CN108485842A - A kind of edible fruits and vegetables are net and meal wash is net and its preparation method and application - Google Patents
A kind of edible fruits and vegetables are net and meal wash is net and its preparation method and application Download PDFInfo
- Publication number
- CN108485842A CN108485842A CN201810358619.8A CN201810358619A CN108485842A CN 108485842 A CN108485842 A CN 108485842A CN 201810358619 A CN201810358619 A CN 201810358619A CN 108485842 A CN108485842 A CN 108485842A
- Authority
- CN
- China
- Prior art keywords
- net
- protein
- vegetables
- fruits
- meal wash
- 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.)
- Pending
Links
- 235000012054 meals Nutrition 0.000 title claims abstract description 42
- 235000013399 edible fruits Nutrition 0.000 title claims abstract description 16
- 235000013311 vegetables Nutrition 0.000 title claims abstract description 13
- 238000002360 preparation method Methods 0.000 title claims abstract description 11
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 75
- 102000004169 proteins and genes Human genes 0.000 claims abstract description 75
- 108090000765 processed proteins & peptides Proteins 0.000 claims abstract description 73
- 102000004196 processed proteins & peptides Human genes 0.000 claims abstract description 49
- 235000012055 fruits and vegetables Nutrition 0.000 claims abstract description 43
- 108091005804 Peptidases Proteins 0.000 claims abstract description 38
- 239000004365 Protease Substances 0.000 claims abstract description 36
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims abstract description 21
- 235000019750 Crude protein Nutrition 0.000 claims abstract description 17
- 239000000575 pesticide Substances 0.000 claims abstract description 16
- 239000000463 material Substances 0.000 claims abstract description 15
- 239000000447 pesticide residue Substances 0.000 claims abstract description 15
- 238000000108 ultra-filtration Methods 0.000 claims abstract description 8
- 239000012752 auxiliary agent Substances 0.000 claims abstract description 7
- 239000012141 concentrate Substances 0.000 claims abstract description 7
- 239000007788 liquid Substances 0.000 claims abstract description 7
- 239000007787 solid Substances 0.000 claims abstract description 6
- 231100000419 toxicity Toxicity 0.000 claims abstract description 5
- 230000001988 toxicity Effects 0.000 claims abstract description 5
- 238000005904 alkaline hydrolysis reaction Methods 0.000 claims abstract description 4
- 239000012528 membrane Substances 0.000 claims abstract description 4
- 238000001694 spray drying Methods 0.000 claims abstract description 4
- 230000002779 inactivation Effects 0.000 claims abstract description 3
- 239000002994 raw material Substances 0.000 claims abstract description 3
- 238000005292 vacuum distillation Methods 0.000 claims abstract description 3
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 claims abstract 4
- 108090000790 Enzymes Proteins 0.000 claims description 34
- 102000004190 Enzymes Human genes 0.000 claims description 34
- 235000019419 proteases Nutrition 0.000 claims description 22
- 235000010469 Glycine max Nutrition 0.000 claims description 12
- 244000068988 Glycine max Species 0.000 claims description 11
- 235000000346 sugar Nutrition 0.000 claims description 11
- 241000196324 Embryophyta Species 0.000 claims description 9
- 241001465754 Metazoa Species 0.000 claims description 7
- 229920002472 Starch Polymers 0.000 claims description 7
- 235000019698 starch Nutrition 0.000 claims description 7
- 239000008107 starch Substances 0.000 claims description 7
- 239000000344 soap Substances 0.000 claims description 6
- 108010004032 Bromelains Proteins 0.000 claims description 5
- 235000019835 bromelain Nutrition 0.000 claims description 5
- 239000003795 chemical substances by application Substances 0.000 claims description 4
- 230000000813 microbial effect Effects 0.000 claims description 4
- 244000189799 Asimina triloba Species 0.000 claims description 3
- 235000006264 Asimina triloba Nutrition 0.000 claims description 3
- 235000009467 Carica papaya Nutrition 0.000 claims description 3
- 108090000270 Ficain Proteins 0.000 claims description 3
- 229910019142 PO4 Inorganic materials 0.000 claims description 3
- 235000019836 ficin Nutrition 0.000 claims description 3
- POTUGHMKJGOKRI-UHFFFAOYSA-N ficin Chemical compound FI=CI=N POTUGHMKJGOKRI-UHFFFAOYSA-N 0.000 claims description 3
- 238000000746 purification Methods 0.000 claims description 3
- KRKNYBCHXYNGOX-UHFFFAOYSA-K Citrate Chemical compound [O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O KRKNYBCHXYNGOX-UHFFFAOYSA-K 0.000 claims description 2
- 230000003213 activating effect Effects 0.000 claims description 2
- TVHALOSDPLTTSR-UHFFFAOYSA-H hexasodium;[oxido-[oxido(phosphonatooxy)phosphoryl]oxyphosphoryl] phosphate Chemical compound [Na+].[Na+].[Na+].[Na+].[Na+].[Na+].[O-]P([O-])(=O)OP([O-])(=O)OP([O-])(=O)OP([O-])([O-])=O TVHALOSDPLTTSR-UHFFFAOYSA-H 0.000 claims description 2
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 claims description 2
- 239000010452 phosphate Substances 0.000 claims description 2
- 239000003755 preservative agent Substances 0.000 claims description 2
- 230000002335 preservative effect Effects 0.000 claims description 2
- UEUXEKPTXMALOB-UHFFFAOYSA-J tetrasodium;2-[2-[bis(carboxylatomethyl)amino]ethyl-(carboxylatomethyl)amino]acetate Chemical class [Na+].[Na+].[Na+].[Na+].[O-]C(=O)CN(CC([O-])=O)CCN(CC([O-])=O)CC([O-])=O UEUXEKPTXMALOB-UHFFFAOYSA-J 0.000 claims description 2
- 235000018102 proteins Nutrition 0.000 description 54
