysis products.
The cellulolytic complex has been chosen on the basis of the above criteria after a great number of tests had been performed on various vegetables.
A cellulase is defined by its activity as expressed in
International Units per gramme of product, on
International Unit (I.U.) corresponding to the amount of enzyme which sets free, in the form of reducing sugar, the equivalent of one micromole of glucose per minute on a given cellulosic substrate.
The activity varies depending on the nature of the substrate used:
- when the activity is tested on "Whatman"
(Registered Trade Mark) paper powder CC31,
the result is C, negative,
- when the activity is tested on carboxymethylcel
lulose, the result is Cx activity.
The complex used in accordance with the present invention has a very high cellulolytic activity, as well as secondary activities of the hemicellulolytic type.
The high cellulolytic power is indicated by extremely high Ct and Cx activity values, and bycellobiase (beta-glucosidase) activity.
The activity of the C1 enzymatic complex, defined in accordance with current hypotheses as being a compound having Cx activity to which an unknown factor is added, expresses in particular a power of solubilisation of cellulose.
C, is capable of degrading the native cellulose (crystalline cellulose having a polymerization rate (DP) higher than 3,500 glucose units) into amorphous cellulose.
The activity of the Cx enzymatic complex expresses in particular the reducing of power endoglucanase and exoglucanase. These enzymes mainly act on the cellulose fibres in the zones of reduced crystallinity and splitthe long glucose chains into smaller units.
The activity of beta-glucodiase expresses an action on the units obtained as a result of the action of Cx.
These different activities cannot be considered separately. There exists a synergistic interaction between C1 and Cx as far as the degradation of these homopolymers is concerned. The enzymatic mechanisms C, and Cx lead to the production of cellobiase; the latter is then submitted to hydrolysis by a beta-glucosidase, thus producing two glucose units.
Apparently the hydrolysis reactions of cellulose comprise the stages schematically indicated herein-below:
C1 Native cellulose ---------------------------------------- cellulose hydrolytic Cx
Reactive cellulose ------------------------------------------ cellobiose Hydrolytic beta-glucosidase Cellobiose ---------------------------------------- molecules of glucose
The C, comples solubilizesthe crystalline cellulose (polymerization degree DP higher than 3,500 glucose monomers) and produces reactive cellulose (amorphous cellulose).
Under the action of the enzymatic Cx complex (endoglucanase and exoglucanase) the chains of reactive cellulose are split either inside the chain and randomly, in the case of endoglucanase, or starting from the non-reducing chain ends, in the case of exoglucanase.
These reactions, taken as a whole, produce cellobiose units.
These cellobiose units are hydrolysed by betaglucosidase to produce two glucose molecules.
In the case of fungic cellulases according to the
invention the enzymatic C1 and Cx complex is capable of hydrolyzing the insoluble native cellulose, so as to produce glucose.
The cellulases according to the invention are chosen not only on the basis of the above-indicated general criteria, but also on the basis of considerations regarding the particular ensilaging medium envisaged, taking into account the po lysaccha ro lytic behaviourofthese cellulases.
This polysaccharolytic behaviour has been determined on two types of substrates:
a) - pure substrates;
b) - dehydrated substrates.
CASE OF THE PURE SUBSTRATES:
The activity of cellulases A, B, C, D, E, and F has been determined on various substrates at a given concentration in a 10-'M M acetate buffer medium.
The activity has been measured in accordance with the conventional standards, to wit, at pH 4.8 and 50"C, after hydrolysis during 20 minutes. The reducing power has been determined by the method using hexaferrocyanide.
TABLEI
SUBSTRATE "Whatman" C.M.C. Pectin Xylane Arabino Starch Locus (concen- paper galactane bean ration) 1% 1% 0.25% 0.25% 0.10% 0.25% 0.25 ENZYMES Ulig Ullg U Ullg Ullg Ulig Ulig (activity) (C, ) (Cx) A 400 6444 356 511 22 394 544 B 211 5660 322 611 33 100 300 C 266 1999 411 311 0 244 389 D 52 6440 255 511 0 120 132 E 372 8500 305 605 0 0 0 F 960 7666 1030 1200 0 0 140 CASE OF THE DEHYDRATED SUBSTRATES:
The activity of enzymes A, B, C, D, E and F, has also been determined on various dehydrated vegetable substrates.
The activity has been tested at pH values of 3.8,4.8 and 5.8 et 30"C after hydrolysis during 24 hours. The reducing power has been determined by means of the method using dinitrosalicyclic acid.
