CN107846944A - Edible meat modifying agent - Google Patents
Edible meat modifying agent Download PDFInfo
- Publication number
- CN107846944A CN107846944A CN201680042880.6A CN201680042880A CN107846944A CN 107846944 A CN107846944 A CN 107846944A CN 201680042880 A CN201680042880 A CN 201680042880A CN 107846944 A CN107846944 A CN 107846944A
- Authority
- CN
- China
- Prior art keywords
- protease
- edible meat
- yeast containing
- yeast
- containing metal
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Granted
Links
- 235000013372 meat Nutrition 0.000 title claims abstract description 179
- 108091005804 Peptidases Proteins 0.000 claims abstract description 183
- 239000004365 Protease Substances 0.000 claims abstract description 177
- 240000004808 Saccharomyces cerevisiae Species 0.000 claims abstract description 175
- 229910052751 metal Inorganic materials 0.000 claims abstract description 126
- 239000002184 metal Substances 0.000 claims abstract description 126
- 241000193830 Bacillus <bacterium> Species 0.000 claims abstract description 42
- 241000228212 Aspergillus Species 0.000 claims abstract description 34
- 210000003205 muscle Anatomy 0.000 claims abstract description 34
- 241000894006 Bacteria Species 0.000 claims abstract description 14
- 230000006872 improvement Effects 0.000 claims abstract description 14
- 241000233866 Fungi Species 0.000 claims abstract description 11
- 238000012545 processing Methods 0.000 claims abstract description 10
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 claims abstract 22
- 102000008186 Collagen Human genes 0.000 claims description 87
- 108010035532 Collagen Proteins 0.000 claims description 87
- 229920001436 collagen Polymers 0.000 claims description 86
- 238000000034 method Methods 0.000 claims description 84
- 238000003776 cleavage reaction Methods 0.000 claims description 65
- 230000007017 scission Effects 0.000 claims description 65
- 230000000694 effects Effects 0.000 claims description 52
- 102000004190 Enzymes Human genes 0.000 claims description 47
- 108090000790 Enzymes Proteins 0.000 claims description 47
- 239000003795 chemical substances by application Substances 0.000 claims description 44
- 108090000623 proteins and genes Proteins 0.000 claims description 42
- 102000004169 proteins and genes Human genes 0.000 claims description 38
- 239000011572 manganese Substances 0.000 claims description 27
- PWHULOQIROXLJO-UHFFFAOYSA-N Manganese Chemical compound [Mn] PWHULOQIROXLJO-UHFFFAOYSA-N 0.000 claims description 24
- 229910052748 manganese Inorganic materials 0.000 claims description 24
- XEEYBQQBJWHFJM-UHFFFAOYSA-N Iron Chemical compound [Fe] XEEYBQQBJWHFJM-UHFFFAOYSA-N 0.000 claims description 18
- 238000004519 manufacturing process Methods 0.000 claims description 16
- WPBNNNQJVZRUHP-UHFFFAOYSA-L manganese(2+);methyl n-[[2-(methoxycarbonylcarbamothioylamino)phenyl]carbamothioyl]carbamate;n-[2-(sulfidocarbothioylamino)ethyl]carbamodithioate Chemical compound [Mn+2].[S-]C(=S)NCCNC([S-])=S.COC(=O)NC(=S)NC1=CC=CC=C1NC(=S)NC(=O)OC WPBNNNQJVZRUHP-UHFFFAOYSA-L 0.000 claims description 14
- FYYHWMGAXLPEAU-UHFFFAOYSA-N Magnesium Chemical compound [Mg] FYYHWMGAXLPEAU-UHFFFAOYSA-N 0.000 claims description 9
- HCHKCACWOHOZIP-UHFFFAOYSA-N Zinc Chemical compound [Zn] HCHKCACWOHOZIP-UHFFFAOYSA-N 0.000 claims description 9
- 229910052742 iron Inorganic materials 0.000 claims description 9
- 229910052749 magnesium Inorganic materials 0.000 claims description 9
- 239000011777 magnesium Substances 0.000 claims description 9
- 239000011701 zinc Substances 0.000 claims description 9
- 229910052725 zinc Inorganic materials 0.000 claims description 9
- 239000004902 Softening Agent Substances 0.000 claims description 8
- 238000000354 decomposition reaction Methods 0.000 claims description 8
- PCHJSUWPFVWCPO-UHFFFAOYSA-N gold Chemical compound [Au] PCHJSUWPFVWCPO-UHFFFAOYSA-N 0.000 claims description 2
- 229910052737 gold Inorganic materials 0.000 claims description 2
- 239000010931 gold Substances 0.000 claims description 2
- 102000035195 Peptidases Human genes 0.000 description 161
- 235000014680 Saccharomyces cerevisiae Nutrition 0.000 description 149
- 235000019419 proteases Nutrition 0.000 description 141
- 229940088598 enzyme Drugs 0.000 description 45
- 235000018102 proteins Nutrition 0.000 description 37
- 239000004480 active ingredient Substances 0.000 description 29
- 239000000243 solution Substances 0.000 description 27
- 239000000203 mixture Substances 0.000 description 24
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 24
- 230000000593 degrading effect Effects 0.000 description 17
- 238000010828 elution Methods 0.000 description 15
- 238000010438 heat treatment Methods 0.000 description 13
- 239000000725 suspension Substances 0.000 description 12
- 238000010411 cooking Methods 0.000 description 11
- 238000006911 enzymatic reaction Methods 0.000 description 11
- 244000005700 microbiome Species 0.000 description 11
- 239000012085 test solution Substances 0.000 description 11
- 240000006439 Aspergillus oryzae Species 0.000 description 10
- 235000002247 Aspergillus oryzae Nutrition 0.000 description 10
- 244000063299 Bacillus subtilis Species 0.000 description 10
- 235000014469 Bacillus subtilis Nutrition 0.000 description 10
- 239000012153 distilled water Substances 0.000 description 10
- 230000008569 process Effects 0.000 description 10
- KRKNYBCHXYNGOX-UHFFFAOYSA-N citric acid Chemical compound OC(=O)CC(O)(C(O)=O)CC(O)=O KRKNYBCHXYNGOX-UHFFFAOYSA-N 0.000 description 9
- 235000013601 eggs Nutrition 0.000 description 9
- 235000019833 protease Nutrition 0.000 description 9
- 239000006228 supernatant Substances 0.000 description 9
- 241000228245 Aspergillus niger Species 0.000 description 8
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 8
- 239000007788 liquid Substances 0.000 description 8
- 235000009467 Carica papaya Nutrition 0.000 description 7
- 241000894007 species Species 0.000 description 7
- 239000000126 substance Substances 0.000 description 7
- 239000000758 substrate Substances 0.000 description 7
- GHCZTIFQWKKGSB-UHFFFAOYSA-N 2-hydroxypropane-1,2,3-tricarboxylic acid;phosphoric acid Chemical class OP(O)(O)=O.OC(=O)CC(O)(C(O)=O)CC(O)=O GHCZTIFQWKKGSB-UHFFFAOYSA-N 0.000 description 6
- 241000193744 Bacillus amyloliquefaciens Species 0.000 description 6
- 238000011156 evaluation Methods 0.000 description 6
- 235000020138 yakult Nutrition 0.000 description 6
- 241000194110 Bacillus sp. (in: Bacteria) Species 0.000 description 5
- 101000693530 Staphylococcus aureus Staphylokinase Proteins 0.000 description 5
- 238000002835 absorbance Methods 0.000 description 5
- 239000003513 alkali Substances 0.000 description 5
- 210000002808 connective tissue Anatomy 0.000 description 5
- 238000001816 cooling Methods 0.000 description 5
- 235000013305 food Nutrition 0.000 description 5
- 239000000843 powder Substances 0.000 description 5
- 239000000047 product Substances 0.000 description 5
- 239000002994 raw material Substances 0.000 description 5
- 241000228257 Aspergillus sp. Species 0.000 description 4
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 4
- 241000194108 Bacillus licheniformis Species 0.000 description 4
- 241000222120 Candida <Saccharomycetales> Species 0.000 description 4
- 241000219173 Carica Species 0.000 description 4
- ISWSIDIOOBJBQZ-UHFFFAOYSA-N Phenol Chemical compound OC1=CC=CC=C1 ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 description 4
- 239000007864 aqueous solution Substances 0.000 description 4
- 210000004556 brain Anatomy 0.000 description 4
- 239000005018 casein Substances 0.000 description 4
- BECPQYXYKAMYBN-UHFFFAOYSA-N casein, tech. Chemical compound NCCCCC(C(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(CC(C)C)N=C(O)C(CCC(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(C(C)O)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(COP(O)(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(N)CC1=CC=CC=C1 BECPQYXYKAMYBN-UHFFFAOYSA-N 0.000 description 4
- 235000021240 caseins Nutrition 0.000 description 4
- 230000002301 combined effect Effects 0.000 description 4
- 238000002156 mixing Methods 0.000 description 4
- 239000008363 phosphate buffer Substances 0.000 description 4
- 230000035484 reaction time Effects 0.000 description 4
- 239000011780 sodium chloride Substances 0.000 description 4
- 235000013547 stew Nutrition 0.000 description 4
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 3
- 241000251468 Actinopterygii Species 0.000 description 3
- 241000981399 Aspergillus melleus Species 0.000 description 3
- 240000006432 Carica papaya Species 0.000 description 3
- 241000193385 Geobacillus stearothermophilus Species 0.000 description 3
- 108010006035 Metalloproteases Proteins 0.000 description 3
- 102000005741 Metalloproteases Human genes 0.000 description 3
- 108090000526 Papain Proteins 0.000 description 3
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 3
- 108010056079 Subtilisins Proteins 0.000 description 3
- 102000005158 Subtilisins Human genes 0.000 description 3
- 108090001109 Thermolysin Proteins 0.000 description 3
- 239000002253 acid Substances 0.000 description 3
- 235000015278 beef Nutrition 0.000 description 3
- 238000006243 chemical reaction Methods 0.000 description 3
- BNIILDVGGAEEIG-UHFFFAOYSA-L disodium hydrogen phosphate Chemical compound [Na+].[Na+].OP([O-])([O-])=O BNIILDVGGAEEIG-UHFFFAOYSA-L 0.000 description 3
- 235000013399 edible fruits Nutrition 0.000 description 3
- 238000005516 engineering process Methods 0.000 description 3
- 238000002474 experimental method Methods 0.000 description 3
- 235000019688 fish Nutrition 0.000 description 3
- 239000003292 glue Substances 0.000 description 3
- 235000019629 palatability Nutrition 0.000 description 3
- 235000019834 papain Nutrition 0.000 description 3
- 229940055729 papain Drugs 0.000 description 3
- 235000013594 poultry meat Nutrition 0.000 description 3
- 238000001556 precipitation Methods 0.000 description 3
- 235000020989 red meat Nutrition 0.000 description 3
- 150000003839 salts Chemical class 0.000 description 3
- 238000009461 vacuum packaging Methods 0.000 description 3
- QCVGEOXPDFCNHA-UHFFFAOYSA-N 5,5-dimethyl-2,4-dioxo-1,3-oxazolidine-3-carboxamide Chemical compound CC1(C)OC(=O)N(C(N)=O)C1=O QCVGEOXPDFCNHA-UHFFFAOYSA-N 0.000 description 2
- FRXSZNDVFUDTIR-UHFFFAOYSA-N 6-methoxy-1,2,3,4-tetrahydroquinoline Chemical compound N1CCCC2=CC(OC)=CC=C21 FRXSZNDVFUDTIR-UHFFFAOYSA-N 0.000 description 2
- 244000099147 Ananas comosus Species 0.000 description 2
- 235000007119 Ananas comosus Nutrition 0.000 description 2
- 102000035101 Aspartic proteases Human genes 0.000 description 2
- 108091005502 Aspartic proteases Proteins 0.000 description 2
- 241001225321 Aspergillus fumigatus Species 0.000 description 2