- 102000035195 Peptidases Human genes 0.000 description 34
- 230000000694 effects Effects 0.000 description 31
- 229940088598 enzyme Drugs 0.000 description 31
- 239000003921 oil Substances 0.000 description 9
- 235000019198 oils Nutrition 0.000 description 9
- 238000000034 method Methods 0.000 description 8
- 239000004094 surface-active agent Substances 0.000 description 8
- 230000007062 hydrolysis Effects 0.000 description 7
- 238000006460 hydrolysis reaction Methods 0.000 description 7
- 229920001184 polypeptide Polymers 0.000 description 7
- 235000013339 cereals Nutrition 0.000 description 6
- 238000002474 experimental method Methods 0.000 description 6
- 239000000047 product Substances 0.000 description 6
- 229940024999 proteolytic enzymes for treatment of wounds and ulcers Drugs 0.000 description 6
- 241000251468 Actinopterygii Species 0.000 description 5
- 108010059378 Endopeptidases Proteins 0.000 description 5
- 102000005593 Endopeptidases Human genes 0.000 description 5
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 5
- 240000007594 Oryza sativa Species 0.000 description 5
- 235000007164 Oryza sativa Nutrition 0.000 description 5
- 108090000526 Papain Proteins 0.000 description 5
- 229940055729 papain Drugs 0.000 description 5
- 235000019834 papain Nutrition 0.000 description 5
- 235000009566 rice Nutrition 0.000 description 5
- 238000003756 stirring Methods 0.000 description 5
- 102000004400 Aminopeptidases Human genes 0.000 description 4
- 108090000915 Aminopeptidases Proteins 0.000 description 4
- 108010038807 Oligopeptides Proteins 0.000 description 4
- 102000015636 Oligopeptides Human genes 0.000 description 4
- 239000000413 hydrolysate Substances 0.000 description 4
- 238000004519 manufacturing process Methods 0.000 description 4
- -1 peptase Proteins 0.000 description 4
- 239000000843 powder Substances 0.000 description 4
- 235000017060 Arachis glabrata Nutrition 0.000 description 3
- 244000105624 Arachis hypogaea Species 0.000 description 3
- 235000010777 Arachis hypogaea Nutrition 0.000 description 3
- 235000018262 Arachis monticola Nutrition 0.000 description 3
- 241000193830 Bacillus <bacterium> Species 0.000 description 3
- 241000194108 Bacillus licheniformis Species 0.000 description 3
- 108010032088 Calpain Proteins 0.000 description 3
- 102000007590 Calpain Human genes 0.000 description 3
- 108010006303 Carboxypeptidases Proteins 0.000 description 3
- 102000005367 Carboxypeptidases Human genes 0.000 description 3
- 101710180012 Protease 7 Proteins 0.000 description 3
- 108090000783 Renin Proteins 0.000 description 3
- 102100028255 Renin Human genes 0.000 description 3
- 238000007792 addition Methods 0.000 description 3
- KRKNYBCHXYNGOX-UHFFFAOYSA-N citric acid Chemical compound OC(=O)CC(O)(C(O)=O)CC(O)=O KRKNYBCHXYNGOX-UHFFFAOYSA-N 0.000 description 3
- 239000012459 cleaning agent Substances 0.000 description 3
- 239000000835 fiber Substances 0.000 description 3
- 235000013305 food Nutrition 0.000 description 3
- 239000004615 ingredient Substances 0.000 description 3
- 239000008267 milk Substances 0.000 description 3
- 210000004080 milk Anatomy 0.000 description 3
- 235000020232 peanut Nutrition 0.000 description 3
- 231100000614 poison Toxicity 0.000 description 3
- 239000007858 starting material Substances 0.000 description 3
- 244000099147 Ananas comosus Species 0.000 description 2
- 235000007119 Ananas comosus Nutrition 0.000 description 2
- 241000228212 Aspergillus Species 0.000 description 2
- 241000131386 Aspergillus sojae Species 0.000 description 2
- 240000002791 Brassica napus Species 0.000 description 2
- 235000004977 Brassica sinapistrum Nutrition 0.000 description 2
- 108010080937 Carboxypeptidases A Proteins 0.000 description 2
- 102000000496 Carboxypeptidases A Human genes 0.000 description 2
- 108090000317 Chymotrypsin Proteins 0.000 description 2
- 102000008186 Collagen Human genes 0.000 description 2
- 108010035532 Collagen Proteins 0.000 description 2
- 108010016626 Dipeptides Proteins 0.000 description 2
- 102000018389 Exopeptidases Human genes 0.000 description 2
- 108010091443 Exopeptidases Proteins 0.000 description 2
- 108010088842 Fibrinolysin Proteins 0.000 description 2
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 2
- 102000009127 Glutaminase Human genes 0.000 description 2
- 108010073324 Glutaminase Proteins 0.000 description 2
- 108060005986 Granzyme Proteins 0.000 description 2
- 102000001398 Granzyme Human genes 0.000 description 2
- 102000002704 Leucyl aminopeptidase Human genes 0.000 description 2
- 108010004098 Leucyl aminopeptidase Proteins 0.000 description 2
- 240000003183 Manihot esculenta Species 0.000 description 2
- 235000016735 Manihot esculenta subsp esculenta Nutrition 0.000 description 2
- 241000194105 Paenibacillus polymyxa Species 0.000 description 2
- 108090000284 Pepsin A Proteins 0.000 description 2
- 102000057297 Pepsin A Human genes 0.000 description 2
- 244000046052 Phaseolus vulgaris Species 0.000 description 2
- 235000010627 Phaseolus vulgaris Nutrition 0.000 description 2
- ISRUGXGCCGIOQO-UHFFFAOYSA-N Rhoden Chemical compound CNC(=O)OC1=CC=CC=C1OC(C)C ISRUGXGCCGIOQO-UHFFFAOYSA-N 0.000 description 2
- 108010022999 Serine Proteases Proteins 0.000 description 2
- 102000012479 Serine Proteases Human genes 0.000 description 2
- 108010056079 Subtilisins Proteins 0.000 description 2
- 102000005158 Subtilisins Human genes 0.000 description 2
- 235000001014 amino acid Nutrition 0.000 description 2
- 150000001413 amino acids Chemical class 0.000 description 2
- 239000008280 blood Substances 0.000 description 2