TABLE II
Tested substrates Lucerne Ray-grass Maize Beetroot Straw Tested + (Rye-grass) cellulases pH ACTIVITY (tug) 3,8 2810 2280 1560 1810 1560 A 4,8 2440 2560 2080 1530 1690 5,8 I 2560 2220 1690 1500 1530 3,8 1560 1670 ' 1530 1220 1390 B 4,8 1280 2060 1670 1220 1500 5,8 890 1680 1940 890 1380 3,8 1280 1530 1390 1110 1110 C 4,8 1280 1750 1530 1110 1290 5,8 940 1560 1170 720 1110 3,8 1390 1440 1470 1278 1167 D 4,8 1190 2060 1390 1111 1306 5,8 890 1720 1530 972 1222 3,8 611 1190 1111 556 694 E 4,8 972 1528 1250 0 694 5,8 0 1167 1278 0 694 3,8 1306 500 694 556 F 4,8 889 972 1222 610 444 5,8 750 1000 560 550 333 The analysis of these various behaviours allowed the of the cellulolytic complex to be used in accordance with the invention to be used for ensilaging vegetables::
It was thus found that the cellulase or the cellulolytic complex to be added to the fresh vegetables when carrying out the process according to the invention must correspond to a C1 activity of 50 to 0.005 l.U. and a Cx activity of 500 to 0.05 l.U. per 100 grammes vegetable, these activities being determined at pH 4.8 at a temperature of 50"C after hydrolysis for 20 minutes.
Furthermore, the selected cellulase must retain a considerable activity even after a long dwelling time in the silo.
It has been shown experimentallythat under conditions close to those prevailing when vegetables are ensilaged the cellulolytic complex must retain at least 30% of its initial activity after 10 days.
TABLE 111
Preservation 0 5 10 15 | 20 time (days) pH4,8 100% 97% 61% 26% 3% pH5,8 100% 85% 58% 27% 0% The velocity, or rate, of enzymatic degradation of the vegetable structure is a function of glucose elimination; this enzymatic unbalance is obtained by using bacteria having a high fermentation power; the acidification of the medium occurs very rapidly.
When the vegetable mass has been stabilized the bacterial proliferation and the formation of lactic acid are discontinued, contrary to the cellulolytic activity of cellulase, which continues for more than 10 days.
This activity of producing and accumulating the glucose formed within the ensilaged material increases the nutritive value of the ensilaged vegetables.
The enzymatic composition used in accordance with the present invention thus comprises a cellulase or cellulolytic complex having the aboveindicated characteristics, in association with the enzymes described in French Patent specification No 2390 908, to wit, a fungic amylase, a bacterial amylase, an amyloglucosidase and a hemicellulolytic complex.
These enzymes present in the composition thus exhibit a complementary activity on account of their effect on the glucides-which may be extremely simple glucides or extremely complex ones - in pH ranges comprised between 7 and 2. The respective maximum activities of the various enzymes occur in relays as the pH decreases (which latter does not reach values lowerthan 3.5 in the silo), and within temperature intervals varying from 10 to 30"C which are compatible with the conditions prevailing in the silo.
The bacterial composition used in accordance with the present invention is characterized by the utilisation of novel bacterial strains adapted to be used when ensilaging vegetables, said strains being adapted to be used separately or in admixture with the bacterial strains andlorthe enzymes disclosed in the prior art and in the present description. This novel composition leads to considerably improved ensilaging results. The novel bacterial strains according to the invention are gram - bacteria; they belong to the Enterobacteriaceae family, the Erwinia or Pectobacterium type and the Herbiola group; they are called Enterobacter agglomerans (classification according to Bergey's Manual of Bacteriology, eighth edition).
The properties of such bacteria are listed in the appended TABLE IV.
TABLE IV
EnterobacterAgglomerans Adonitol
Gram - Inositol
Utilisation malonate + Sorbitol
Glucose + Arabinose +
Phenylalamine desaminase - Maltose
ONPG + Trehalose +
Indole - Xylose
H2S - Starch +
LDC - Oxydase
ODC - Gelatine +
Urease - Amygdaline +
Saccharose + Melibiose Argininedihydrolase - V.P. +
Salicine - Rhamnose
The utilisation of these novel bacterial strains, separately or in combination with other bacterial strains and/or enzymes, for ensilaging vegetables is effected in accordance with the operating conditions described in the prior publications. The bacteria may be grown on a nutritive support comprising cereal wheats. The composition to be introduced into the silo comprises a mixture of the required bacteria deposited on a soluble or insoluble support, with the enzymes defined in the present disclosure.