- 241000131386 Aspergillus sojae Species 0.000 description 2
- 241000193755 Bacillus cereus Species 0.000 description 2
- 241001328122 Bacillus clausii Species 0.000 description 2
- 241000193422 Bacillus lentus Species 0.000 description 2
- 241000726108 Blastocystis Species 0.000 description 2
- 108091006146 Channels Proteins 0.000 description 2
- VYZAMTAEIAYCRO-UHFFFAOYSA-N Chromium Chemical compound [Cr] VYZAMTAEIAYCRO-UHFFFAOYSA-N 0.000 description 2
- 241000235646 Cyberlindnera jadinii Species 0.000 description 2
- 102000002322 Egg Proteins Human genes 0.000 description 2
- 108010000912 Egg Proteins Proteins 0.000 description 2
- 108010068370 Glutens Proteins 0.000 description 2
- ZOKXTWBITQBERF-UHFFFAOYSA-N Molybdenum Chemical compound [Mo] ZOKXTWBITQBERF-UHFFFAOYSA-N 0.000 description 2
- 241001494479 Pecora Species 0.000 description 2
- 241000235070 Saccharomyces Species 0.000 description 2
- 241000235346 Schizosaccharomyces Species 0.000 description 2
- 241000235347 Schizosaccharomyces pombe Species 0.000 description 2
- BUGBHKTXTAQXES-UHFFFAOYSA-N Selenium Chemical compound [Se] BUGBHKTXTAQXES-UHFFFAOYSA-N 0.000 description 2
- 108010022999 Serine Proteases Proteins 0.000 description 2
- 102000012479 Serine Proteases Human genes 0.000 description 2
- CDBYLPFSWZWCQE-UHFFFAOYSA-L Sodium Carbonate Chemical compound [Na+].[Na+].[O-]C([O-])=O CDBYLPFSWZWCQE-UHFFFAOYSA-L 0.000 description 2
- 229920002472 Starch Polymers 0.000 description 2
- 108090000787 Subtilisin Proteins 0.000 description 2
- 150000001413 amino acids Chemical group 0.000 description 2
- 229940091771 aspergillus fumigatus Drugs 0.000 description 2
- 239000002585 base Substances 0.000 description 2
- 230000003139 buffering effect Effects 0.000 description 2
- 239000003153 chemical reaction reagent Substances 0.000 description 2
- 229910052804 chromium Inorganic materials 0.000 description 2
- 239000011651 chromium Substances 0.000 description 2
- 229910017052 cobalt Inorganic materials 0.000 description 2
- 239000010941 cobalt Substances 0.000 description 2
- GUTLYIVDDKVIGB-UHFFFAOYSA-N cobalt atom Chemical compound [Co] GUTLYIVDDKVIGB-UHFFFAOYSA-N 0.000 description 2
- 238000010790 dilution Methods 0.000 description 2
- 239000012895 dilution Substances 0.000 description 2
- 235000014103 egg white Nutrition 0.000 description 2
- 210000000969 egg white Anatomy 0.000 description 2
- 239000003995 emulsifying agent Substances 0.000 description 2
- 239000000706 filtrate Substances 0.000 description 2
- -1 for example Substances 0.000 description 2
- 235000015220 hamburgers Nutrition 0.000 description 2
- PNDPGZBMCMUPRI-UHFFFAOYSA-N iodine Chemical compound II PNDPGZBMCMUPRI-UHFFFAOYSA-N 0.000 description 2
- NUJOXMJBOLGQSY-UHFFFAOYSA-N manganese dioxide Chemical compound O=[Mn]=O NUJOXMJBOLGQSY-UHFFFAOYSA-N 0.000 description 2
- 239000000463 material Substances 0.000 description 2
- 229910052750 molybdenum Inorganic materials 0.000 description 2
- 239000011733 molybdenum Substances 0.000 description 2
- 229910052757 nitrogen Inorganic materials 0.000 description 2
- 235000011837 pasties Nutrition 0.000 description 2
- 238000002360 preparation method Methods 0.000 description 2
- 229910052711 selenium Inorganic materials 0.000 description 2
- 239000011669 selenium Substances 0.000 description 2
- 239000011734 sodium Substances 0.000 description 2
- 235000014347 soups Nutrition 0.000 description 2
- 235000019698 starch Nutrition 0.000 description 2
- 239000008107 starch Substances 0.000 description 2
- 238000012360 testing method Methods 0.000 description 2
- ILJSQTXMGCGYMG-UHFFFAOYSA-N triacetic acid Chemical compound CC(=O)CC(=O)CC(O)=O ILJSQTXMGCGYMG-UHFFFAOYSA-N 0.000 description 2
- YNJBWRMUSHSURL-UHFFFAOYSA-N trichloroacetic acid Chemical compound OC(=O)C(Cl)(Cl)Cl YNJBWRMUSHSURL-UHFFFAOYSA-N 0.000 description 2
- 229910052720 vanadium Inorganic materials 0.000 description 2
- LEONUFNNVUYDNQ-UHFFFAOYSA-N vanadium atom Chemical compound [V] LEONUFNNVUYDNQ-UHFFFAOYSA-N 0.000 description 2
- 210000004885 white matter Anatomy 0.000 description 2
- LDVVTQMJQSCDMK-UHFFFAOYSA-N 1,3-dihydroxypropan-2-yl formate Chemical compound OCC(CO)OC=O LDVVTQMJQSCDMK-UHFFFAOYSA-N 0.000 description 1
- WURBVZBTWMNKQT-UHFFFAOYSA-N 1-(4-chlorophenoxy)-3,3-dimethyl-1-(1,2,4-triazol-1-yl)butan-2-one Chemical compound C1=NC=NN1C(C(=O)C(C)(C)C)OC1=CC=C(Cl)C=C1 WURBVZBTWMNKQT-UHFFFAOYSA-N 0.000 description 1
- 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 description 1
- QGBLCIBATKETJC-UHFFFAOYSA-N 3,7-dioxido-2,4,6,8,9-pentaoxa-1,3,5,7-tetraborabicyclo[3.3.1]nonane;manganese(2+) Chemical compound [Mn+2].O1B([O-])OB2OB([O-])OB1O2 QGBLCIBATKETJC-UHFFFAOYSA-N 0.000 description 1
- 108091005508 Acid proteases Proteins 0.000 description 1
- 101800000263 Acidic protein Proteins 0.000 description 1
- 244000298715 Actinidia chinensis Species 0.000 description 1
- 235000009434 Actinidia chinensis Nutrition 0.000 description 1
- 235000009436 Actinidia deliciosa Nutrition 0.000 description 1
- ZHQQRIUYLMXDPP-SSDOTTSWSA-N Actinidine Natural products C1=NC=C(C)C2=C1[C@H](C)CC2 ZHQQRIUYLMXDPP-SSDOTTSWSA-N 0.000 description 1
- 244000144730 Amygdalus persica Species 0.000 description 1
- 241000272525 Anas platyrhynchos Species 0.000 description 1
- 241000272814 Anser sp. Species 0.000 description 1
- 101000577180 Aspergillus oryzae (strain ATCC 42149 / RIB 40) Neutral protease 2 Proteins 0.000 description 1
- 241000972773 Aulopiformes Species 0.000 description 1
- 241000194102 Bacillus intermedius Species 0.000 description 1
- 241000193389 Bacillus thermoproteolyticus Species 0.000 description 1
- 235000017166 Bambusa arundinacea Nutrition 0.000 description 1
- 235000017491 Bambusa tulda Nutrition 0.000 description 1
- 108010004032 Bromelains Proteins 0.000 description 1
- OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 description 1
- 241000282693 Cercopithecidae Species 0.000 description 1
- KRKNYBCHXYNGOX-UHFFFAOYSA-K Citrate Chemical compound [O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O KRKNYBCHXYNGOX-UHFFFAOYSA-K 0.000 description 1
- 102000029816 Collagenase Human genes 0.000 description 1
- 108060005980 Collagenase Proteins 0.000 description 1
- 241001149724 Cololabis adocetus Species 0.000 description 1
- 235000000423 Convallaria keiskei Nutrition 0.000 description 1
- 240000007938 Convallaria keiskei Species 0.000 description 1
- RYGMFSIKBFXOCR-UHFFFAOYSA-N Copper Chemical compound [Cu] RYGMFSIKBFXOCR-UHFFFAOYSA-N 0.000 description 1
- 229920001353 Dextrin Polymers 0.000 description 1
- 239000004375 Dextrin Substances 0.000 description 1
- 102000016942 Elastin Human genes 0.000 description 1
- 108010014258 Elastin Proteins 0.000 description 1
- 241000196324 Embryophyta Species 0.000 description 1
- 241000276438 Gadus morhua Species 0.000 description 1
- 241000287828 Gallus gallus Species 0.000 description 1
- 101001091385 Homo sapiens Kallikrein-6 Proteins 0.000 description 1
- DGAQECJNVWCQMB-PUAWFVPOSA-M Ilexoside XXIX Chemical compound C[C@@H]1CC[C@@]2(CC[C@@]3(C(=CC[C@H]4[C@]3(CC[C@@H]5[C@@]4(CC[C@@H](C5(C)C)OS(=O)(=O)[O-])C)C)[C@@H]2[C@]1(C)O)C)C(=O)O[C@H]6[C@@H]([C@H]([C@@H]([C@H](O6)CO)O)O)O.[Na+] DGAQECJNVWCQMB-PUAWFVPOSA-M 0.000 description 1
- 102100034866 Kallikrein-6 Human genes 0.000 description 1
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 1
- 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 description 1
- 229910021380 Manganese Chloride Inorganic materials 0.000 description 1
- GLFNIEUTAYBVOC-UHFFFAOYSA-L Manganese chloride Chemical compound Cl[Mn]Cl GLFNIEUTAYBVOC-UHFFFAOYSA-L 0.000 description 1
- 239000012901 Milli-Q water Substances 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- 244000082204 Phyllostachys viridis Species 0.000 description 1
- 235000015334 Phyllostachys viridis Nutrition 0.000 description 1
- 241000269978 Pleuronectiformes Species 0.000 description 1
- 241000932075 Priacanthus hamrur Species 0.000 description 1
- 101710180012 Protease 7 Proteins 0.000 description 1
- 108010009736 Protein Hydrolysates Proteins 0.000 description 1
- 235000006040 Prunus persica var persica Nutrition 0.000 description 1
- 241000235342 Saccharomycetes Species 0.000 description 1
- 241000187747 Streptomyces Species 0.000 description 1
- 241001655322 Streptomycetales Species 0.000 description 1
- 241000282898 Sus scrofa Species 0.000 description 1
- 241001441726 Tetraodontiformes Species 0.000 description 1
- BZHJMEDXRYGGRV-UHFFFAOYSA-N Vinyl chloride Chemical class ClC=C BZHJMEDXRYGGRV-UHFFFAOYSA-N 0.000 description 1
- HNIASRFAODUYDL-UHFFFAOYSA-N acetyl acetate;sodium Chemical compound [Na].CC(=O)OC(C)=O HNIASRFAODUYDL-UHFFFAOYSA-N 0.000 description 1
- ZHQQRIUYLMXDPP-ZETCQYMHSA-N actinidine Chemical compound C1=NC=C(C)C2=C1[C@@H](C)CC2 ZHQQRIUYLMXDPP-ZETCQYMHSA-N 0.000 description 1
- 230000009471 action Effects 0.000 description 1
- 239000000654 additive Substances 0.000 description 1
- 230000000996 additive effect Effects 0.000 description 1
- 230000032683 aging Effects 0.000 description 1
- 239000000783 alginic acid Substances 0.000 description 1
- 235000010443 alginic acid Nutrition 0.000 description 1
- 229920000615 alginic acid Polymers 0.000 description 1
- 229960001126 alginic acid Drugs 0.000 description 1
- 150000004781 alginic acids Chemical class 0.000 description 1
- 235000001014 amino acid Nutrition 0.000 description 1
- 239000012491 analyte Substances 0.000 description 1
- 239000011425 bamboo Substances 0.000 description 1
- 235000021168 barbecue Nutrition 0.000 description 1
- 235000021028 berry Nutrition 0.000 description 1
- 210000000481 breast Anatomy 0.000 description 1
- 238000009395 breeding Methods 0.000 description 1
- 230000001488 breeding effect Effects 0.000 description 1
- 235000019835 bromelain Nutrition 0.000 description 1
- 235000014121 butter Nutrition 0.000 description 1
- 239000011575 calcium Substances 0.000 description 1
- 229910052791 calcium Inorganic materials 0.000 description 1
- VSGNNIFQASZAOI-UHFFFAOYSA-L calcium acetate Chemical compound [Ca+2].CC([O-])=O.CC([O-])=O VSGNNIFQASZAOI-UHFFFAOYSA-L 0.000 description 1
- 239000001639 calcium acetate Substances 0.000 description 1
- 229960005147 calcium acetate Drugs 0.000 description 1
- 235000011092 calcium acetate Nutrition 0.000 description 1
- JDOLBYNWFIAOHO-UHFFFAOYSA-L calcium;sodium;acetate;chloride Chemical compound [Na+].[Cl-].[Ca+2].CC([O-])=O JDOLBYNWFIAOHO-UHFFFAOYSA-L 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 239000002738 chelating agent Substances 0.000 description 1
- 239000003638 chemical reducing agent Substances 0.000 description 1
- 238000005660 chlorination reaction Methods 0.000 description 1
- 210000000349 chromosome Anatomy 0.000 description 1
- 229960002424 collagenase Drugs 0.000 description 1