- 210000004369 blood Anatomy 0.000 description 2
- 239000006227 byproduct Substances 0.000 description 2
- 230000008859 change Effects 0.000 description 2
- 229920001436 collagen Polymers 0.000 description 2
- 230000000052 comparative effect Effects 0.000 description 2
- 230000000295 complement effect Effects 0.000 description 2
- 238000005238 degreasing Methods 0.000 description 2
- 238000001035 drying Methods 0.000 description 2
- 238000000605 extraction Methods 0.000 description 2
- 238000000855 fermentation Methods 0.000 description 2
- 230000004151 fermentation Effects 0.000 description 2
- 239000000706 filtrate Substances 0.000 description 2
- 239000008103 glucose Substances 0.000 description 2
- 238000011534 incubation Methods 0.000 description 2
- 244000005700 microbiome Species 0.000 description 2
- 235000013336 milk Nutrition 0.000 description 2
- 229940111202 pepsin Drugs 0.000 description 2
- 235000021317 phosphate Nutrition 0.000 description 2
- 229940012957 plasmin Drugs 0.000 description 2
- 230000008569 process Effects 0.000 description 2
- 235000019833 protease Nutrition 0.000 description 2
- 230000006920 protein precipitation Effects 0.000 description 2
- 239000000126 substance Substances 0.000 description 2
- 239000008399 tap water Substances 0.000 description 2
- 235000020679 tap water Nutrition 0.000 description 2
- 210000001519 tissue Anatomy 0.000 description 2
- 231100000331 toxic Toxicity 0.000 description 2
- 230000002588 toxic effect Effects 0.000 description 2
- 239000003440 toxic substance Substances 0.000 description 2
- 238000005406 washing Methods 0.000 description 2
- UUUHXMGGBIUAPW-UHFFFAOYSA-N 1-[1-[2-[[5-amino-2-[[1-[5-(diaminomethylideneamino)-2-[[1-[3-(1h-indol-3-yl)-2-[(5-oxopyrrolidine-2-carbonyl)amino]propanoyl]pyrrolidine-2-carbonyl]amino]pentanoyl]pyrrolidine-2-carbonyl]amino]-5-oxopentanoyl]amino]-3-methylpentanoyl]pyrrolidine-2-carbon Chemical compound C1CCC(C(=O)N2C(CCC2)C(O)=O)N1C(=O)C(C(C)CC)NC(=O)C(CCC(N)=O)NC(=O)C1CCCN1C(=O)C(CCCN=C(N)N)NC(=O)C1CCCN1C(=O)C(CC=1C2=CC=CC=C2NC=1)NC(=O)C1CCC(=O)N1 UUUHXMGGBIUAPW-UHFFFAOYSA-N 0.000 description 1
- CUVGUPIVTLGRGI-UHFFFAOYSA-N 4-(3-phosphonopropyl)piperazine-2-carboxylic acid Chemical compound OC(=O)C1CN(CCCP(O)(O)=O)CCN1 CUVGUPIVTLGRGI-UHFFFAOYSA-N 0.000 description 1
- LKDMKWNDBAVNQZ-UHFFFAOYSA-N 4-[[1-[[1-[2-[[1-(4-nitroanilino)-1-oxo-3-phenylpropan-2-yl]carbamoyl]pyrrolidin-1-yl]-1-oxopropan-2-yl]amino]-1-oxopropan-2-yl]amino]-4-oxobutanoic acid Chemical compound OC(=O)CCC(=O)NC(C)C(=O)NC(C)C(=O)N1CCCC1C(=O)NC(C(=O)NC=1C=CC(=CC=1)[N+]([O-])=O)CC1=CC=CC=C1 LKDMKWNDBAVNQZ-UHFFFAOYSA-N 0.000 description 1
- 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 1
- ODHCTXKNWHHXJC-VKHMYHEASA-N 5-oxo-L-proline Chemical compound OC(=O)[C@@H]1CCC(=O)N1 ODHCTXKNWHHXJC-VKHMYHEASA-N 0.000 description 1
- 206010001497 Agitation Diseases 0.000 description 1
- 108010001779 Ancrod Proteins 0.000 description 1
- 108700016171 Aspartate ammonia-lyases Proteins 0.000 description 1
- 108091005502 Aspartic proteases Proteins 0.000 description 1
- 102000035101 Aspartic proteases Human genes 0.000 description 1
- 240000006439 Aspergillus oryzae Species 0.000 description 1
- 235000002247 Aspergillus oryzae Nutrition 0.000 description 1
- 241000228251 Aspergillus phoenicis Species 0.000 description 1
- 244000063299 Bacillus subtilis Species 0.000 description 1
- 235000014469 Bacillus subtilis Nutrition 0.000 description 1
- 241000345998 Calamus manan Species 0.000 description 1
- 108090000397 Caspase 3 Proteins 0.000 description 1
- 102000004018 Caspase 6 Human genes 0.000 description 1
- 108090000425 Caspase 6 Proteins 0.000 description 1
- 108090000567 Caspase 7 Proteins 0.000 description 1
- 108090000426 Caspase-1 Proteins 0.000 description 1
- 102100035904 Caspase-1 Human genes 0.000 description 1
- 102000004068 Caspase-10 Human genes 0.000 description 1
- 108090000572 Caspase-10 Proteins 0.000 description 1
- 102000004046 Caspase-2 Human genes 0.000 description 1
- 108090000552 Caspase-2 Proteins 0.000 description 1
- 102100029855 Caspase-3 Human genes 0.000 description 1
- 102100025597 Caspase-4 Human genes 0.000 description 1
- 101710090338 Caspase-4 Proteins 0.000 description 1
- 102100038916 Caspase-5 Human genes 0.000 description 1
- 101710090333 Caspase-5 Proteins 0.000 description 1
- 102100038902 Caspase-7 Human genes 0.000 description 1
- 102100026548 Caspase-8 Human genes 0.000 description 1
- 108090000538 Caspase-8 Proteins 0.000 description 1
- 102100026550 Caspase-9 Human genes 0.000 description 1
- 108090000566 Caspase-9 Proteins 0.000 description 1
- 102000011727 Caspases Human genes 0.000 description 1
- 108010076667 Caspases Proteins 0.000 description 1
- 108010059081 Cathepsin A Proteins 0.000 description 1
- 102000005572 Cathepsin A Human genes 0.000 description 1
- 108090000712 Cathepsin B Proteins 0.000 description 1
- 102000004225 Cathepsin B Human genes 0.000 description 1
- 102000003902 Cathepsin C Human genes 0.000 description 1
- 108090000267 Cathepsin C Proteins 0.000 description 1
- 102000003908 Cathepsin D Human genes 0.000 description 1
- 108090000258 Cathepsin D Proteins 0.000 description 1
- 108090000617 Cathepsin G Proteins 0.000 description 1
- 102000004173 Cathepsin G Human genes 0.000 description 1
- 108090000619 Cathepsin H Proteins 0.000 description 1
- 102000004175 Cathepsin H Human genes 0.000 description 1
- 235000007516 Chrysanthemum Nutrition 0.000 description 1
- 244000189548 Chrysanthemum x morifolium Species 0.000 description 1
- 108090001069 Chymopapain Proteins 0.000 description 1