In a preferred embodiment of the present invention, the enzymes and the bacteria are placed on a cereal support (corn, barley, germinated barley), preferably in a finely ground condition.
In another preferred embodiment of the invention the bacteria and the enzymes are placed onto a support of a type constituted by pre-gelated starch, maltohexose, etc..., which support is highly soluble in cold water.
The starch and other polysaccharides contained in the supports combine with the glucides of the vegetables and thus increase the nutritive value of the ensilaged matter. The composition comprising the mixture of bacteria on their support with the enzymatic complex, deposited or not on a cereal support, may include various proportions of each of one of these constituents. The dry mixture comprises an amount of about 100,000 to 1 million cocci and 100,000 to 1 million bacilli pergramme.
The amounts of cellulase, hemicellulolytic complex, amylase and amyloglucosidase may vary; they are calculated according to the nature of the fodder to be treated.
The amount of cellulase to be added to the ensilaged fresh vegetables must correspond to a Cl activity of 50 to 0.005 I.U. per 100 g. vegetable; it must thus be equal to 2 to 2.10-4#by weight of fresh vegetables when a cellulase having a 250 I.U./gramme titre is used.The proportions of the other enzymes are comprised between 0.05 and 0.2/ bacterial amylases having a 250 units/gramme titre (by weight of vegetables), 0.10 to 0.20%o fungic amylases having a 50,000 units
AG/gramme titre (by weight of vegetables), 0.10 to 0.70 /Oo amylglucosidase having a 200 units
AG/gramme titre (by weight of vegetables), 0.05 to 0.20%o hemicellulolytic complex having a 35,000 I.U./gramme titre (by weight of vegetables).
When the enzymes are deposited on a cereal support in accordance with a preferred embodiment of the present invention, the product to be incorporated in the ensilaged matter may contain about 1 kg enzymes per 9 kg support. When a soluble support is used, the ratios of enzyme concentration to support vary and may be comprised between 1/1.5 and 1/4.
Due to this incorporation of cellulase in the support, the amount of available fermentable sugars is increased, whereby a larger and more rapid production of lactic acid is obtained. The vegetable protein wil thus be more efficiently preserved. Furthermore, the nutritive value of the medium will be increased.
With a view to showing the advantages brought about by using a cellulolytic complex and bacteria of the Enterobacteriaceae family, tests were performed in micro-silos and mini-silos. The various preservation parameters as well as the vegetable structure
parameters were studied.
1. TESTS PERFORMED IN MICRO-SILOS
A first laboratory test series was performed in
micro-silos. These tests were carried out in May on
lucerne (alfafa). The micro-silos had a capacity of 1
kg. The lucerne was finely chopped and then ensil
aged in accordance with the following operating
mode:
A- One series of micro-silos were treated by means of a preserving additive having the following general formula:
cereal support 90%
pre-mixture 10%, the pre-mixture being constituted by:
- a bacterial complex (5 lactic bacteria on lactose
support):
- an enzymatic complex comprising:: an amylase of fungic origin; an amylase of bacterial origin; an amyloglucosidase; a a hemicellulolytic-complex of fungic origin, the main activity of which was a galactomannasic
activity;
- a high-energy support: finely ground barley +
lactoserum, the bacterial and enzymatic comp
lexes representing each 1% of the pre-mixture
composition.
The preservation additive was admixed with the lucerne in a proportion of 2% (the rate of incorporated pre-mixture thus being 0.2%), and 1% barley was added.
B - A series of micro-silos were treated with the same preservation additive as that used according to
A, however, a cellulase of fungic origin (stemming from Trichoderma viride) was added, said cellulase presenting a C, activity of 250 units/gramme and a Cx activity of 2,500 units/gramme, as determined at pH.
4.8 at a temperature of 50 C, for a reaction time of 20 minutes, the proportion of incorporation of this cellulase being 2 g/T (i.e.2.10-4% by weight) as referred to the fresh vegetables (Test B) and 200 g/T (i.e.
0.02%) by weight as referred to the fresh vegetables (Test B').
C - A series of micro-silo reference tests:
- a series of micro-silo tests with lucerne contain
ing no preservation product : T = 0.
After 100 days duration of ensilaging the microsilos were opened, the following parameters were recorded: pH, lactic acid, NH$N (total). The results are listed in TABLE V overleaf.