- 239000000470 constituent Substances 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- 239000010949 copper Substances 0.000 description 1
- 229910052802 copper Inorganic materials 0.000 description 1
- 239000012228 culture supernatant Substances 0.000 description 1
- 235000021438 curry Nutrition 0.000 description 1
- 235000018417 cysteine Nutrition 0.000 description 1
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 1
- 230000007423 decrease Effects 0.000 description 1
- 235000019425 dextrin Nutrition 0.000 description 1
- 235000005911 diet Nutrition 0.000 description 1
- 230000037213 diet Effects 0.000 description 1
- 235000014113 dietary fatty acids Nutrition 0.000 description 1
- CTNMMTCXUUFYAP-UHFFFAOYSA-L difluoromanganese Chemical compound F[Mn]F CTNMMTCXUUFYAP-UHFFFAOYSA-L 0.000 description 1
- 230000001079 digestive effect Effects 0.000 description 1
- 239000003814 drug Substances 0.000 description 1
- 229920002549 elastin Polymers 0.000 description 1
- 238000001704 evaporation Methods 0.000 description 1
- 230000008020 evaporation Effects 0.000 description 1
- 239000000284 extract Substances 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- 239000011536 extraction buffer Substances 0.000 description 1
- 235000019197 fats Nutrition 0.000 description 1
- 239000000194 fatty acid Substances 0.000 description 1
- 229930195729 fatty acid Natural products 0.000 description 1
- 102000005525 fibrillarin Human genes 0.000 description 1
- 108020002231 fibrillarin Proteins 0.000 description 1
- 238000010304 firing Methods 0.000 description 1
- 239000012530 fluid Substances 0.000 description 1
- 239000010200 folin Substances 0.000 description 1
- 239000003517 fume Substances 0.000 description 1
- 235000021312 gluten Nutrition 0.000 description 1
- 239000004519 grease Substances 0.000 description 1
- CPSYWNLKRDURMG-UHFFFAOYSA-L hydron;manganese(2+);phosphate Chemical compound [Mn+2].OP([O-])([O-])=O CPSYWNLKRDURMG-UHFFFAOYSA-L 0.000 description 1
- 229910052500 inorganic mineral Inorganic materials 0.000 description 1
- 238000011835 investigation Methods 0.000 description 1
- 150000002500 ions Chemical class 0.000 description 1
- 238000002386 leaching Methods 0.000 description 1
- 238000007443 liposuction Methods 0.000 description 1
- 210000004185 liver Anatomy 0.000 description 1
- 229940071125 manganese acetate Drugs 0.000 description 1
- 239000011656 manganese carbonate Substances 0.000 description 1
- 235000006748 manganese carbonate Nutrition 0.000 description 1
- 229940093474 manganese carbonate Drugs 0.000 description 1
- 239000011565 manganese chloride Substances 0.000 description 1
- 235000002867 manganese chloride Nutrition 0.000 description 1
- 229940099607 manganese chloride Drugs 0.000 description 1
- AMWRITDGCCNYAT-UHFFFAOYSA-L manganese oxide Inorganic materials [Mn].O[Mn]=O.O[Mn]=O AMWRITDGCCNYAT-UHFFFAOYSA-L 0.000 description 1
- UOGMEBQRZBEZQT-UHFFFAOYSA-L manganese(2+);diacetate Chemical compound [Mn+2].CC([O-])=O.CC([O-])=O UOGMEBQRZBEZQT-UHFFFAOYSA-L 0.000 description 1
- MIVBAHRSNUNMPP-UHFFFAOYSA-N manganese(2+);dinitrate Chemical compound [Mn+2].[O-][N+]([O-])=O.[O-][N+]([O-])=O MIVBAHRSNUNMPP-UHFFFAOYSA-N 0.000 description 1
- 229910000016 manganese(II) carbonate Inorganic materials 0.000 description 1
- XMWCXZJXESXBBY-UHFFFAOYSA-L manganese(ii) carbonate Chemical compound [Mn+2].[O-]C([O-])=O XMWCXZJXESXBBY-UHFFFAOYSA-L 0.000 description 1
- UMUKXUYHMLVFLM-UHFFFAOYSA-N manganese(ii) selenide Chemical compound [Mn+2].[Se-2] UMUKXUYHMLVFLM-UHFFFAOYSA-N 0.000 description 1
- KNLQKHUBPCXPQD-UHFFFAOYSA-N manganese;sulfuric acid Chemical compound [Mn].OS(O)(=O)=O KNLQKHUBPCXPQD-UHFFFAOYSA-N 0.000 description 1
- 108010003855 mesentericopeptidase Proteins 0.000 description 1
- 108010009355 microbial metalloproteinases Proteins 0.000 description 1
- 108010020132 microbial serine proteinases Proteins 0.000 description 1
- 235000010755 mineral Nutrition 0.000 description 1
- 239000011707 mineral Substances 0.000 description 1
- 238000002715 modification method Methods 0.000 description 1
- 230000007935 neutral effect Effects 0.000 description 1
- 150000007523 nucleic acids Chemical class 0.000 description 1
- 108020004707 nucleic acids Proteins 0.000 description 1
- 102000039446 nucleic acids Human genes 0.000 description 1
- 235000016709 nutrition Nutrition 0.000 description 1
- 230000035764 nutrition Effects 0.000 description 1
- 150000007524 organic acids Chemical class 0.000 description 1
- 235000019449 other food additives Nutrition 0.000 description 1
- 238000004806 packaging method and process Methods 0.000 description 1
- 239000000546 pharmaceutical excipient Substances 0.000 description 1
- 239000010452 phosphate Substances 0.000 description 1
- 235000021317 phosphate Nutrition 0.000 description 1
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 1
- IEQIEDJGQAUEQZ-UHFFFAOYSA-N phthalocyanine Chemical compound N1C(N=C2C3=CC=CC=C3C(N=C3C4=CC=CC=C4C(=N4)N3)=N2)=C(C=CC=C2)C2=C1N=C1C2=CC=CC=C2C4=N1 IEQIEDJGQAUEQZ-UHFFFAOYSA-N 0.000 description 1
- 230000000704 physical effect Effects 0.000 description 1
- 239000000049 pigment Substances 0.000 description 1
- 229920000728 polyester Polymers 0.000 description 1
- 239000012286 potassium permanganate Substances 0.000 description 1
- 244000144977 poultry Species 0.000 description 1
- 108090000765 processed proteins & peptides Proteins 0.000 description 1
- 108010043393 protease N Proteins 0.000 description 1
- 238000000751 protein extraction Methods 0.000 description 1
- 239000003531 protein hydrolysate Substances 0.000 description 1
- 230000007065 protein hydrolysis Effects 0.000 description 1
- 230000017854 proteolysis Effects 0.000 description 1
- 238000000746 purification Methods 0.000 description 1
- 238000011002 quantification Methods 0.000 description 1
- 230000001869 rapid Effects 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 235000019515 salmon Nutrition 0.000 description 1
- 238000007790 scraping Methods 0.000 description 1
- 230000001953 sensory effect Effects 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 238000004904 shortening Methods 0.000 description 1
- 229910052708 sodium Inorganic materials 0.000 description 1
- 229910000029 sodium carbonate Inorganic materials 0.000 description 1
- 235000013599 spices Nutrition 0.000 description 1
- 238000010025 steaming Methods 0.000 description 1
- 230000001954 sterilising effect Effects 0.000 description 1
- 238000004659 sterilization and disinfection Methods 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
- 239000004575 stone Substances 0.000 description 1
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 1
- 229910021642 ultra pure water Inorganic materials 0.000 description 1
- 239000012498 ultrapure water Substances 0.000 description 1
- 238000003805 vibration mixing Methods 0.000 description 1
Classifications
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
- A23L13/00—Meat products; Meat meal; Preparation or treatment thereof
-
- 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
- A23L13/00—Meat products; Meat meal; Preparation or treatment thereof
- A23L13/70—Tenderised or flavoured meat pieces; Macerating or marinating solutions specially adapted therefor
- A23L13/72—Tenderised or flavoured meat pieces; Macerating or marinating solutions specially adapted therefor using additives, e.g. by injection of solutions
- A23L13/74—Tenderised or flavoured meat pieces; Macerating or marinating solutions specially adapted therefor using additives, e.g. by injection of solutions using microorganisms or enzymes
Landscapes
- Life Sciences & Earth Sciences (AREA)
- Health & Medical Sciences (AREA)
- Nutrition Science (AREA)
- Chemical & Material Sciences (AREA)
- Engineering & Computer Science (AREA)
- Food Science & Technology (AREA)
- Polymers & Plastics (AREA)
- Microbiology (AREA)
- Meat, Egg Or Seafood Products (AREA)
Abstract
The present invention provides the means of the improvement of the edible meat of the softening of muscle portion position for realizing edible meat etc..Meat is eaten so as to improve edible meat by using the protease from bacillus (Bacillus) category bacterium or aspergillus (Aspergillus) category fungi and the yeast processing containing metal.
Description
Technical field
The present invention relates to the method for edible meat modifying agent, the manufacture method of edible meat processed goods and the edible meat of improvement.
Background technology
There is increased trend in the consumption of edible meat in the world, it is contemplated that demand also can be improved further from now on.As
One of major reason of palatability of edible meat is determined, can be enumerated " flexibility of meat ".In addition, soft meat is not only to palatability
Favorably, and soft meat is due to being easily chewed upon, thus also excellent in terms of edible easiness.Further, since digestive efficiency also on
Rise, thus it is also excellent in terms of nutrition intake.Especially, in each developed country of aging progress, moderately make meat soft
The demand of the edible meat modifying agent such as edible meat softening agent improve.
In the past, the method (patent document 1) for using protease as edible meat softening agent has been carried out.As usually used
Edible meat softening agent, can enumerate the papain from papaya, the bromelain from pineapple, the Mi from Kiwi berry
Monkey peach alkali etc. (patent document 2,3).However, when using these enzymes, following problems be present:The degree of unmanageable softening, by
In overbating and the meat of mouthfeel as similar liver.In addition, when using these enzymes, although can carry out based on muscle fibril
The decomposition at the red meat position of body, but the muscle portion position comprising the more connective tissue being made up of hard protein matter (collagen)
Softening is insufficient.
On the other hand, using alternatively decomposing to property the constituent i.e. collagen of connective tissue, elastin laminin
The Collagenase of enzyme, elastoser, the method mainly decompose the hard protein in meat, softened are also known
(patent document 4,5).However, when using these enzymes, following such problems be present:With above-mentioned papain, pineapple
Protease, actinidine are compared, it is difficult to manufacture and preparation;In order to hard protein be decomposed, it is necessary to substantial amounts of enzyme amount or long-time
Processing time;Even in increase enzyme amount or in the case of processing time, hard protein matter also can not be fully decomposed, softening is not filled
Divide (patent document 6).
As described above, there is the leeway of improvement in the edible meat improving technology for having used the edible meat of protease to soften etc..