- 235000005979 Citrus limon Nutrition 0.000 description 1
- 244000131522 Citrus pyriformis Species 0.000 description 1
- 108090000044 Complement Factor I Proteins 0.000 description 1
- 108090000059 Complement factor D Proteins 0.000 description 1
- 102000003706 Complement factor D Human genes 0.000 description 1
- 102100035431 Complement factor I Human genes 0.000 description 1
- 239000005946 Cypermethrin Substances 0.000 description 1
- 241000252233 Cyprinus carpio Species 0.000 description 1
- 102000005927 Cysteine Proteases Human genes 0.000 description 1
- 108010005843 Cysteine Proteases Proteins 0.000 description 1
- 108090001081 Dipeptidases Proteins 0.000 description 1
- 102000004860 Dipeptidases Human genes 0.000 description 1
- 102000002322 Egg Proteins Human genes 0.000 description 1
- 108010000912 Egg Proteins Proteins 0.000 description 1
- 108010067770 Endopeptidase K Proteins 0.000 description 1
- 108010013369 Enteropeptidase Proteins 0.000 description 1
- 102100029727 Enteropeptidase Human genes 0.000 description 1
- 108010074860 Factor Xa Proteins 0.000 description 1
- 108010073385 Fibrin Proteins 0.000 description 1
- 102000009123 Fibrin Human genes 0.000 description 1
- BWGVNKXGVNDBDI-UHFFFAOYSA-N Fibrin monomer Chemical compound CNC(=O)CNC(=O)CN BWGVNKXGVNDBDI-UHFFFAOYSA-N 0.000 description 1
- 108010058643 Fungal Proteins Proteins 0.000 description 1
- 108090001126 Furin Proteins 0.000 description 1
- 102000004961 Furin Human genes 0.000 description 1
- 108010051815 Glutamyl endopeptidase Proteins 0.000 description 1
- MVORZMQFXBLMHM-QWRGUYRKSA-N Gly-His-Lys Chemical compound NCCCC[C@@H](C(O)=O)NC(=O)[C@@H](NC(=O)CN)CC1=CN=CN1 MVORZMQFXBLMHM-QWRGUYRKSA-N 0.000 description 1
- PMMYEEVYMWASQN-DMTCNVIQSA-N Hydroxyproline Chemical compound O[C@H]1CN[C@H](C(O)=O)C1 PMMYEEVYMWASQN-DMTCNVIQSA-N 0.000 description 1
- 108060005987 Kallikrein Proteins 0.000 description 1
- 102000001399 Kallikrein Human genes 0.000 description 1
- 101710094902 Legumin Proteins 0.000 description 1
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 1
- 101001018085 Lysobacter enzymogenes Lysyl endopeptidase Proteins 0.000 description 1
- 108010000684 Matrix Metalloproteinases Proteins 0.000 description 1
- 102000002274 Matrix Metalloproteinases Human genes 0.000 description 1
- 102000005741 Metalloproteases Human genes 0.000 description 1
- 108010006035 Metalloproteases Proteins 0.000 description 1
- 241000526657 Microchloa Species 0.000 description 1
- RCEAADKTGXTDOA-UHFFFAOYSA-N OS(O)(=O)=O.CCCCCCCCCCCC[Na] Chemical compound OS(O)(=O)=O.CCCCCCCCCCCC[Na] RCEAADKTGXTDOA-UHFFFAOYSA-N 0.000 description 1
- 241001560086 Pachyrhizus Species 0.000 description 1
- 235000019483 Peanut oil Nutrition 0.000 description 1
- 108090000882 Peptidyl-Dipeptidase A Proteins 0.000 description 1
- 102000004270 Peptidyl-Dipeptidase A Human genes 0.000 description 1
- 108010059712 Pronase Proteins 0.000 description 1
- 108010072866 Prostate-Specific Antigen Proteins 0.000 description 1
- 102100038358 Prostate-specific antigen Human genes 0.000 description 1
- 101710180313 Protease 3 Proteins 0.000 description 1
- 102000004245 Proteasome Endopeptidase Complex Human genes 0.000 description 1
- 108090000708 Proteasome Endopeptidase Complex Proteins 0.000 description 1
- 102000001253 Protein Kinase Human genes 0.000 description 1
- ODHCTXKNWHHXJC-GSVOUGTGSA-N Pyroglutamic acid Natural products OC(=O)[C@H]1CCC(=O)N1 ODHCTXKNWHHXJC-GSVOUGTGSA-N 0.000 description 1
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 1
- 108090000083 Serine Endopeptidases Proteins 0.000 description 1
- 102000003667 Serine Endopeptidases Human genes 0.000 description 1
- 244000061456 Solanum tuberosum Species 0.000 description 1
- 235000002595 Solanum tuberosum Nutrition 0.000 description 1
- 108010073771 Soybean Proteins Proteins 0.000 description 1
- 241000187392 Streptomyces griseus Species 0.000 description 1
- 229930006000 Sucrose Natural products 0.000 description 1
- CZMRCDWAGMRECN-UGDNZRGBSA-N Sucrose Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 CZMRCDWAGMRECN-UGDNZRGBSA-N 0.000 description 1
- 239000005864 Sulphur Substances 0.000 description 1
- 108090001109 Thermolysin Proteins 0.000 description 1
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 1
- 239000004473 Threonine Substances 0.000 description 1
- ISWQCIVKKSOKNN-UHFFFAOYSA-L Tiron Chemical compound [Na+].[Na+].OC1=CC(S([O-])(=O)=O)=CC(S([O-])(=O)=O)=C1O ISWQCIVKKSOKNN-UHFFFAOYSA-L 0.000 description 1
- 235000021307 Triticum Nutrition 0.000 description 1
- 244000098338 Triticum aestivum Species 0.000 description 1
- 108090000435 Urokinase-type plasminogen activator Proteins 0.000 description 1
- 102000003990 Urokinase-type plasminogen activator Human genes 0.000 description 1
- 240000004922 Vigna radiata Species 0.000 description 1
- 235000010721 Vigna radiata var radiata Nutrition 0.000 description 1
- 235000011469 Vigna radiata var sublobata Nutrition 0.000 description 1
- 240000001417 Vigna umbellata Species 0.000 description 1
- 235000011453 Vigna umbellata Nutrition 0.000 description 1
- 240000008042 Zea mays Species 0.000 description 1
- 235000005824 Zea mays ssp. parviglumis Nutrition 0.000 description 1
- 235000002017 Zea mays subsp mays Nutrition 0.000 description 1
- 101710151579 Zinc metalloproteinase Proteins 0.000 description 1
- NCSHGROOCJHAFK-UHFFFAOYSA-N [Cl].N#CC#N Chemical compound [Cl].N#CC#N NCSHGROOCJHAFK-UHFFFAOYSA-N 0.000 description 1
- ODHCTXKNWHHXJC-UHFFFAOYSA-N acide pyroglutamique Natural products OC(=O)C1CCC(=O)N1 ODHCTXKNWHHXJC-UHFFFAOYSA-N 0.000 description 1