It can be seen that the admixing of a cellulase to a bacteria + enzyme complex according to patent specification no 2 390 908 leads to an improvement of the performances of the preservation additive. A more satisfactory preservation of the vegetables is obtained, as illustrated by the comparison of A and
B', as follows:
- a decrease of the pH value from 4.13 to 3.73
(decrease of 10%);
TABLE V
Lactic acid pH Total NH3/N (g/kg MS) Référence: T = 0 5.66 26g 25.15 Premixed lucerne 4.13 143.68 16.33 + 0,2%(A).
. Premixed lucerne + 0,2% + cellulase of fungic 4.32 144.75 16.20 origin 2 g/T (B)- Premixed luceme + 0,2% + cellulase of fungic 3.73 169.47 15.02 origin 200 g/T (B') - a 15% decrease of the lactic acid production; - a 8% decrease of the total NHJN ratio; this shows an improvement of the preser
vation of the vegetable protein which results from the rapid acidification of the medium.
2. TESTS PERFORMED IN MINI-SILOS
These tests were carried out in June with lucerne in mini-silos having a capacity of 150 kg.
The lucerne was finely chopped, then ensilaged in
accordance with the operation conditions indicated
herein-above.
A. -A series of mini-silos was treated by means of
the same preservation additive as that used in the
micro-silo tests described under A, the proportion of
incorporation being 0.2% pre-mixture.
B. -A series of mini-silos was treated in accor
dance with the formula and the dose indicated under
A, to which the same cellulase of fungic origin was added in a proportion of 2 grammes/T.
After 100 days ensilaging the mini-silos were opened, the analysis of the ensilaged materials gave
the results shown in TABLE VI overleaf.
The results listed listed herein-above clearly show
the advantages of adding a cellulase to the bacterial
+ enzyme complex described in Patent specification no 2 390 908.
This addition results in:
- a decreased pH :3.94 as compared to 4.20 (less 6%); TABLE Vl
A B silos 0.2% premixture | silos 0.2% premixture + cellulase (2 gfT) . Dry matter (MS)% ....... 23.67 27.27 . E.N.A. (g/kg MS) ....... 51.25 48.97 . pH ....... 4.20 3.94 - Lactic acid (glkg MS) ....... | 80.62 | 114.40 . Acetic acid (g/kg MS) ....... 17.42 20.04 . Total NH3/N ....... 18.40 13.31 . Total N (g/kg MS) ....... 21.70 23.12 . Ammoniacal N(g/kg MS) ....... 3.87 3.09 - an increased proportion of lactic acid (plus
29.53%); - a more satisfactory preservation of the proteinic
part of the ensilaged matter, when a cellulase is
added; this is confirmed by analysis.
The following results are obtained in this case: - a decreased total NH/N ratio (less 27.6%); - an increased proteic rate (plus 6%); - a decreased ammoniacal nitrogen rate (less
20.1%).
This increased acidification velocity may be explained by the fact that the bacteria are provided more rapidly with an important amount of fermentable sugars which are easily converted into lactic acid.
The effect of the cellulase introduced into the medium can be seen here again.
In the examples given herein-below, the mixture applied on the support in accordance with the invention was constituted by the complex described in
French Patent Specification no 2 361 828 and/or in
French Patent Specification no 2 390 908, the enzymatic complex disclosed in the present description, to which gram - bacilli of the Enterobacteriaceae family, of the Erwinia or Pectobacterium type, Herbicola group, were added, the proportion of incorporation of these bacilli in the mixture corresponding to 105 to 106 bacilli per gramme
EXAMPLES
Tests were carried out in silos having a capacity of 4 m3 with Dactile Lucifer harvested in June, at the starting stage of heading.The finely chopped fodder was stocked under four different conditions:
A. ensilaging without treatment;
B. ensilaging with 4 litres formic acid/ton in
accordance with known methods;
C. ensilaging with the pre-mixture, the composi tionofwhich is described in French Patent
specifications no 2 361 828 and no 2 390 908:
ensilaging the matterto be treated with an
addition of 7 kg of the strain of 7 bacteria on
support, the properties of which are indicated
in French Patent Specification no 2 361 828
page 7, no 1 to 7 and enzymes; proportion of
incorporation: 10 kg/ton;
D. ensilaging with the pre-mixture according to C,
which bacilli according to the invention were
added, to wit: gram - bacteria, bacteria of the
Enterobacteriaceae family, Erwinia or Pec
tobacterium type, Herbicola group, named
Enterobacter agglomerans.The proportion of
the incorporation of the complex was 10 kg/T.
After 90 to 100 days the different silos were opened, and the vegetables were analysed. The results thus obtained were listed herein-after in
TABLE VII.