Prior art literature
Patent document
[patent document 1] Japanese Unexamined Patent Publication 2007-319166 publications
[patent document 2] Japanese Unexamined Patent Publication 5-7476 publications
[patent document 3] Japanese Unexamined Patent Publication 5-252911 publications
[patent document 4] Japanese Unexamined Patent Publication 4-197156 publications
[patent document 5] Japanese Unexamined Patent Publication 5-276899 publications
[patent document 6] Japanese Unexamined Patent Publication 6-169729 publications.
The content of the invention
Invent problem to be solved
Like this, the method for the connective tissue softening one of preferentially made the main reason for as meat toughness is not yet established.Therefore,
By establishing this technology, so that the preferable improvement of various meat is possibly realized, following various advantages can be expected:Edible meat
The further raising of palatability, the shortening of cooking length of time is such to cook easy, and the physical property of low-quality meat improves, because hard
And the meat position that abandons or old ox effectively utilize etc. effectively applying flexibly for food resource.
Therefore, problem of the invention be the modification method that edible meat is provided and edible meat processed goods manufacture method, with
And the edible meat modifying agent of the above method can be suitably used for.The problem of the present invention is particularly preferably to provide and made as edible meat
One of connective tissue the softening of muscle portion position method and make the manufacture method for the edible meat processed goods that muscle portion position softens, Yi Jike
It is suitably used for the edible meat softening agent of the above method.
Means for solving the problems
Present inventor has performed further investigation, as a result finds, by and with from bacillus (Bacillus) category bacterium or song
The yeast containing metal such as the protease of mould (Aspergillus) category fungi and the yeast containing manganese, the collagen egg of protease can be improved
White specific cleavage ability, and the softening of the muscle portion position of edible meat can be promoted, so as to complete the present invention.
That is, the present invention can illustrate as described below.
[1] meat modifying agent is eaten, it contains protease and the yeast containing metal,
Aforementioned proteases are selected from the protease from bacillus (Bacillus) category bacterium and from aspergillus
(Aspergillus) the one kind or two or more protease in the protease of fungi is belonged to;
[2] the edible meat modifying agent according to [1], wherein, the foregoing yeast containing metal is selected from the yeast containing manganese, containing zinc
One kind or two or more yeast in the yeast of yeast, the yeast containing magnesium and iron content;
[3] the edible meat modifying agent according to [1] or [2], wherein, the foregoing yeast containing metal is the yeast containing manganese;
[4] according to the edible meat modifying agent any one of [1]~[3], wherein, aforementioned proteases are and with the ferment containing metal
Collagen specific cleavage ability when female is not relative to and with collagen specific cleavage energy during yeast containing metal
The ratio of power is (and with collagen specific cleavage ability during yeast containing metal/not and with glue during yeast containing metal
Former protein-specific capacity of decomposition) it is more than 1 protease;
[5] the edible meat modifying agent according to [4], wherein, aforementioned ratio is more than 1.1;
[6] the edible meat modifying agent according to any one of [1]~[5], wherein, relative to 1U aforementioned proteases, with metal
Gauge, contain 0.4 × 10-9~2.0 × 10-7The foregoing yeast containing metal of mol;
[7] the edible meat modifying agent according to any one of [1]~[6], it is edible meat muscle softening agent;
[8] manufacture method of meat processed goods is eaten, methods described includes being improved with the edible meat any one of [1]~[7]
The step of agent processing eats meat;
[9] manufacture method of meat processed goods is eaten, methods described includes eating meat with protease and the processing of the yeast containing metal,
Aforementioned proteases are selected from the protease from bacillus (Bacillus) category bacterium and from aspergillus
(Aspergillus) the one kind or two or more protease in the protease of fungi is belonged to;
[10] method according to [9], wherein, the foregoing yeast containing metal is selected from the yeast containing manganese, the yeast containing zinc, contained
One kind or two or more yeast in the yeast of magnesium and the yeast of iron content;
[11] method according to [9] or [10], wherein, the foregoing yeast containing metal is the yeast containing manganese;
[12] according to the method any one of [9]~[11], wherein, aforementioned proteases are and with during yeast containing metal
Collagen specific cleavage ability is not relative to and with the ratio of collagen specific cleavage ability during yeast containing metal
Rate (and with collagen specific cleavage ability during yeast containing metal/not and with collagen during yeast containing metal
Specific cleavage ability) it is more than 1 protease;
[13] method according to [12], wherein, aforementioned ratio is more than 1.1;
[14] method according to any one of [8]~[13], wherein, relative to 1U aforementioned proteases, with metal gauge, make
0.4×10-9~2.0 × 10-7The foregoing yeast effects containing metal of mol;
[15] method according to any one of [8]~[14], wherein, relative to the foregoing edible meat of 1g, make 0.1U to go forward
State albumen enzyme effect;
[16] method for improveing edible meat, methods described include being handled with the edible meat modifying agent any one of [1]~[7]
Edible meat;
[17] method for improveing edible meat, methods described include handling edible meat with protease and the yeast containing metal,
Aforementioned proteases are selected from the protease from bacillus (Bacillus) category bacterium and from aspergillus
(Aspergillus) the one kind or two or more protease in the protease of fungi is belonged to;
[18] according to the method described in [17], wherein, the foregoing yeast containing metal be selected from the yeast containing manganese, the yeast containing zinc,
Yeast containing magnesium and the one kind or two or more yeast in the yeast of iron content;
[19] method according to [17] or [18], wherein, the foregoing yeast containing metal is the yeast containing manganese;
[20] according to the method any one of [17]~[19], wherein, aforementioned proteases are and during with yeast containing metal
Collagen specific cleavage ability relative to not and with collagen specific cleavage ability during yeast containing metal
Ratio (and with collagen specific cleavage ability during yeast containing metal/not and with collagen egg during yeast containing metal
White specific cleavage ability) it is more than 1 protease;
[21] method according to [20], wherein, aforementioned ratio is more than 1.1;
[22] according to the method any one of [16]~[21], wherein, relative to 1U aforementioned proteases, with metal gauge,
Make 0.4 × 10-9~2.0 × 10-7The foregoing yeast effects containing metal of mol;
[23] method according to any one of [16]~[22], wherein, relative to the foregoing edible meat of 1g, make 0.1U to go forward
State albumen enzyme effect;
[24] method according to any one of [16]~[23], it is by the method for the muscle portion position softening of edible meat.
Brief description of the drawings
[Fig. 1] is represented by and with the yeast containing metal the collagen specific cleavage ability of protease brought
Improve the figure of effect.
Embodiment
The edible meat modifying agent of the > of < 1 present invention
The edible meat modifying agent of the present invention is the edible meat modifying agent of the yeast containing protease and containing metal.Hereinafter, also by egg
White enzyme and the yeast containing metal are referred to as " active ingredient ".
The edible meat modifying agent of the present invention can be used for the edible meat of improvement.As the improvement of edible meat, edible meat can be enumerated
Softening.As the softening of edible meat, the softening of the muscle portion position of edible meat can be enumerated.That is, edible meat modifying agent of the invention, such as
It can be edible meat softening agent, can be edible meat muscle softening agent specifically.
In the present invention, by being used in combination for protease and the yeast containing metal, so as to the situation phase using only protease
Than can obtain the effective effect for the improvement for eating meat.Also the effect is referred to as " combined effect ".As and with effect
Fruit, it can enumerate:The effect that the collagen specific cleavage ability of protease improves;It is edible based on protease to improve (promotion)
The effect of the softening of the muscle portion position of meat.That is, being used in combination by protease and the yeast containing metal, with the feelings using only protease
Condition is compared, for example, the flexibility of the muscle portion position of edible meat can be improved, can be reduced in order that the muscle portion position of edible meat softens and needed
Time, enzyme amount.
The edible meat modifying agent of the present invention contains protease.
So-called " protease ", refer to the enzyme of the peptide bond hydrolysis of protein.Also protease is referred to as proteolytic enzyme
(proteinase)。
Workable protease is selected from the protease from bacillus (Bacillus) category bacterium and come from the present invention
Aspergillus (Aspergillus) belongs to the protease of fungi.As long as protease comes from bacillus or aspergillus fungi,
It is not particularly limited.As bacillus, can enumerate for example:Bacillus amyloliquefaciens (Bacillus
Amyloliquefaciens), bacillus cereus (Bacillus cereus), Bacillus clausii (Bacillus
Clausii), middle bacillus (Bacillus intermedius), bacillus lentus (Bacillus lentus),
Clothing bacillus (Bacillus licheniformis), bacillus stearothermophilus (Bacillus
Stearothermophilus), bacillus subtilis (Bacillus subtilis) and thermophilic proteolysis bacillus
(Bacillus thermoproteolyticus).As aspergillus fungi, can enumerate for example:Aspergillus fumigatus (Aspergillus
Fumigatus), Aspergillus melleus (Aspergillus melleus), aspergillus niger (Aspergillus niger), aspergillus oryzae
(Aspergillus oryzae) and Aspergillus sojae (Aspergillus sojae).Protease for example can be acidic protein
Enzyme, neutral proteinase or alkali protease.In addition, protease for example can be aspartic protease, serine protease,
Or metalloproteinases.As the protease from bacillus, such as subtilopeptidase A can be enumerated
(subtilisin;EC 3.4.21.62;Also referred to as PROTIN, Bioprase (PVC オ プ ラ ー ゼ), Alcalase etc.) etc. silk
Serine protease, thermolysin (thermolysin;EC 3.4.24.27) etc. metalloproteinases
(metalloprotease), other various acid, neutral or alkalescence protease.As the albumen from aspergillus fungi
Enzyme, the aspartic proteases such as the alkali proteases such as the neutral proteinase such as NPI, NPII, ALP, PEPO (acid egg can be enumerated
White enzyme).
As the protease from bacillus, specifically, for example following protease can be enumerated,
As neutral proteinase:
Protease N " Amano " G (comes from bacillus subtilis;Amano Enzyme Inc. (Amano Enzyme
Inc.))
PROTIN SD-NY10 (come from bacillus amyloliquefaciens;Amano Enzyme Inc.)
THERMOASE PC10F (come from bacillus stearothermophilus;Amano Enzyme Inc.)
Brewers (Block リ ュ ー ワ ー ズ) Protease (comes from bacillus amyloliquefaciens;DSM Japan Co., Ltd.)
Accelerzyme (ア Network セ ラ ザ イ system) NP50.000 (comes from bacillus amyloliquefaciens;DSM Japan strain formula meetings
Society)
Neutrase (comes from bacillus amyloliquefaciens;Novozymes Japan Co., Ltd.)
Nucleicin (ヌ Network レ イ シ Application) (comes from bacillus subtilis;HBI Co., Ltd. (HBI Enzymes Inc.))
Orientase 90N (come from bacillus subtilis;HBI Co., Ltd.)
Corolase N (come from bacillus subtilis;The HiguchiKou chambers of commerce of Co., Ltd. (HIGUCHI INC.))
AROASE NS (come from bacillus subtilis;Yakult Pharmaceutical Industry Co., Ltd.)
AROASE AP-10 (come from bacillus subtilis;Yakult Pharmaceutical Industry Co., Ltd.)
AROASE NP-10 (come from bacillus subtilis;Yakult Pharmaceutical Industry Co., Ltd.);
As alkali protease:
PROTIN SD-AY10 (come from bacillus licheniformis;Amano Enzyme Inc.)
Delvolase (デ Le ボ ラ ー ゼ) (comes from bacillus licheniformis;DSM Japan Co., Ltd.)
Esperase (comes from bacillus (Bacillus sp.);Novozymes Japan Co., Ltd.)
Savinase (comes from bacillus (Bacillus sp.);Novozymes Japan Co., Ltd.)
Everlase (comes from bacillus (Bacillus sp.);Novozymes Japan Co., Ltd.)
Alcalase (comes from bacillus licheniformis;Novozymes Japan Co., Ltd.)
Bioprase OP (come from bacillus (Bacillus sp.);Long rapids industry (Nagase ChemteX) strain formula meeting
Society)
Bioprase SP-20FG (come from bacillus (Bacillus sp.);Nagase Industrial Co., Ltd.)