- 230000004913 activation Effects 0.000 description 1
- 125000002252 acyl group Chemical group 0.000 description 1
- 238000013019 agitation Methods 0.000 description 1
- 239000003513 alkali Substances 0.000 description 1
- 150000001408 amides Chemical class 0.000 description 1
- 150000001412 amines Chemical class 0.000 description 1
- 229960004233 ancrod Drugs 0.000 description 1
- 235000021120 animal protein Nutrition 0.000 description 1
- 239000003945 anionic surfactant Substances 0.000 description 1
- 239000007864 aqueous solution Substances 0.000 description 1
- 239000002585 base Substances 0.000 description 1
- WQZGKKKJIJFFOK-VFUOTHLCSA-N beta-D-glucose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-VFUOTHLCSA-N 0.000 description 1
- VEMKTZHHVJILDY-UXHICEINSA-N bioresmethrin Chemical class CC1(C)[C@H](C=C(C)C)[C@H]1C(=O)OCC1=COC(CC=2C=CC=CC=2)=C1 VEMKTZHHVJILDY-UXHICEINSA-N 0.000 description 1
- 235000019658 bitter taste Nutrition 0.000 description 1
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 1
- 108010054847 carboxypeptidase P Proteins 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 238000006757 chemical reactions by type Methods 0.000 description 1
- 229960002976 chymopapain Drugs 0.000 description 1
- 229960002376 chymotrypsin Drugs 0.000 description 1
- 235000005822 corn Nutrition 0.000 description 1
- 108090000200 cucumisin Proteins 0.000 description 1
- KAATUXNTWXVJKI-UHFFFAOYSA-N cypermethrin Chemical compound CC1(C)C(C=C(Cl)Cl)C1C(=O)OC(C#N)C1=CC=CC(OC=2C=CC=CC=2)=C1 KAATUXNTWXVJKI-UHFFFAOYSA-N 0.000 description 1
- 229960005424 cypermethrin Drugs 0.000 description 1
- 210000000172 cytosol Anatomy 0.000 description 1
- 239000003599 detergent Substances 0.000 description 1
- 238000004851 dishwashing Methods 0.000 description 1
- NEKNNCABDXGBEN-UHFFFAOYSA-L disodium;4-(4-chloro-2-methylphenoxy)butanoate;4-(2,4-dichlorophenoxy)butanoate Chemical compound [Na+].[Na+].CC1=CC(Cl)=CC=C1OCCCC([O-])=O.[O-]C(=O)CCCOC1=CC=C(Cl)C=C1Cl NEKNNCABDXGBEN-UHFFFAOYSA-L 0.000 description 1
- PMMYEEVYMWASQN-UHFFFAOYSA-N dl-hydroxyproline Natural products OC1C[NH2+]C(C([O-])=O)C1 PMMYEEVYMWASQN-UHFFFAOYSA-N 0.000 description 1
- 230000035622 drinking Effects 0.000 description 1
- 235000014103 egg white Nutrition 0.000 description 1
- 210000000969 egg white Anatomy 0.000 description 1
- 235000013601 eggs Nutrition 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 229950003499 fibrin Drugs 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- 108010062699 gamma-Glutamyl Hydrolase Proteins 0.000 description 1
- 102000034356 gene-regulatory proteins Human genes 0.000 description 1
- 108091006104 gene-regulatory proteins Proteins 0.000 description 1
- 235000021474 generally recognized As safe (food) Nutrition 0.000 description 1
- 235000021473 generally recognized as safe (food ingredients) Nutrition 0.000 description 1
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 1
- 108010038983 glycyl-histidyl-lysine Proteins 0.000 description 1
- 229940043257 glycylglycine Drugs 0.000 description 1
- 239000004519 grease Substances 0.000 description 1
- 230000036541 health Effects 0.000 description 1
- 238000010438 heat treatment Methods 0.000 description 1
- 230000002949 hemolytic effect Effects 0.000 description 1
- 125000004836 hexamethylene group Chemical group [H]C([H])([*:2])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])[*:1] 0.000 description 1
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 1
- 230000003301 hydrolyzing effect Effects 0.000 description 1
- 229960002591 hydroxyproline Drugs 0.000 description 1
- 230000036039 immunity Effects 0.000 description 1
- 239000012535 impurity Substances 0.000 description 1
- 230000000749 insecticidal effect Effects 0.000 description 1
- 239000002917 insecticide Substances 0.000 description 1
- 238000011835 investigation Methods 0.000 description 1
- 150000002632 lipids Chemical class 0.000 description 1
- 235000013372 meat Nutrition 0.000 description 1
- 108010003855 mesentericopeptidase Proteins 0.000 description 1
- 229910052751 metal Inorganic materials 0.000 description 1
- 239000002184 metal Substances 0.000 description 1
- NNKVPIKMPCQWCG-UHFFFAOYSA-N methamidophos Chemical compound COP(N)(=O)SC NNKVPIKMPCQWCG-UHFFFAOYSA-N 0.000 description 1
- 108010009355 microbial metalloproteinases Proteins 0.000 description 1
- 210000001589 microsome Anatomy 0.000 description 1
- 238000002156 mixing Methods 0.000 description 1
- 239000000203 mixture Substances 0.000 description 1
- 231100000252 nontoxic Toxicity 0.000 description 1
- 230000003000 nontoxic effect Effects 0.000 description 1
- 229920001542 oligosaccharide Polymers 0.000 description 1
- 150000002482 oligosaccharides Chemical class 0.000 description 1
- 150000007524 organic acids Chemical class 0.000 description 1
- 210000000496 pancreas Anatomy 0.000 description 1
- 235000020265 peanut milk Nutrition 0.000 description 1
- 239000000312 peanut oil Substances 0.000 description 1
- 235000021118 plant-derived protein Nutrition 0.000 description 1
- 239000002574 poison Substances 0.000 description 1
- 238000012545 processing Methods 0.000 description 1
- 230000002035 prolonged effect Effects 0.000 description 1
- 108010017314 prolyl dipeptidase Proteins 0.000 description 1
- 108010043535 protease S Proteins 0.000 description 1
- 235000004252 protein component Nutrition 0.000 description 1
- 230000007065 protein hydrolysis Effects 0.000 description 1
- 108060006633 protein kinase Proteins 0.000 description 1
- 230000017854 proteolysis Effects 0.000 description 1