The results show that the mixture according to the
French Patent specifications no 2361 828 and no 2 390 906 led already to a considerable improvement, as regards the preservation of the ensilaged matter, which is illustrated by:
TABLE Vll
Parameters N-Nk3 N soluble Organic acids (g/kg M.S.) pH o/ Total N Total N lactic propionic acetic butyric Treatments A: not treated. 5.28 17.76 63.80 23 1.38 29.46 ' traces B : treatment with 4.05 7.10 45.43 41.36 traces 14.95 0 formic acid 4%.
C : treatment according 4.02 14 48.10 90 0 14.20 0 French Patent 2.390.908.
D: novel treatment 3.70 8 44 112 0 18.28 0 (C=bactericid straties according to the invention).
- a decrease of pH value, which was lowered from
5.28 to 4.02; - an increased lactic acid content of 90 g/kg MS as
compared to 23 g/kg MS; - an improved proteinic protection which is illus
N-NH3
trated by decrease of the ---- ratio dropping
total N
soluble N
from 17.76 to 14 and of the ratio dropping
total N
from 63.80 to 48.10.
This mixture had the advantage of leading to no formation of propionic and butyric acid.
The mixture according to the present invention resulted in a supplementary improvement which is illustrated by:
- a decrease of the pH value (dropping from 4.02
to 3.70); an increased lactic acid content (112 g/kg MS as compared to 90 g/kg MS);
- an improved proteic protection which is illus
trated by a decrease of the N-NH3/total N ratio
(dropping from 14 to 8 and of the soluble N/total
N ratio (dropping from 48.10 to 44).
One advantage of this mixture resides in the fact that it leads to no fermentation of propionic and butyric acid.
The digestibility and ingestibility of these ensilaged matters were measured on mutton; after the various treatments the following results were found:
B : treatment with formic acid : 0.64 UF/kg; C : treatment according to French Patent specifica
tion no 2 361 828 and no 2 390 908: 0.74 UF/kg; D : treatment according to the present invention
0.82 UF/kg.
The nitrogen balance on animals in the growth period produced results which showed the advantages brought about by the treatment with ensilaging products according to the present invention, as illustrated in TABLE VIII.
The nitrogen retention obtained when applying the method according to the present invention is more than twice as large as that obtained by treatment with formic acid.
The invention is not limited by the foregoing description and the various embodiments illustrated therein. Various modifications may be envisaged by those skilled in the art without departing from the spirit and the scope of the invention as defined by the appended claims.
The EnterobacterAgglomerans bacteria employed in embodiments of the present invention has been lodged at the C.N.C.M., Institut Pasteur, 28 rue du
Docteur Roux, 75724 Paris, Cedex 15, France on 11th
February 1980, under accession number 1-114.
TABLE Vlil
Parameters Ingested Fecal N Urinary N Retained N N Ingested Ingested Ingested Treatments < g/j 9/i % N g/j % N g/j % N A: nottreated. 21 7.90 3.76 13 61.9 0.10 0.50 B : treatment with formic acid 0.4%. 18.9 7.34 38.8 10.4 55 1.1 5.88 C : treatment according to main patent + 17 7.07 41.6 8.12 47.7 1.8 10.50 1 st Addition.
D : treatment according to invention. 16.5 5.4 38.8 7.70 47 2.40 14.50
Claims (2)
1. A process of preserving and valorizing fresh vegetable matter by lactic acidification, comprising admixing to said vegetable matter prior to ensilaging the same, bacteria capable of initiating lactic fermentation, and adding degradation agent which is adapted to degrade higher glucides into fermentable glucides for use by the bacteria initiating said lactic fermentation, and which is constituted by enzymes and/or bacteria, wherein said enzymes, if present, comprise, optionally in combination with a fungic amylase, with an amyloglucosidase, or with a hemicellulolytic complex of fungic origin having primarily a galactomannanasic activity, a cellulase or cellulolytic complex of fungic origin capable of degrading the native cellulose into glucose and having a
C, activity of 50 to 0.005. International Units and a Cx activity of 500 to 0.05 International Units per 100 grammes fresh vegetables and retaining under the prevailing ensilaging conditions at least 30% of said activity after 10 days, and said bacteria, if present, being gram-bacteria which initiate starch fermentation but do not initiate maltose fermentation and belonging to the family of Enterobacteriaceae, type
Erwinia or Pectobacterium, group Herbicola, named
Enterobacter agglomerans.