Orientase 22BF (come from bacillus subtilis;HBI Co., Ltd.).
As the protease from aspergillus fungi, specifically, for example following protease can be enumerated,
As acid protease:
Protease M " Amano " G (comes from aspergillus oryzae;Amano Enzyme Inc.)
Sumizyme (ス ミ チ ー system) AP (comes from aspergillus niger;New Nippon Chemical Ind)
Denapushin (デ Na プ シ Application) 2P (comes from aspergillus (Aspergillus sp.);Nagase Industrial Co., Ltd.)
Orientase AY (come from aspergillus niger;HBI Co., Ltd.)
Tetorase (テ ト ラ ー ゼ) S (comes from aspergillus niger;HBI Co., Ltd.)
Brewers Clarex (come from aspergillus niger;DSM Japan Co., Ltd.)
Baridase (バ リ ダ ー ゼ) AFP (comes from aspergillus niger;DSM Japan Co., Ltd.)
Protease YP-SS (come from aspergillus niger;Yakult Pharmaceutical Industry Co., Ltd.);
As neutral proteinase:
Protease A " Amano " SD (comes from aspergillus oryzae;Amano Enzyme Inc.)
Protease P " Amano " 3SD (comes from Aspergillus melleus;Amano Enzyme Inc.)
Sumizyme ACP-G (come from aspergillus oryzae;New Nippon Chemical Ind)
Sumizyme LP (come from aspergillus oryzae;New Nippon Chemical Ind)
Sumizyme FP-G (come from aspergillus oryzae;New Nippon Chemical Ind)
Baridase FP60 (come from aspergillus oryzae;DSM Japan Co., Ltd.)
Denatyme (デ ナ チ ー system) AP (comes from aspergillus (Aspergillus sp.);Nagase Industrial Co., Ltd.)
Orientase OP (come from aspergillus oryzae;HBI Co., Ltd.)
Pancidase (パ Application チ ダ ー ゼ) P (comes from aspergillus (Aspergillus sp.);Yakult
Pharmaceutical Industry Co., Ltd.)
Pancidase NP-2 (come from aspergillus oryzae;Yakult Pharmaceutical Industry Co., Ltd.);
As alkali protease:
Sumizyme MP (come from aspergillus (Aspergillus sp.);New Nippon Chemical Ind).
In addition, as protease, using the homologue of known protease as above-mentioned illustration.As long as homologue
Protease being found in bacillus or aspergillus fungi, having desired proteinase activity, does not have
There is special limitation.In addition, as protease, known protease as above-mentioned illustration can also be used or their homologue
Artificial modified body.Artificial modified body is not particularly limited as long as there is desired proteinase activity.That is, " albumen
Enzyme is from bacillus or aspergillus fungi " also include the protease for can be true in bacillus or aspergillus
The situation of the artificial modified body of the protease found in bacterium.
As protease, a kind of protease can be used, 2 kinds or two or more proteinase combination can also be used.
Workable protease can be the high protease of collagen specific cleavage ability in the present invention.Also by " glue
Former protein-specific capacity of decomposition " is referred to as " muscle specific cleavage ability ".In the present invention, " collagen specific cleavage ability "
The degrading activity of collagen is represented by relative to ratio (the collagen decomposition work of the degrading activity of myofibrillar protein
Property/myofibrillar protein degrading activity).That is, so-called " collagen specific cleavage ability ", refers in fribrillin
The degree of the property of collagen is optionally decomposed in matter and collagen.The collagen egg of workable protease in the present invention
The value of white specific cleavage ability for example can be higher than the value of the collagen specific cleavage ability of papain.Not simultaneously
During with yeast containing metal, the value of the collagen specific cleavage ability of workable protease for example can be in the present invention
More than 0.20, more than 0.25, more than 0.30, more than 0.35, more than 0.50 or more than 0.70.It is in addition, workable in the present invention
The value of the collagen specific cleavage ability of protease need not especially set upper limit, not and with the yeast containing metal
When, such as can be less than 10000, less than 1000 or less than 100.In addition, when not and with yeast containing metal, the present invention
In the value of collagen specific cleavage ability of workable protease also can be in the range of the combination of foregoing illustrative value.
The degrading activity of collagen relative to the degrading activity of myofibrillar protein ratio (collagen decompose live
Property/myofibrillar protein degrading activity) collagen heating elution amount can be used as to be washed relative to myofibrillar protein heating
Take off the ratio (collagen heating elution amount/myofibrillar protein heating elution amount) of amount and calculate.
The step of myofibrillar protein heating elution amount is by described in embodiment 1 determines.That is, by 0.02 μ g/ml eggs
White enzyme aqueous solution and 800 μ g/ml myofibrillar protein suspension mixed in equal amounts, stand 10 minutes, then in 80 at normal temperatures
DEG C heat within 10 minutes, and then in 100 DEG C heat within 10 minutes, the ice cooling of 1 minute is carried out, in centrifuged supernatant
Albumen quality is quantified, and elution amount is heated as myofibrillar protein.The myofibrillar protein example used as substrate
Such as can using Mimced Beef as raw material, it is prepared by the step of being recorded by embodiment 1 (1-1).
The step of collagen heating elution amount is recorded by embodiment 1 determines.That is, by 2 μ g/ml aqueous solution of protease
With 80mg/ml collagen suspension liquid mixed in equal amounts, 10 minutes are stood at normal temperatures, then carries out adding for 10 minutes in 80 DEG C
Heat, and then in 100 DEG C heat within 10 minutes, the ice cooling of 1 minute is carried out, the albumen quality in centrifuged supernatant is determined
Amount, elution amount is heated as collagen.The collagen used as substrate for example can using Cowhells as raw material, pass through implementation
It is prepared by the step of example 1 (1-2) record.
By the way that protease and the yeast containing metal are used in combination, the collagen specific cleavage ability of protease can be improved.
The degree of the raising of collagen specific cleavage ability is not particularly limited.The raising of collagen specific cleavage ability
Degree is represented by and with collagen specific cleavage ability during yeast containing metal relative to not and with the ferment containing metal
The ratio of collagen specific cleavage ability when female is (and with collagen specific cleavage energy during yeast containing metal
Power/not and with collagen specific cleavage ability during yeast containing metal;Hereinafter, also referred to as " compare ").Compare
Such as can be more than 1, can be more than 1.01, more than 1.03, more than 1.05, more than 1.1, more than 1.15, more than 1.2,1.3 with
Above, more than 1.4, more than 1.5 or more than 1.7.Compare need not especially set upper limit, such as can be less than 5 or 3 with
Under.Also can be in the range of the combination of foregoing illustrative value in addition, comparing.It should be noted that calculating is so-called when comparing
" and during with yeast containing metal " refer to following situations:Relative to 1g protease, with metal gauge, and with 8.0 × 10-6mol
The yeast (such as yeast containing manganese) containing metal.
As protease, commercially available product can be used, it is possible to use the protease as obtained from suitably manufacturing.The system of protease
The method of making is not particularly limited.Protease for example can produce the microorganism of protease by cultivating and egg is reclaimed from culture
White enzyme and manufacture.The microorganism for producing protease can just be produced the microorganism of protease originally or be modified to
Produce the microorganism of protease.The microorganism for producing protease for example can be by the way that the channel genes of encoding proteins enzyme can extremely be expressed
Obtained in the microorganism of the gene.The importing of gene for example can be micro- by the way that the carrier (vector) for carrying the gene is directed into
Biology will be realized on the chromosome of channel genes to microorganism.It is each from bacillus or aspergillus fungi
The amino acid sequence for planting protease, the base sequence for encoding their gene for example can be from NCBI (http://
) etc. www.ncbi.nlm.nih.gov/ common data base obtains.For the condition of culture of microorganism, as long as micro- life can be made
Thing growth and breeding, protease can be produced, is not particularly limited.Microorganism such as can culture bacterium or fungi microorganism
It is common under the conditions of cultivated.
Protease can include the composition beyond protease, can also not include the composition beyond protease.That is, as albumen
Enzyme, purified protease can be used, it is possible to use the raw material containing protease., can as the raw material containing protease
Enumerate for example produce protease microorganism culture, separated from the culture culture supernatant, from the culture
The thalline of separation, the processed material of the thalline.Can be by protease purification to desired degree.
The edible meat modifying agent of the present invention contains the yeast containing metal.
As long as yeast of the yeast containing metal containing metal, is not particularly limited.The species of metal is not special
Limitation.As metal, zinc, calcium, chromium, selenium, copper, magnesium, vanadium, manganese, molybdenum, cobalt, iodine, iron etc. can be enumerated.That is, as the ferment containing metal
Mother, the yeast containing zinc, the yeast of calcic can be enumerated, the yeast containing chromium, the yeast containing selenium, the yeast of cupric, the yeast containing magnesium, contained
The yeast of vanadium, the yeast containing manganese, the yeast containing molybdenum, the yeast containing cobalt, the yeast containing iodine, the yeast etc. of iron content.In these, preferably
Yeast containing manganese, the yeast containing zinc, the yeast containing magnesium, the yeast of iron content, the more preferably yeast containing manganese.Metal can with simple substance,
Any form in ion, salt etc. is included in the yeast containing metal.For example, the salt as manganese, can enumerate manganese chloride, sulfuric acid
Manganese, manganese carbonate, manganese phthalocyanine, manganese nitrate, manganese acetate, manganese phosphate, manganese borate, manganous fluoride, triacetic acid manganese (maganese
Triacetate), manganese selenide, manganese dioxide, mangano-manganic oxide, potassium permanganate etc..Yeast containing metal can contain a kind of metal,
Also it can be combined and contain 2 kinds or two or more metal.Yeast containing metal for example can be by adding metal in culture yeasts, making institute
Metal is stated to be absorbed into saccharomycete body and obtain.As the commercially available yeast containing metal, can enumerate for example by Sceti strain formula meetings
The yeast containing various mineral matters that society commercially sells.For the tenor in the yeast containing metal, for example, phase
For the dry weight 1g of yeast, such as can be 0.2 × 10-4~0.2 × 10-2Mol, preferably 0.2 × 10-3~1.4 × 10- 3Mol, more preferably 0.7 × 10-3~1.1 × 10-3mol.The form of yeast containing metal is not particularly limited.Yeast containing metal
Such as can be any form in powdered, pasty state, suspension etc..In addition, the yeast containing metal can keep viable bacteria
State or through product obtained from sterilization.The species of yeast is not particularly limited.As yeast, it can enumerate and for example make
Brewer yeast (Saccharomyces cerevisiae) etc. Blastocystis (Saccharomyces) yeast, schizosaccharomyces pombe
(Schizosaccharomyces pombe) etc. Schizosaccharomyces (Schizosaccharomyces) yeast, candida utili
(Candida utilis) etc. candida (Candida) yeast.In these, Blastocystis is preferably belonged to
(Saccharomyces) or candida (Candida) yeast.
As the yeast containing metal, a kind of yeast containing metal can be used, also can be by 2 kinds or two or more yeast containing metal
It is applied in combination.
The edible meat modifying agent of the present invention only can be made up of above-mentioned active ingredient, can also include other compositions.
" other compositions " are not particularly limited as long as not damaging the purpose of the present invention., can profit as " other compositions "
The composition utilized with can for example coordinate in flavoring, diet product or medicine.As " other compositions ", example can be enumerated
Such as dextrin, starch, producing starch, reduction maltose excipient;The flavorings such as amino acid, nucleic acid, poultry meat extract;Plant egg
The protein such as white matter, glutelin (gluten), egg white, casein;The protein such as protein hydrolysate, protein portion analyte
Processed goods;The emulsifying agents such as fatty acid glyceride, organic acid mono-glyceride;The chelating agents such as citrate, polymeric phosphate;Gluathione
The reducing agents such as peptide, cysteine;Other food additives such as alginic acid, salt water, grease, pigment, acid flavoring, spices.As " its
His composition ", can be used a kind of composition, also 2 kinds or two or more composition can be applied in combination.From improve edible meat bating effect this
From the aspect of, preferably add emulsifying agent.
The form of the edible meat modifying agent of the present invention is not particularly limited.The present invention edible meat modifying agent for example can be
Any form in liquid, pasty state, graininess, powdered, solid-like etc..