- 235000012950 rattan cane Nutrition 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 238000007789 sealing Methods 0.000 description 1
- 108010059841 serine carboxypeptidase Proteins 0.000 description 1
- 239000002893 slag Substances 0.000 description 1
- 238000002791 soaking Methods 0.000 description 1
- 230000007928 solubilization Effects 0.000 description 1
- 238000005063 solubilization Methods 0.000 description 1
- 239000000243 solution Substances 0.000 description 1
- 229940001941 soy protein Drugs 0.000 description 1
- 238000003860 storage Methods 0.000 description 1
- 239000005720 sucrose Substances 0.000 description 1
- 235000020238 sunflower seed Nutrition 0.000 description 1
- 239000004557 technical material Substances 0.000 description 1
- 238000010998 test method Methods 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- 230000035922 thirst Effects 0.000 description 1
- FGMPLJWBKKVCDB-UHFFFAOYSA-N trans-L-hydroxy-proline Natural products ON1CCCC1C(O)=O FGMPLJWBKKVCDB-UHFFFAOYSA-N 0.000 description 1
- 229960005356 urokinase Drugs 0.000 description 1
- 238000009834 vaporization Methods 0.000 description 1
- 230000008016 vaporization Effects 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
- C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
- C11D7/00—Compositions of detergents based essentially on non-surface-active compounds
- C11D7/22—Organic compounds
- C11D7/32—Organic compounds containing nitrogen
- C11D7/3263—Amides or imides
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
- A23J3/00—Working-up of proteins for foodstuffs
- A23J3/30—Working-up of proteins for foodstuffs by hydrolysis
- A23J3/32—Working-up of proteins for foodstuffs by hydrolysis using chemical agents
- A23J3/34—Working-up of proteins for foodstuffs by hydrolysis using chemical agents using enzymes
-
- 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
- A23L5/00—Preparation or treatment of foods or foodstuffs, in general; Food or foodstuffs obtained thereby; Materials therefor
- A23L5/20—Removal of unwanted matter, e.g. deodorisation or detoxification
- A23L5/27—Removal of unwanted matter, e.g. deodorisation or detoxification by chemical treatment, by adsorption or by absorption
-
- C—CHEMISTRY; METALLURGY
- C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
- C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
- C11D10/00—Compositions of detergents, not provided for by one single preceding group
-
- C—CHEMISTRY; METALLURGY
- C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
- C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
- C11D10/00—Compositions of detergents, not provided for by one single preceding group
- C11D10/04—Compositions of detergents, not provided for by one single preceding group based on mixtures of surface-active non-soap compounds and soap
-
- C—CHEMISTRY; METALLURGY
- C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
- C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
- C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
- C11D3/16—Organic compounds
- C11D3/37—Polymers
- C11D3/3703—Macromolecular compounds obtained otherwise than by reactions only involving carbon-to-carbon unsaturated bonds
- C11D3/3719—Polyamides or polyimides
-
- C—CHEMISTRY; METALLURGY
- C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
- C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
- C11D2111/00—Cleaning compositions characterised by the objects to be cleaned; Cleaning compositions characterised by non-standard cleaning or washing processes
- C11D2111/10—Objects to be cleaned
- C11D2111/14—Hard surfaces
Landscapes
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Engineering & Computer Science (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Organic Chemistry (AREA)
- Wood Science & Technology (AREA)
- Oil, Petroleum & Natural Gas (AREA)
- Health & Medical Sciences (AREA)
- Nutrition Science (AREA)
- Food Science & Technology (AREA)
- Polymers & Plastics (AREA)
- General Chemical & Material Sciences (AREA)
- Biochemistry (AREA)
- Detergent Compositions (AREA)
Abstract
The invention discloses a kind of edible fruits and vegetables only and meal wash is net, including protein peptides, and the molecular weight of protein peptides is 500 100000D.Invention also discloses the preparation methods that fruits and vegetables are net and meal wash is net, include the following steps:Extract the crude protein in protein material;Above-mentioned crude protein is digested with protease, alkaline hydrolysis, acidolysis, Ultra filtration membrane obtains protein peptides of the molecular weight between 500 100000D;Above-mentioned protein peptides obtain protein peptides concentrate or pulvis by vacuum distillation, ultrafiltration membrance filter or spray drying;Using above-mentioned protein peptides concentrate or pulvis as raw material heat inactivation, be directly prepared into liquid or solid, powdery fruits and vegetables it is net/meal wash is net;After protein peptides are purified, after auxiliary agent is added, obtain liquid or solid, powdery fruits and vegetables it is net/meal wash is net.The problem of the present invention discloses its application, the greasy dirt in water can be effectively removed, remove pesticide residue, reduce toxicity of pesticide, avoid common meal wash net secondary pollution.
Description
Technical field
The invention belongs to filed of daily-use chemical industry, and in particular to a kind of edible fruits and vegetables are net and meal wash is net and preparation method thereof
Application.