1. A process of preserving and valorizing fresh vegetable matter by lactic acidification, comprising admixing to said vegetable matter prior to ensilaging the same, bacteria capable of initiating lactic fermentation, and adding degradation agent which is adapted to degrade higher glucides into fermentable glucides for use by the bacteria initiating said lactic fermentation, and which is constituted by enzymes and/or bacteria, wherein said enzymes if present, comprise in combination with a fungic amylase, an amyloglucosidase, a hemicellulolytic complex of fungic origin having primarily a galactomannanasic activity, a native glucose cellulose
having a C1 activity of 50 to 0.005 International
Units and a Cx activity of 500 to 0.05 International
Units per 100 grammes fresh vegetables and retaining
under the prevailing ensilaging conditions at least 30% of said activity after 10 days, and said bacteria, if
present, being gram-bacteria which initiate starch fermentation but do not initiate maltose fermentation, and belonging to the family of Enterobacteriaceae, type Erwinia or Pectobacterium, group
Herbicola, named Enterobacter agglomerans.
2. A process according to Claim 1, wherein the bacteria belonging to the family of Enterobacteriaceae are used in association with other bacteria capable of degrading higher glucides into fermentable glucides.
3. A process according to claim 2, wherein said other bacteria are selected from the bacteria capable of degrading higher carbohydrates which are disclosed in Patent Application No: 34183/77 (Serial No..
..............).
4. A process according to claim 1 or 2, wherein the bacteria belonging to the family of Enterobacteriaceae are used in association with gram + bacteria which ferment starch, glucose, mannitol,
rahmnose, saccharose, amygdaline and arabinose
and do not ferment maltose, inositol and sorbitol.
5. A process according to any preceding claim,
wherein the enzymes are present as a mixture cons tituted by:
-
2.10-4 to 20/or cellulose having a titre of 250 l.U.
C1/g, - 0.05 to 0.2/oo bacterial amylase having a titre of
250 units/g,
- 0.10 to 0.2/oo fungic amylase having a titre of
5,000 units P.S. 50/9,
- 0.10 to 0.70'/or amyloglucosidase having a titre
of 200 unitsAG/g, - 0.05 to 0.200/, hemicellulolytic complex having a
titre of 35,000 l.U./g, the percentage values being expressed by weight with reference to the ensilaged vegetables.
6. A process according to any one of the preceding claims, wherein the enzymes are present and are incorporated on a cereal support in a proportion of about 1 kg enzymes per 9 kg support.
7. A process according to any one of the preceding claims, wherein the bacteria are present and are cultivated on a support comprising cereal wheats.
8. A process according to any one of claims 1 to 5, wherein the bacteria and the enzymes are present and are incorporated on a support of the cereal starch type, pregelated starch type, malto-hexose type, which is soluble in cold water, in a proportion of 1 kg bacteria and enzymes per 1.5 to 4 kg support.
9. A process according to one of the preceding claims wherein the amount of enzymes and bacterial culture with their support, in the dry state, added per ton of vegetables to be ensilated is 10 to 15 kg, this additive containing 105 to 10off live germs per gramme.
10. A composition for preserving and valorizing fresh vegetables which comprises lactic acidproducing bacteria strains and a degradation agent capable of degrading higher glucides into fermentable glucides constituted by an enzymes complex and/or bacteria, wherein the enzymes if present comprise, possibly in association with fungic amylase, amyloglucosidase, a hemicellulolytic complex of fungic origin having primarily a galactomannanasic activity, a cellulase orcellulolytic complex of fungic origin, capable of degrading the native cellulose into glucose and having a C1 activity of 50 to 0.005 International Units and a Cx activity of 500 to 0.05 International Units for 100 grammes of fresh vegetables and retained under the prevailing ensilaging conditions at least 30% of said activity after 10 days, said bacteria if present, being grambacteria which initiate starch fermentation but do not ferment maltose, belonging to the family of
Enterobacteriaceae, type Erwinia or Pectobacterium, group Herbicola, named EnterobacterAgglomerans.
11. A composition according to claim 9, wherein the Enterobacteriaceae gram-bacteria are present and are associated with bacteria capable of degrading the higher glucides into fermentable sugars, and especially gram + bacteria which ferment the starch, glucose, mannitol, rahmnose saccharose, and amygdaline, arabinose, and do not ferment maltose, inositol and sorbitol.
12. A process of preserving and valorizing fresh vegetable matter by lactic acidification, as claimed in claim 1 and substantially as hereinbefore described, with reference to any one of runs B and B' of Test 1, run B of Test 2, and run D of the Examples.
13. A composition for preserving valorizing fresh vegetable matter, as claimed in claim 10 and substantially as hereinbefore described with reference to any one of runs B and B' of Test 1, run B of Test 2 and run D of the Examples.