For the present invention edible meat modifying agent in each composition (that is, active ingredient and as needed and use other
Composition) concentration, for containing ratio, as long as can obtain combined effect and can be applied to the improvement of edible meat, do not have
Especially limitation.Concentration, the containing ratio of each composition in the edible meat modifying agent of the present invention can change according to the edible meat of the present invention
The various conditions such as good dose of usage amount are suitably set.
The total concentration of active ingredient in the edible meat modifying agent of the present invention for example can be more than 1ppm (w/w), 10ppm
(w/w) more than, more than 100ppm (w/w) or more than 1000ppm (w/w), can be 100% (w/w) below, 10% (w/w) with
Under or 1% (w/w) below, or combinations thereof.
For the content of the yeast containing metal, relative to 1U protease, with metal gauge, such as can be 0.4 ×
10-10More than mol or 0.4 × 10-9More than mol, can be 2.0 × 10-6Below mol or 2.0 × 10-7Below mol, can also
For combinations thereof.For the content of the yeast containing metal, relative to 1U protease, with metal gauge, such as can be
0.4×10-9~2.0 × 10-7mol.Specifically, for example, the edible meat modifying agent of the present invention contains protease and the ferment containing manganese
When female, in edible meat modifying agent of the invention, relative to 1U protease, to be scaled manganese gauge, 0.4 × 10 can be contained-9~2.0
×10-7The yeast containing manganese of mol amount.In addition, for the content of the yeast containing metal, relative to 1g protease, with gold
Belong to gauge, such as can be 1.0 × 10-7More than mol or 1.0 × 10-6More than mol, can be 1.0 × 10-3Below mol or
1.0×10-4Below mol, or combinations thereof.
In the present invention, proteinase activity is the result that will be measured using casein as substrate, using folin's methods.That is, it is of the invention
In, using casein as substrate, when carrying out enzyme reaction using conventional method, will cause in 1 minute equivalent to 1 μ g tyrosine
The increased enzyme amount of forint test solution present-color material be defined as 1U proteinase activity.
Specifically, proteinase activity for example determines using following step.By protease stirring and dissolving in calcium acetate-
Sodium chloride test solution (is prepared in the following manner:By 0.2mol/L calcium acetate test solution 5ml and 2mol/L sodium chloride test solutions 2.5ml
Mixing, 500ml is settled to distilled water) in, 7000 times of dilutions are carried out, enzyme solutions are made.In addition, to casein (breast make) 1.2g
Middle addition 0.05mol/L disodium hydrogen phosphate test solution 160ml, heat and make its dissolving in a water bath.After carrying out flowing water cooling,
PH is adjusted to 8.0 with sodium hydroxide test solution, 200ml is settled to distilled water, as substrate solution.Take substrate solution
5ml carries out heating for 10 minutes into test tube in 37 DEG C, then adds enzyme solutions 1ml and is mixed, is placed 10 minutes in 37 DEG C
Afterwards, addition trichloroacetic acid test solution (is prepared in the following manner:Trichloroacetic acid 36g and acetic anhydride sodium 36g are dissolved in distilled water
In 1.6L, mixed with 6mol/L acetic acid test solutions 110ml, be then settled to 2L with distilled water) 5ml and vibration mixing is carried out, again
Place 30 minutes, filtered in 37 DEG C.Then, take 0.55mol/L sodium carbonate test solutions 5ml into test tube, add filtrate 2ml and
Forint test solution (forint-Qiao Ka ladders phenol reagent (the Folin-Ciocalteu phenol difficult to understand of 3 times of dilutions have been carried out with distilled water
Reagent), Wako Pure Chemical Industries, Ltd.'s system) and mixed, then, placed 30 minutes in 37 DEG C.Then, will distill
Water is as control, the absorbance of measure 660nm wavelength, as enzyme reaction solution absorbance.In addition, by enzyme solutions 1ml and three chloroethenes
Sour test solution 5ml mixing, then adds substrate solution 5ml, is placed 30 minutes in 37 DEG C, same operation is carried out below, as sky
White absorbance.The value as obtained from subtracting the absorbance of blank from the absorbance of enzyme reaction solution, calculate the unit reaction time
Variable quantity, calculate proteinase activity.
The concentration of each active ingredient in the edible meat modifying agent of the present invention for example can be according to meeting the effective of example above
The total concentration of composition, the mode of containing ratio are set.
The present invention edible meat modifying agent in include each composition (that is, active ingredient and as needed and use other
Composition) it can be mutually mixed and be included in the edible meat modifying agent of the present invention, also can be separately or only in any combination
On the spot it is included in the edible meat modifying agent of the present invention.Separately wrapped for example, the edible meat modifying agent of the present invention can be used as
The external member (set) of the protease of dress and the yeast containing metal and provide.In this case, the composition included in external member can use
When be suitably used in combination.
The method of the > of < 2 present invention
In the present invention, edible meat is improved using active ingredient (that is, protease and yeast containing metal).That is, it is of the invention
Method is the method for including handling the edible meat of improvement of edible meat with active ingredient.The method of the edible meat of improvement for example can be by
The method of edible meat softening, can be by the method for the muscle portion position softening of edible meat specifically.In addition, this hair can also be used
Bright method manufactures edible meat processed goods.That is, a mode of method of the invention is to include being handled with active ingredient eating
The manufacture method of the edible meat processed goods of meat.It is referred to as " making effectively it should be noted that also " edible meat will be handled with active ingredient "
Composition acts on edible meat ".In addition, also " will handle edible meat with active ingredient ", process will be referred to as " enzyme reaction process ".
In the present invention, for example, the edible meat modifying agent of the invention containing active ingredient can be utilized to improve edible meat.
I.e., in other words, method of the invention can include eating meat with the improvement of the edible meat of edible meat modifying agent processing of the present invention
Method.In addition, a mode of the method for the present invention can include the edible meat of edible meat modifying agent processing with the present invention
Edible meat processed goods manufacture method.
Also the edible meat processed goods method by the present invention obtained is referred to as " edible meat processed goods of the invention ".This hair
Bright edible meat processed goods is improved edible meat processed goods.Improved edible meat processed goods for example can be that flexibility carries
High edible meat processed goods, can be the edible meat processed goods that the flexibility of muscle portion position improves specifically.
For the edible meat processed goods of the present invention, in addition to being handled with active ingredient, it can be used and usual
The same raw material of edible meat processed goods, manufactured using same cooking method.In addition, cooking method can suitably be become
More.For example, the edible meat processed goods of the present invention can use the shorter heat time of the situation than manufacturing common edible meat processed goods
Manufactured.
The species of edible meat is not particularly limited.As edible meat, can enumerate the poultry meat such as ox, pig, sheep, chicken, turkey,
The flesh of fish such as the poultries such as duck, goose, scad, salmon, cod, flatfish, saury, filefish.The position of edible meat does not limit especially
System.As the position of edible meat, especially from the aspect of effect is good, preferably shin, shoulder, neck, tongue, cheek, stock, tail, foot etc. wrap
The position of protein containing more hard.The form of edible meat is not particularly limited.Edible meat for example can be block, cube,
Any form in chunk, thin slice (section), powder etc..
The cooking method of edible meat is not particularly limited.Cooking method can be each according to the species of edible meat, position, form etc.
Kind condition is suitably set.As cooking method, preferably heated.As cooking method, can enumerate for example boil, bake, frying, frying,
The methods of steaming.The species of the edible meat processed goods of the present invention is not particularly limited.As the edible meat processed goods of the present invention, can lift
Go out for example stew the chopped cooked entrails of sheep, stew Cowhells, tail soup (tail soup), barbecue, steak (steak), hamburger (minced beef cutlet, hamburger),
Schnitzel, fried food (fry), tempura, dry fried food (Tang Yang), imperial field fried food (Dragon Tian Yang げ), curry, stew
Dish (stew), rinse meat, grilled fish, French butter grilled fish (meuniere), matelote.
In any stage for cooking process active ingredient can be made to act on edible meat, if combined effect is can obtain, and
Can the edible meat of improvement.That is, the edible meat that active ingredient can be made to act on before cooking, can also act on active ingredient and cook
Edible meat in tune, the edible meat that active ingredient can also be made to act on after end of cooking.Active ingredient can by directly or
It is prepared into appropriate solution etc., coexisted with edible meat, so as to acts on edible meat.For example, active ingredient can be added to edible meat
In, edible meat can be also impregnated in the treatment fluid containing active ingredient.Hereinafter, also active ingredient and edible meat are made by such
The operation coexisted is referred to as " addition " of active ingredient.For reaction time, reaction temperature, as long as can obtain and use effect
Fruit and edible meat can be improved, be not particularly limited.Reaction time, reaction temperature can according to the species of edible meat, effectively into
Point the various conditions such as addition and suitably set.Cooking process can be used to double as enzyme reaction process, it is anti-also can separately to implement enzyme
Answer process.Reaction time is for example preferably 1 minute~72 hours.Reaction temperature for example can be preferably 4~95 DEG C, be more preferably
4~80 DEG C.Enzyme reaction process can the implementation under the coexisting of the active ingredient of whole.For example, whole can have by adding simultaneously
Composition is imitated, so as to start enzyme reaction process.In addition, for example, also can be by separately or in any combination independently adding
Add active ingredient, so as to which the time point coexisted in the active ingredient of whole starts enzyme reaction process.Add the order of active ingredient
It is not particularly limited.Specifically, for example, make protease act on edible meat, be then total to the yeast containing metal with can preparing
Deposit, so as to start enzyme reaction process.In addition, each active ingredient can be added only 1 time, can also add 2 times or more than 2 times.For example,
When protease inactivates, addition protease can be added.In addition, also can and with the enzyme beyond active ingredient, additive.
For adding for each composition (that is, the active ingredient and other compositions that are as needed and using) in the method for the present invention
For dosage, addition ratio, as long as can obtain combined effect and edible meat can be improved, it is not particularly limited.The present invention
Method in each composition addition, addition ratio can be appropriate according to the various conditions such as the species of edible meat, position, form
Setting.
For the addition of protease, meat is eaten relative to 1g, in terms of being scaled proteinase activity, such as can be
More than 0.1U, more than 10U or more than 100U, can be below 100000U, below 10000U or below 1000U, or
Combinations thereof.For the addition of protease, meat is eaten relative to 1g, such as can be 1.0 × 10-7More than g, 1.0
×10-6More than g or 1.0 × 10-5More than g, or 1.0 × 10-2Below g, 1.0 × 10-3Below g or 1.0 × 10-4g
Below, or combinations thereof.
With metal gauge, such as can be 0.4 relative to 1U protease for the addition of the yeast containing metal
×10-10More than mol or 0.4 × 10-9More than mol, or 2.0 × 10-6Below mol or 2.0 × 10-7Below mol,
It can be combinations thereof.For the addition of the yeast containing metal, relative to 1U protease, with metal gauge, such as
Can be 0.4 × 10-9~2.0 × 10-7mol.Specifically, for example, making protease and yeast containing manganese act on edible meat
When, relative to 1U protease, to be scaled manganese gauge, can and with 0.4 × 10-9~2.0 × 10-7The ferment containing manganese of mol amount
It is female.With metal gauge, such as can be 1.0 relative to 1g protease in addition, for the addition of the yeast containing metal
×10-7More than mol or 1.0 × 10-6More than mol, can be 1.0 × 10-3Below mol or 1.0 × 10-4Below mol, also may be used
Think combinations thereof.
Embodiment
Embodiment is enumerated below further specifically describes the present invention.The present invention is not by any restrictions of these embodiments.
Embodiment 1:By and with the yeast containing metal and the collagen specific cleavage ability of protease brought
Improve the evaluation (1) of effect
In the present embodiment, for various protease, to not and with during yeast containing metal with and with glue during yeast containing metal
Former protein-specific capacity of decomposition (muscle specific cleavage ability) is compared, to being brought by and with the yeast containing metal
The raising effect of collagen specific cleavage ability is evaluated.The protease used is shown in table 1.
[table 1]
。
(1) not and with the collagen specific cleavage ability of various protease during yeast containing metal
Firstly, for various protease (table 1), measure is not and with collagen specific cleavage energy during yeast containing metal
Power.