Background technology
Fruit, vegetable pesticide residue are a global problems, and limited resources support the population of the vast number of growth, can not
Leave pesticide.People's use fruits and vegetables made of surfactant are made a return journey only removes water fruits and vegetables pesticide residue, and effect is pretty good.But
It is that the surfactant that fruits and vegetables contain only can remain in water fruits and vegetables, brings new pollution.Anion surfactant has
There are certain hemolytic, some surfactants also toxic side effect, the safe and healthy risk brought to be increasingly subject to all circles
Concern.Meal wash also faces same problem only.People are net to the even edible fruits and vegetables of totally nontoxic and meal wash net demand is non-
It is often urgent.And the secondary pollution problem of the dishwashing detergent of infant, parent are concerned about very much, thirst for very much without the secondary work of any poison
Meal wash is net.
The fruits and vegetables that food-borne material makes are net or meal wash is net, are highly safe, many people have carried out this largely
Research and production.But unfortunately, with traditional fruits and vegetables net phase ratio by surfactant formulatory, it is residual to remove pesticide
It stays or the effect of greasy dirt is poor, it is unsatisfactory.
Food-borne enzymolysis protein peptide is highly safe, and having reduces blood fat, blood glucose, improves efficacy of immunity, makees
Enter people’s lives for health products.Pig collagen hydrolysate by soybean oligopeptide, is recognized as by U.S. FDA for 1999 for 2003
The component substances of GRAS safety formulas, China in 2004 by soy oligosaccharides Gly-His-Lys, 2007 by fish oligopeptide powder, as food
Dispensing has formulated national proposed standard.Food-borne enzymolysis protein peptide food, it is highly safe to have no toxic side effect, trusted by people.
Invention content
To solve the above problems, the present inventor has studied a kind of edible fruits and vegetables by further investigation and many experiments
Net and meal wash is net, which can effectively remove the greasy dirt in water, can also effectively remove pesticide residue, reduces toxicity of pesticide, keeps away
The problem of having exempted from common meal wash net secondary pollution.
The invention discloses a kind of edible fruits and vegetables are net and meal wash is net, including protein peptides, the molecular weight of protein peptides are
500-100000D。
The fruits and vegetables are net and auxiliary agent can also be added in meal wash only, and auxiliary agent is water and surfactant, soya-bean oil soap, phosphatide, sugar, shallow lake
Powder, protein, citrate, EDETATE SODIUM salt, phosphate, Quadrafos water softener, it is a kind of in anti-agglomerating agent and preservative or one
Kind or more.
Preferably, the protein peptides are plant-derived albumen peptide, animal derived protein peptide or microbial protein peptide.
The preparation method that fruits and vegetables described above are net and meal wash is net, includes the following steps:
(1)Extract the crude protein in protein material;
(2)Above-mentioned crude protein is digested with protease, alkaline hydrolysis, acidolysis, the Ultra filtration membrane of the different cutoff values of protein peptides,
Obtain different molecular weight section protein peptides, as oligopeptide (molecular weight≤500D), polypeptide (molecular weight 500D~100000D), compared with
Macromolecular peptide (molecular weight >=100000D) selects polypeptide (molecular weight 500D~100000D), the protein peptides as needed;
(3)By the protein peptides of above-mentioned molecular weight 500D~100000D by vacuum distillation, ultrafiltration membrance filter or spray drying, obtain
To protein peptides concentrate or pulvis;
(4)Using above-mentioned protein peptides concentrate or pulvis as raw material heat inactivation, be directly prepared into liquid or solid, powdery fruits and vegetables it is net/
Meal wash is net;
(5)By step(2)In protein peptides purification after, after auxiliary agent is added, obtain liquid or solid, powdery fruits and vegetables it is net/meal wash
Only.
Protein is universally present in plant, animal, microorganism, seed, leaf, stem, root, the skin of plant, animal
Meat, skin, hair, milk and microorganism etc., all contain protein, can extract protein.
The seed of oil crops, including soybean, peanut, rapeseed, sunflower seeds, the dregs of rice after extract oil, protein content is more
It is high.
Vinasse with grain fermentation manufacture alcohol or after drinking, sugar are decomposed, protein content higher.
The grain fermented with grain after manufacturing organic acid, sugar, protein content higher.
Protein is more stable in pH10 or less, can dissolve under alkaline condition, is precipitated at its isoelectric pH 4~5,
Using this property, extract containing the protein in protein material.
Step(1)Described in protein material include plant-derived albumen material, animal derived protein material, microbial protein
Material.
The plant-derived albumen material, plant-derived albumen material include the oilseeds such as soybean, peanut, rapeseed or
Dregs of rice etc., red bean, mung bean, black soya bean, pea, etc. beans, the cereals such as corn, rice, wheat, the potatos such as pachyrhizus, cassava also include
The grains fermentation industry by-product such as grain, oil, food processing, alcohol, citric acid, glucose dregs of beans, peanut meal, the rape dregs of rice, cassava
The by-products such as slag, lemon dregs also include plant base of leaf root and water fruits and vegetables;Before extracting plant-derived protein, first taken off
Fat can be used hexamethylene and detach lipid solubilization.The seed of oil crops can squeeze extraction grease, the dregs of rice after extraction, but fat
Fat residual is higher.Then it smashes to required granularity, solubilising protein, 6~48h, are filtered to remove fiber under alkaline condition, adjust
Filtrate PH4~5, protein precipitation, filtering obtain crude protein.A small amount of impurity such as fiber, sugar, starch can be contained in crude protein,
Have no effect on the effect of the present invention.
The animal protein materials such as the animal derived protein material, including fish, milk, animal flesh, skin, hair;Protein content
After height, alkali degreasing or sour ash disposal, after heating is fully hydrolyzed, enzyme hydrolysis.
The microbial protein material, including Yeast protein, can directly enzyme hydrolysis.
Crude protein, it is also possible to which commercial goods albumen powder replaces.
The step(2)In one kind in papain, bromelain and ficin of protease
Or more than one.Papain, bromelain, ficin can also be replaced with pawpaw, pineapple, fig.
The step(2)In, the mass ratio of protease addition and crude protein is:0.5-3:20, mmp reaction when
Between be 1-48 hours.The enzyme that enough units should be used, to obtain substantive hydrolysis.The amount of enzyme is selected, it is enough to ensure
Activity, and avoid generating bitter taste.Content used depends on the activity of enzyme.
Useful enzyme Bao Kuo be in aminosal key proteolytic enzyme.
Proteolytic enzyme preparation usually contains protease, and aminosal forms small peptide and peptase, hydrolyzes little albumen
Matter or peptide usually discharge amino acid from its end.Usually by with endopeptidase and endopeptidase activity protease and peptase include
In such preparation, with effectively out of each protein and obtained peptide or from each protein and obtained peptide
End decomposing protein.