14. Vegetable matter when treated buy a process according to any of claims 1 to 9 and 12 or by means of a composition, according to any of claims 10,11 and 13.
15. An animal fed upon vegetable matter as claimed in claim 14.
16. The features hereinbefore disclosed, or their equivalents, in any novel selection.
New claims or amendments to claims filed on 28
July 1980.
Superseded claims 1.
Applications Claiming Priority (2)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
FR7903499A FR2448299A2 (en) | 1979-02-12 | 1979-02-12 | Ensilage using added cellulase(s) - esp. by fermentation of Enterobacter agglomerans |
FR7915887A FR2459006A2 (en) | 1979-06-21 | 1979-06-21 | Ensilage using added cellulase(s) - esp. by fermentation of Enterobacter agglomerans |
Publications (2)
Publication Number | Publication Date |
---|---|
GB2046567A true GB2046567A (en) | 1980-11-19 |
GB2046567B GB2046567B (en) | 1983-11-30 |
Family
ID=26221011
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
GB8004578A Expired GB2046567B (en) | 1979-02-12 | 1980-02-12 | Ensilaging vegetable matter |
Country Status (21)
Country | Link |
---|---|
AR (1) | AR219435A1 (en) |
AT (1) | AT368842B (en) |
AU (1) | AU537458B2 (en) |
BG (1) | BG48331A3 (en) |
CA (1) | CA1127101A (en) |
CH (1) | CH643988A5 (en) |
DD (1) | DD149015A6 (en) |
DE (1) | DE3005020A1 (en) |
DK (1) | DK57980A (en) |
ES (1) | ES488462A2 (en) |
GB (1) | GB2046567B (en) |
GR (1) | GR74002B (en) |
HU (1) | HU185784B (en) |
IT (1) | IT1212401B (en) |
LU (1) | LU82150A1 (en) |
NL (1) | NL8000876A (en) |
PL (1) | PL122629B1 (en) |
PT (1) | PT70817A (en) |
RO (1) | RO85921B (en) |
SE (1) | SE452244B (en) |
YU (1) | YU43215B (en) |
Cited By (5)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
GB2159388A (en) * | 1984-06-01 | 1985-12-04 | Pan Britannica Ind Ltd | Preservation of silage |
US4751089A (en) * | 1982-11-02 | 1988-06-14 | Suomen Sokeri Oy | Composition and method for ensilaging fodder and grain |
WO1993020714A1 (en) * | 1992-04-10 | 1993-10-28 | Finnfeeds International Ltd. | Enzyme products for use in the improvement of feed value and conservation of fibrous crops |
WO1998016651A1 (en) * | 1996-10-17 | 1998-04-23 | Wisconsin Alumni Research Foundation | Transgenic plants as an alternative source of lignocellulosic-degrading enzymes |
US6818803B1 (en) | 1997-06-26 | 2004-11-16 | Wisconsin Alumni Research Foundation | Transgenic plants as an alternative source of lignocellulosic-degrading enzymes |
Families Citing this family (2)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
DE3916563A1 (en) * | 1989-05-20 | 1990-11-22 | Atochem Werke Gmbh | COMBINATION DEVICE AND METHOD FOR ACIDIFYING GREEN FORAGE AND PREVENTING AEROBIC DEGRADING PROCESSES IN GAERFUTTER |
WO1991015966A1 (en) * | 1990-04-18 | 1991-10-31 | Ssv-Development Oy | Enzyme treated forage for silage |
Family Cites Families (5)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
SE302239B (en) * | 1960-03-29 | 1968-07-08 | N Nilsson | |
IT1109471B (en) * | 1976-08-17 | 1985-12-16 | Deral Sa | PROCEDURE AND PRODUCT FOR THE PRESERVATION AND ENHANCEMENT OF GREEN VEGETABLES AND OF THE WET PRODUCTS UNDER AGRO-FOOD INDUSTRIES |
FR2361828A1 (en) * | 1976-08-17 | 1978-03-17 | Deral Sa | Silaging process for plants for animal feeds - by adding to lactic fermentation a factor for breaking down higher glucides |
FR2390908A2 (en) * | 1977-05-18 | 1978-12-15 | Deral Sa | Silaging process for plants for animal feeds - by adding to lactic fermentation a factor for breaking down higher glucides |