The myofibrillar protein degrading activity of (1-1) various protease
Finger as various protease (table 1) to the degrading activity of the myofibrillar protein at the red meat position of main composition meat
Mark, utilize following method measure myofibrillar protein heating elution amount.
As myofibrillar protein extraction buffer solution, 30mM citrate-phosphates buffering is prepared according to following step
Liquid (pH5.5, contains 0.1M NaCl).First, 30mM aqueous citric acid solutions, the 60mM disodium hydrogen phosphates aqueous solution, 1M chlorinations are prepared
Sodium water solution.Next, by 30mM aqueous citric acid solutions 852ml and the 60mM disodium hydrogen phosphates aqueous solution 1,148ml is mixed, on one side
30mM aqueous citric acid solutions are added bit by bit, while pH is adjusted into 5.5.Addition 1M sodium chloride water in solution is prepared to this
Solution 400ml, 4L is settled to distilled water, obtains 30mM citrate phosphate buffers (pH5.5, containing 0.1M NaCl).
The extraction and preparation of myofibrillar protein follow the steps below.At 2L polyester beaker (Port リ ビ ー カ ー)
The citrate phosphate buffer of interior 200g and about 7.5 times of amount (1,500ml) of mixing Mimced Beef (commercially available japanese product), while will
Surrounding is cooled with ice, while carrying out 1 minute (homogenizer that homogenizes with 6,000rpm:POLYTRON PT 3100, axle:PT-
DA3030).Obtained suspension is filtered with gauze (SUZURAN, mesh size diameter 1mm), 1,000ml filtrates are filled
Enter into centrifuge tube, 1,660 × g, 10min, centrifuged under conditions of 5 DEG C and (use centrifuge:CR22G, rotor:R9AF,
Centrifuge tube:1,000ml capacity).Supernatant is removed, the citrate-phosphate buffering of about 7.5 times of amounts (500ml) is added into precipitation
Liquid and make its suspension, suspension is centrifuged under identical condition.The operation is carried out again, is added into obtained precipitation
Citrate phosphate buffer 30ml and make its suspension, after suspension is moved into 50ml centrifuge tubes, 9,520 × g, 5min, 5 DEG C
Under conditions of centrifuged and (use centrifuge:CR22G, rotor:R12A2, centrifuge tube:50ml capacity).Supernatant is removed, then
2 same operations are repeated, the citrate phosphate buffer of about 2 times of amounts (10ml) is added into obtained precipitation and makes it
Suspend, myofibrillar protein standard items are made.
In 1.5ml micro-pipes, each protease is prepared into 0.02 μ g/ml with distilled water, as enzyme solutions.Use liquid relief
Device and turbine mixer make myofibrillar protein standard items fully suspend, and are then prepared into 1.5ml micro-pipes with distilled water
800 μ g/ml, are made myofibrillar protein suspension.Each the μ l of enzyme solutions 250 and muscle fibril egg are mixed in 1.5ml micro-pipes
μ l (S/E=40000 of white matter suspension 250:1) after, it is fully suspended, 10 minutes are stood at normal temperatures.After standing, using adding
Hot device (block heater) (CTU-Neo), heated 10 minutes in 80 DEG C.Then, 100 DEG C of heaters, Jin Erjin are quickly moved to
Row heats for 10 minutes.The ice cooling of 1 minute is carried out, is then centrifuged and (used under conditions of 12,000 × g, 1min, normal temperature
Centrifuge:CF15RXII, rotor:T15A39), supernatant is reclaimed.For the supernatant, carry out the protein based on BCA methods and determine
Amount, elution amount is heated as myofibrillar protein.
The collagen degrading activity of (1-2) various protease
It is collagen to the hard protein matter of the muscle portion position of main composition meat as various protease (table 1) in the present embodiment
Degrading activity index, utilize following method measure collagen heating elution amount.
Red meat and fat meat subsidiary on Cowhells (commercially available Japan's production ox shin meat) are cut off using kitchen knife, being chopped into the length of side is about
5mm cube size.The cylindrical type that the above-mentioned chopping things of 3.5g are put into 50ml capacity is crushed in tank (using crushing tank:
Mixer Mill Type MM301 accessories), and then 1 a diameter of 25mm crushing ball is put into from the upper side (using crushing
Ball:Mixer Mill Type MM301 accessories).The lid for crushing tank is covered, in fume hood, is impregnated in equipped with liquid nitrogen
Container in 5 minutes.Liquid nitrogen capacity is turned into fully submergence and crush the overall amount of tank, added as evaporation is reduced.Leaching
After stain 5 minutes, it will crush tank using special tweezers and take out, be arranged in pulverizer, in the bar that vibration number is 25/s, 1.5min
Crushed under part and (use pulverizer:Mixer Mill Type MM301).The lid for crushing tank is opened, crushing ball is taken out, with scraping
Shovel reclaims the sample of chilled crushing.Using the sample as collagen powder standard items.
In 1.5ml micro-pipes, each protease is prepared into 2 μ g/ml with distilled water, as enzyme solutions.Weigh collagen
Protein powder standard items 80mg makes its suspension in 1.5ml micro-pipes, then adding distilled water 1ml, and collagen powder is made and hangs
Supernatant liquid.Each μ l of the enzyme solutions 250 and μ l of collagen powder suspension 250 are mixed into (S/E=40000 in 1.5ml micro-pipes:1),
After fully suspending, 10 minutes are stood at normal temperatures.After standing, using heater (CTU-Neo), heated 10 minutes in 80 DEG C.So
Afterwards, 100 DEG C of heaters are quickly moved to, further heating 10 minutes.After carrying out the ice cooling of 1 minute, 12,000 × g, 1min,
Centrifuged under normal temperature and (use centrifuge:CF15RXII, rotor:T15A39), supernatant is reclaimed.For the supernatant, carry out
Based on the quantification of protein of BCA methods, elution amount is heated as collagen.
(1-3) collagen specific cleavage ability
For each protease, by the way that the collagen obtained in (1-2) is heated into the myogen obtained in elution value divided by (1-1)
Celloglobulin heating elution value, lives so as to calculate the degrading activity of collagen relative to the decomposition of myofibrillar protein
The ratio (collagen degrading activity/myofibrillar protein degrading activity) of property, using the value as not and with the ferment containing metal
Collagen specific cleavage ability (muscle specific cleavage ability) when female.Egg from papaya (Carica papaya)
The collagen specific cleavage ability (muscle specific cleavage ability) of white enzyme is 0.17.In addition, come for what is used in experiment
Protease from bacillus and the protease from aspergillus fungi, (muscle is special for collagen specific cleavage ability
Different in nature capacity of decomposition) it is more than 0.20.
(2) and with the collagen specific cleavage ability of various protease during yeast containing metal
Next, for various protease (table 1), determine and with collagen specific cleavage energy during yeast containing metal
Power.As the yeast containing metal, the yeast (saccharomyces cerevisiae containing manganese has been used;SCETI Co., Ltd.).
For each protease, when carrying out enzyme reaction, according to be scaled manganese gauge, final concentration turn into 0.2 μM (with mixing
Concentration in preceding enzyme solutions is calculated as 0.4 μM) mode add the yeast containing manganese, according to the step same with (1-1) and (1-2)
Suddenly, measure and with collagen heating elution value during yeast containing metal and myofibrillar protein heating elution value.
Next, for each protease, according to the step same with (1-3), the degrading activity for calculating collagen is fine relative to myogen
The ratio (collagen degrading activity/myofibrillar protein degrading activity) of the degrading activity of fibrillarin matter, using the value as
And with the collagen specific cleavage ability (muscle specific cleavage ability) during yeast containing metal.
(3) imitated by and with the yeast containing metal and the raising of the collagen specific cleavage ability of the protease brought
The evaluation of fruit
For each protease, by will be being obtained in (2) and with collagen specific cleavage ability during yeast containing metal
Divided by obtained in (1) not and with collagen specific cleavage ability during yeast containing metal, so as to calculate collagen
The degree of the raising of specific cleavage ability.Show the result in Fig. 1.In Fig. 1, " Cont (M.Q.) " is represented:Instead of enzyme solutions, make
With the ultra-pure water (Milli Q water) for adding or being not added with the yeast containing manganese, obtained according to the step with (1-1)~(1-3) same
Result.For the protease from bacillus used in experiment and the protease from aspergillus fungi,
Obtain by and with the yeast containing manganese the raising effect of collagen specific cleavage ability brought.On the other hand, it is right
In the protease from streptomycete (Streptomyces) category bacterium and protease from papaya (Carica papaya),
Do not find by and with the yeast containing metal the raising effect of collagen specific cleavage ability brought.
It is indicated above that by and with protease from bacillus or aspergillus fungi and the ferment containing metal
Mother, improve the collagen specific cleavage ability (muscle specific cleavage ability) of protease.
Embodiment 2:(promote and the raising effect of the softening for the muscle portion position of edible meat brought by and with the yeast containing metal
Enter effect) evaluation
In the present embodiment, for various protease, with the food system of reality to being brought by and with the yeast containing metal
The raising effect (facilitation effect) of the softening of the muscle portion position of edible meat is evaluated.Step is as described below:
(1) by the unnecessary lipectomy of the upper brain (ox Jian ロ ー ス) (12mm sections) of Australia production ox, adjust to 200g, as sample
Product;
(2) sample of (1) is put into the bag of vacuum packaging;
(3) to contain protein weight, 5mg (the 1/40000 of brain weight on ox) each protease (table 2) is measured, is dissolved in certainly
In water 200ml, as enzyme solutions;
(4) for and with the yeast containing manganese trial zone (Mn.Y.+), according to be scaled manganese gauge as in a manner of 0.2 μM
The yeast containing manganese is added into the enzyme solutions of (3);
(5) for not and with the trial zone (Mn.Y.-) of the yeast containing manganese, the enzyme solutions of (3) are added in (2), vacuum is carried out
Packaging, for the yeast containing manganese and trial zone (Mn.Y.+) is used, by the enzyme solutions of (4) added in (2), is vacuum-packed.
For check plot (Cont.), instead of enzyme solutions, the running water for adding or being not added with the yeast containing manganese is added in (2), carried out
Vacuum packaging;
(6) in 4 DEG C of stored refrigerated nights (18hr.);
(7) after vacuum packaging is broken a seal, control water is carried out to the upper brain of ox with bamboo strainer;
(8) with 250 DEG C of ram (impinger), the two sides of the upper brain of ox of (7) is respectively carried out firing for 2 minutes;
(9) with 7 grades of -3 points~+3 points, sensory evaluation (n=6) is carried out to the flexibility of the muscle portion position of each trial zone.
Show the result in table 2.For using protease from bacillus in experiment and from aspergillus
The protease of fungi, obtain by and with the yeast containing manganese the raising effect of the flexibility of muscle portion position brought.The opposing party
Face, it is unconfirmed to be brought to by and with the yeast containing metal for the protease from papaya (Carica papaya)
The raising effect of the flexibility of muscle portion position, flexibility decline on the contrary.
[table 2]
※ metewands:- 3 points ~+3 points of 7 grades of evaluations
- 3 points ... stone
- 2 points ... hard
- 1 point ... slightly hard
0 point ... common (not hard also not soft)
+ 1 point ... slightly soft
+ 2 points ... soft
+ 3 points ... very soft.
It is indicated above that by and with the protease from bacillus or aspergillus fungi and the ferment containing metal
Mother, the softening that (promotion) eats the muscle portion position of meat can be improved.
Embodiment 3:By and with the yeast containing metal and the collagen specific cleavage ability of protease brought
Improve the evaluation (2) of effect
In the present embodiment, for the protease from bacillus, to by and with the various yeast containing metal and band
The raising effect for the collagen specific cleavage ability come is evaluated.
Trial zone is shown in table 3.As protease, the neutral proteinase from bacillus has been used.As
Yeast containing metal, it (is wine brewing ferment to have used the yeast containing manganese, the yeast containing zinc, the yeast of iron content and yeast containing magnesium
It is female;SCETI Co., Ltd.).For each trial zone, the step of being recorded according to embodiment 1, implements enzyme reaction (S/E=40000:1, make
To be scaled the yeast containing metal of final concentration of 0.2 μM of metal gauge), calculate collagen specific cleavage ability (muscle
Specific cleavage ability).