GB1547063A (en) * | 1977-07-07 | 1979-06-06 | Salen Interdevelop Ab | Process for the biological ensiling of vegetable and/or animals materials |
-
1980
- 1980-02-08 GR GR61164A patent/GR74002B/el unknown
- 1980-02-08 HU HU80293A patent/HU185784B/en unknown
- 1980-02-11 DK DK57980A patent/DK57980A/en not_active Application Discontinuation
- 1980-02-11 AR AR279921A patent/AR219435A1/en active
- 1980-02-11 SE SE8001062A patent/SE452244B/en not_active IP Right Cessation
- 1980-02-11 YU YU349/80A patent/YU43215B/en unknown
- 1980-02-11 LU LU82150A patent/LU82150A1/en unknown
- 1980-02-11 IT IT8019844A patent/IT1212401B/en active
- 1980-02-11 DD DD80218995A patent/DD149015A6/en not_active IP Right Cessation
- 1980-02-11 DE DE19803005020 patent/DE3005020A1/en active Granted
- 1980-02-11 CA CA345,395A patent/CA1127101A/en not_active Expired
- 1980-02-11 ES ES488462A patent/ES488462A2/en not_active Expired
- 1980-02-11 BG BG46562A patent/BG48331A3/en unknown
- 1980-02-11 PL PL1980221935A patent/PL122629B1/en unknown
- 1980-02-11 AU AU55412/80A patent/AU537458B2/en not_active Expired
- 1980-02-11 CH CH111280A patent/CH643988A5/en not_active IP Right Cessation
- 1980-02-11 PT PT70817A patent/PT70817A/en not_active IP Right Cessation
- 1980-02-12 NL NL8000876A patent/NL8000876A/en not_active Application Discontinuation
- 1980-02-12 AT AT0074580A patent/AT368842B/en not_active IP Right Cessation
- 1980-02-12 RO RO100155A patent/RO85921B/en unknown
- 1980-02-12 GB GB8004578A patent/GB2046567B/en not_active Expired
Cited By (6)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US4751089A (en) * | 1982-11-02 | 1988-06-14 | Suomen Sokeri Oy | Composition and method for ensilaging fodder and grain |
GB2159388A (en) * | 1984-06-01 | 1985-12-04 | Pan Britannica Ind Ltd | Preservation of silage |
WO1993020714A1 (en) * | 1992-04-10 | 1993-10-28 | Finnfeeds International Ltd. | Enzyme products for use in the improvement of feed value and conservation of fibrous crops |
US5948454A (en) * | 1992-04-10 | 1999-09-07 | Ssv Development Oy | Method for treatment of fibrous crops with a modified cellulase to improve feed values storage and other properties |
WO1998016651A1 (en) * | 1996-10-17 | 1998-04-23 | Wisconsin Alumni Research Foundation | Transgenic plants as an alternative source of lignocellulosic-degrading enzymes |
US6818803B1 (en) | 1997-06-26 | 2004-11-16 | Wisconsin Alumni Research Foundation | Transgenic plants as an alternative source of lignocellulosic-degrading enzymes |
Also Published As
Publication number | Publication date |
---|---|
HU185784B (en) | 1985-03-28 |
DD149015A6 (en) | 1981-06-24 |
PL221935A3 (en) | 1980-10-20 |
CH643988A5 (en) | 1984-07-13 |
PL122629B1 (en) | 1982-08-31 |
AT368842B (en) | 1982-11-10 |
IT1212401B (en) | 1989-11-22 |
GB2046567B (en) | 1983-11-30 |
YU34980A (en) | 1983-02-28 |
PT70817A (en) | 1980-03-01 |
GR74002B (en) | 1984-06-06 |
DE3005020C2 (en) | 1991-08-01 |
DK57980A (en) | 1980-08-13 |
RO85921A (en) | 1985-01-24 |
CA1127101A (en) | 1982-07-06 |
ATA74580A (en) | 1982-04-15 |
DE3005020A1 (en) | 1980-08-28 |
AU5541280A (en) | 1980-08-21 |
IT8019844A0 (en) | 1980-02-11 |
YU43215B (en) | 1989-06-30 |
AR219435A1 (en) | 1980-08-15 |
NL8000876A (en) | 1980-08-14 |
SE8001062L (en) | 1980-08-13 |
LU82150A1 (en) | 1980-05-07 |
AU537458B2 (en) | 1984-06-28 |
SE452244B (en) | 1987-11-23 |
ES488462A2 (en) | 1980-10-01 |
BG48331A3 (en) | 1991-01-15 |
RO85921B (en) | 1985-01-30 |
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Legal Events
Date | Code | Title | Description |
---|---|---|---|
PCNP | Patent ceased through non-payment of renewal fee |
Effective date: 19940212 |