Show the result in table 3.It is thin from bacillus and with arbitrarily in the case of the yeast containing metal, obtained
The raising effect of the collagen specific cleavage ability (muscle specific cleavage ability) of the protease of bacterium.
[table 3]
。
Industrial applicability
By the present invention, edible meat can be improved, improves the quality of edible meat.By the mode of the present invention, can especially incite somebody to action
As edible meat connective tissue one of muscle portion position softening.
Claims (17)
1. edible meat modifying agent, it contains protease and the yeast containing metal,
The protease is selected from the protease from bacillus (Bacillus) category bacterium and from aspergillus
(Aspergillus) the one kind or two or more protease in the protease of fungi is belonged to.
2. edible meat modifying agent according to claim 1, wherein, the yeast containing metal be selected from the yeast containing manganese,
One kind or two or more yeast in the yeast of yeast containing zinc, the yeast containing magnesium and iron content.
3. edible meat modifying agent according to claim 1 or 2, wherein, the yeast containing metal is the yeast containing manganese.
4. according to edible meat modifying agent according to any one of claims 1 to 3, wherein, the protease is and uses and contain metal
Yeast when collagen specific cleavage ability relative to not and with the collagen specificity point during yeast containing metal
The ratio of solution ability(And during with collagen specific cleavage ability during yeast containing metal/not and with yeast containing metal
Collagen specific cleavage ability)Protease more than 1.
5. edible meat modifying agent according to claim 4, wherein, the ratio is more than 1.1.
6. according to edible meat modifying agent according to any one of claims 1 to 5, wherein, relative to protease described in 1U, with gold
Belong to gauge, contain 0.4 × 10-9~2.0 × 10-7Yeast containing metal described in mol.
7. according to edible meat modifying agent according to any one of claims 1 to 6, it is edible meat muscle softening agent.
8. the manufacture method of edible meat processed goods, methods described includes being changed with edible meat according to any one of claims 1 to 7
The edible meat of good dose of processing.
9. the manufacture method of edible meat processed goods, methods described includes eating meat with protease and the processing of the yeast containing metal,
The protease is selected from the protease from bacillus (Bacillus) category bacterium and from aspergillus
(Aspergillus) the one kind or two or more protease in the protease of fungi is belonged to.
10. according to the method for claim 9, wherein, the yeast containing metal is selected from the yeast containing manganese, the ferment containing zinc
One kind or two or more yeast in the female, yeast containing magnesium and the yeast of iron content.
11. the method according to claim 9 or 10, wherein, the yeast containing metal is the yeast containing manganese.
12. the method according to any one of claim 9~11, wherein, the protease is and with the yeast containing metal
When collagen specific cleavage ability relative to not and with collagen specific cleavage ability during yeast containing metal
Ratio(And with collagen specific cleavage ability during yeast containing metal/not and with collagen during yeast containing metal
Protein-specific capacity of decomposition)Protease more than 1.
13. according to the method for claim 12, wherein, the ratio is more than 1.1.
14. the method according to any one of claim 8~13, wherein, relative to protease described in 1U, with amount of metal
Meter, makes 0.4 × 10-9~2.0 × 10-7Yeast effect containing metal described in mol.
15. the method according to any one of claim 8~14, wherein, relative to meat is eaten described in 1g, make more than 0.1U
The albumen enzyme effect.
16. the method for the edible meat of improvement, methods described are included with edible meat modifying agent according to any one of claims 1 to 7
The edible meat of processing.
17. the method for the edible meat of improvement, methods described includes handling edible meat with protease and the yeast containing metal,
The protease is selected from the protease from bacillus (Bacillus) category bacterium and from aspergillus
(Aspergillus) the one kind or two or more protease in the protease of fungi is belonged to.
Applications Claiming Priority (3)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
JP2015150044 | 2015-07-29 | ||
JP2015-150044 | 2015-07-29 | ||
PCT/JP2016/072318 WO2017018503A1 (en) | 2015-07-29 | 2016-07-29 | Meat modifying agent |
Publications (2)
Publication Number | Publication Date |
---|---|
CN107846944A true CN107846944A (en) | 2018-03-27 |
CN107846944B CN107846944B (en) | 2021-05-14 |
Family
ID=57884405
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
CN201680042880.6A Active CN107846944B (en) | 2015-07-29 | 2016-07-29 | Meat modifier |
Country Status (5)
Country | Link |
---|---|
JP (1) | JP6756333B2 (en) |
CN (1) | CN107846944B (en) |
BR (1) | BR112018001514B1 (en) |
MY (1) | MY197893A (en) |
WO (1) | WO2017018503A1 (en) |
Cited By (3)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CN110172490A (en) * | 2019-03-13 | 2019-08-27 | 济南大学 | A method of except grease in donkey-hide gelatin peptide |
CN115381041A (en) * | 2022-09-19 | 2022-11-25 | 青海省畜牧兽医科学院 | Method for improving tenderness of yak meat based on connective tissue weakening |
CN115997906A (en) * | 2022-12-28 | 2023-04-25 | 中国肉类食品综合研究中心 | Fermentation liquor, flavor modifier and application thereof in processing of low-salt preserved products |
Families Citing this family (2)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US9504750B2 (en) | 2010-01-28 | 2016-11-29 | Advanced Bionutrition Corporation | Stabilizing composition for biological materials |
JPWO2021167062A1 (en) * | 2020-02-21 | 2021-08-26 |
Citations (4)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
EP0701781A2 (en) * | 1994-08-17 | 1996-03-20 | Kao Corporation | Meat tenderizing composition |
JP2003033161A (en) * | 2001-07-25 | 2003-02-04 | T Hasegawa Co Ltd | Texture and flavor improver for meats |
JP2014158463A (en) * | 2013-01-28 | 2014-09-04 | Ajinomoto Co Inc | Manufacturing method of processed meat product, and modifier for processed meat product |
WO2015105112A1 (en) * | 2014-01-09 | 2015-07-16 | 味の素株式会社 | Manufacturing method for improved protein-containing food and formulation for improving protein-containing food |
Family Cites Families (5)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JPH0856664A (en) * | 1994-08-17 | 1996-03-05 | Kao Corp | Protease and meat-softening agent |
JP3853321B2 (en) * | 1998-04-17 | 2006-12-06 | 松下電器産業株式会社 | Solid polymer electrolyte fuel cell |
JP2000125811A (en) * | 1998-10-27 | 2000-05-09 | Oriental Yeast Co Ltd | Mineral-containing food |
JP2007319166A (en) * | 2001-10-15 | 2007-12-13 | Katayama Hiroshi | Food comprising animal protein, softening method of the animal protein, and softening agent to be used for softening treatment of the animal protein |
JP4514534B2 (en) * | 2004-07-09 | 2010-07-28 | キユーピー株式会社 | Food and drink |
-
2016
- 2016-07-29 CN CN201680042880.6A patent/CN107846944B/en active Active
- 2016-07-29 MY MYPI2018700335A patent/MY197893A/en unknown
- 2016-07-29 BR BR112018001514-8A patent/BR112018001514B1/en active IP Right Grant
- 2016-07-29 JP JP2017530933A patent/JP6756333B2/en active Active
- 2016-07-29 WO PCT/JP2016/072318 patent/WO2017018503A1/en active Application Filing
Patent Citations (5)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
EP0701781A2 (en) * | 1994-08-17 | 1996-03-20 | Kao Corporation | Meat tenderizing composition |
CN1130996A (en) * | 1994-08-17 | 1996-09-18 | 花王株式会社 | Meat modifier and food meat or meat product processed with same |
JP2003033161A (en) * | 2001-07-25 | 2003-02-04 | T Hasegawa Co Ltd | Texture and flavor improver for meats |
JP2014158463A (en) * | 2013-01-28 | 2014-09-04 | Ajinomoto Co Inc | Manufacturing method of processed meat product, and modifier for processed meat product |
WO2015105112A1 (en) * | 2014-01-09 | 2015-07-16 | 味の素株式会社 | Manufacturing method for improved protein-containing food and formulation for improving protein-containing food |
Cited By (4)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CN110172490A (en) * | 2019-03-13 | 2019-08-27 | 济南大学 | A method of except grease in donkey-hide gelatin peptide |
CN115381041A (en) * | 2022-09-19 | 2022-11-25 | 青海省畜牧兽医科学院 | Method for improving tenderness of yak meat based on connective tissue weakening |
CN115997906A (en) * | 2022-12-28 | 2023-04-25 | 中国肉类食品综合研究中心 | Fermentation liquor, flavor modifier and application thereof in processing of low-salt preserved products |
CN115997906B (en) * | 2022-12-28 | 2024-02-02 | 中国肉类食品综合研究中心 | Fermentation liquor, flavor modifier and application thereof in processing of low-salt preserved products |
Also Published As
Publication number | Publication date |
---|---|
JP6756333B2 (en) | 2020-09-16 |
MY197893A (en) | 2023-07-24 |
BR112018001514A2 (en) | 2018-09-11 |
JPWO2017018503A1 (en) | 2018-05-17 |
CN107846944B (en) | 2021-05-14 |
BR112018001514B1 (en) | 2022-05-03 |
WO2017018503A1 (en) | 2017-02-02 |
Similar Documents
Publication | Publication Date | Title |
---|---|---|
Rustad | Utilisation of marine by-products | |
CN107846944A (en) | Edible meat modifying agent | |
Amiza et al. | Optimization of enzymatic protein hydrolysis from silver catfish (Pangasius sp.) frame. | |
Hultmann et al. | Proteolytic activity and properties of proteins in smoked salmon (Salmo salar)—effects of smoking temperature | |
Sriket et al. | Retardation of post-mortem changes of freshwater prawn (Macrobrachium rosenbergii) stored in ice by legume seed extracts | |
JP2003511093A (en) | Protein hydrolyzate produced using marine protease | |
Nikoo et al. | Protein hydrolysates derived from aquaculture and marine byproducts through autolytic hydrolysis | |
JPH10506010A (en) | Method of treating an aqueous protein solution to kill microorganisms therein without causing coagulation | |
Vieira et al. | Production of peptides with radical scavenging activity and recovery of total carotenoids using enzymatic protein hydrolysis of shrimp waste | |
JP3831850B2 (en) | Production method of seafood, shellfish or surimi meat | |
Ramírez | Innovative uses of fisheries by-products | |
CN102948784B (en) | Manufacture process of marinade yak meat | |
KR20160030603A (en) | Using proteolytic enzyme extracted marsh clam extract, and manufacturing method thereof | |
CN107950997A (en) | Sea eel meat tartar sauce and preparation method thereof | |
JP3817125B2 (en) | Method for producing suspension dispersion of meat | |
Ain et al. | Response surface methodology (RSM) identifies the lowest amount of chicken plasma protein (CPP) in surimi-based products with optimum protein solubility, cohesiveness, and whiteness | |
EP1051919B1 (en) | Surimi product and process for preparing same | |
JP2022037925A (en) | Meat modifier, meat modification method, and method for manufacturing modified meat processed food | |
CN1628541A (en) | Method for producing protein mesenchyme originated from animal protein and food containing said protein mesenchyme | |
CN104799134A (en) | Deodorization flavoring agent for fresh food | |
JP2020058291A (en) | Method for producing roe processed product, method for producing cod roe processed product, and texture improving agent for roe | |
JP7456698B2 (en) | Texture improver for protein-containing foods, texture improvement method using same, and method for producing protein-containing foods | |
WO2021167062A1 (en) | Method for meat modification, composition for modification, and food product containing modified meat | |
JPH0526457B2 (en) | ||
KR100440491B1 (en) | Salt-fermented sauce from shrimp processing by-products, and its preparation method |
Legal Events
Date | Code | Title | Description |
---|---|---|---|
PB01 | Publication | ||
PB01 | Publication | ||
SE01 | Entry into force of request for substantive examination | ||
SE01 | Entry into force of request for substantive examination | ||
GR01 | Patent grant | ||
GR01 | Patent grant |