Useful proteolytic enzyme includes, but are not limited to have one or more following active enzymes:
Protease, peptase, glutaminase (include, but are not limited to L-Glutamine-amino-hydrolase (EC3.5.1.2)),
Interior protease, serine endopeptidase, bacillus subtilis peptidase (EC 3.4.21.62).
Other proteolytic enzymes are also useful, and are much known and are obtainable;Following present one
A little others types and example.
Proteolytic enzyme (also referred to as proteinase, protease or peptase) is attributed in six groups at present, including serine protease,
Serine/threonine protein enzyme, cysteine proteinase, aspartic protease, metalloproteinases and hydroxyproline enzyme.Proteolysis
Enzyme can cut (exopeptidase) in the end of protein or attack the inside peptide bond (endopeptidase) of protein.Exopeptidase includes, but
It is not limited to, aminopeptidase, carboxypeptidase and carboxypeptidase A.Endopeptidase includes, but are not limited to trypsase, chymotrypsin protein
Enzyme, pepsin, papain and elastoser.
Proteolytic enzyme is sorted out into (EC 3.4 and EC3.5) by EC numbers (enzyme committee numbering), each classification includes
The various known enzymes of specific reaction type.
EC 3.4 includes acting on the enzyme (peptase/protease) of peptide bond, and EC 3.5 includes acting on carbon-nitrogen bond and non-peptide bond
Enzyme.The example of EC 3.4 includes, but are not limited to below:Aminopeptidase (EC 3.4.11), dipeptidase (3.4.13), dipeptides
Acyl-peptase (3 .4 .14), peptide acyl-dipeptidase (3 .4 .15), serine-carboxypeptidase (3 .4 .16), metal carboxyl peptide
Enzyme (3.4.17), cysteine-carboxypeptidase (3.4.18), acyl peptase (3.4.19), serine-endopeptidase (3.4.21), half
Cystine-endopeptidase (3.4.22), aspartic acid-endopeptidase (3.4.23), Zinc metalloproteinase (3.4.24), the interior peptide of threonine-
Enzyme (3.4.25).
The example of EC 3.5 includes, but are not limited to cut the proteolytic enzyme (3.5.1) of linear amide, for example, glutamy
Amine enzyme (EC 3.5.1.2).
Various proteolytic enzymes are commercially available;Proteolytic enzyme below can be obtained from Sigma-Aldrich:
Colour killing peptase, aminopeptidase, ancrod, angiotensin converting enzyme, bromelain, calpain,
Calpain I, calpain II, carboxypeptidase A, carboxypeptidase, carboxypeptidase G, carboxypeptidase P,
Carboxypeptidase W, carboxypeptidase Y, caspase, caspase 1, caspase 2, Caspase-3, caspase
4, caspase 5, caspase 6, caspase 7, caspase 8, caspase 9, caspase 10, half
Guang aspartase 13, cathepsin B, cathepsin C, cathepsin D, cathepsin G, Cathepsin H organize egg
White enzyme L, chymopapain, renin, chymotrypsin, a- clostripains, clostridiopetidase A, complement Clr, complement Cls,
Complement Factor D, Complement factor I, Cucumisin, dipeptides acyl-peptase IV, elastoser, leucocyte, elastoser, pancreas,
Interior protease A rg-C, interior protease A sp-N, interior protease Glu-C, interior protease Lys-C, enterokinase, factor Xa, fig
Protease, furin, granzyme A, granzyme B, hiv protease, IG enzymes, kallikrein tissue, leucine amino peptide
Enzyme (General), leucine aminopeptidase, cytosol, leucine aminopeptidase, microsome, matrix metalloproteinase, first sulphur
Histidine amino group peptase, Neutrase, papain, pepsin, plasmin, prolinase, pronase e,
Prostate-specific antigen, protease, the enzyme of the basophilic from streptomyces griseus, the protease from aspergillus come from vegetarian rattan
The protease of aspergillus (Aspergillus saitoi) comes from the protease of Aspergillus sojae (Aspergillus sojae), albumen
Enzyme (bacillus licheniformis (B.licheniformis)) (alkalinity), protease (bacillus licheniformis) (Alcalase), from more
Viscous bacillus (bacillus polymyxa) (Bacillus polymyxa)) protease, the protease from bacillus comes
From the protease (Esperase) of bacillus, the protease from head mold, protease S, proteasome, the egg from aspergillus oryzae
White enzyme, protease 3, protease A, Proteinase K, PROTEIN C, pyroglutamic acid aminopeptidase, renin, renin, chain
Kinases, subtilopeptidase A, thermolysin, fibrin ferment, tissue plasmin activation, trypsase, class tryptose
Enzyme, urokinase.
All enzymes all should be food-grade.
Enzyme hydrolysis is carried out under conditions of suitable for all enzymes used.Temperature and pH should be in suitable ranges so that
Hydrolysis is carried out to required degree.Therefore the length of incubation time will change, when condition is closer to optimum condition, incubation time
It is shorter.Usual 1 to 48 hour, preferably 10 to 24 hours.Stirring can accelerate hydrolytic process, such as rotating speed is 50 to 500rpm,
Usually it can improve hydrolysis.
For the enzyme of following some types, it is shown that there is enzyme unit/gram starting material of dosage.U (is indicated by LGG methods
Unit, LGG=L- leucyls-glycyl-glycine)/gram starting material, using 0.007 to 0.7U, for example, 0.01 to
0.1U。
Glutamine enzyme unit (GU)/gram starting material, using 0.00075 to 0.075GU, for example, 0.001 to
0.02GU.The amount of enzyme will change according to enzyme and its use condition.It as described herein, can be by testing different amount and effect
Fruit is readily determined necessary amounts.Pass through one or more proteolytic enzymes hydrolize albumen.
By the hydrolysate of one or more proteolytic enzymes hydrolize crude protein, it can be directly used as that fruits and vegetables are net or meal wash
Net ingredient.
It, can be by well known drying means such as by the hydrolysate of one or more proteolytic enzymes hydrolize crude protein
Spray drying, is made dry product, is used as that fruits and vegetables are net or the net ingredient of meal wash.
By the hydrolysate of one or more proteolytic enzymes hydrolize crude protein, purification can be carried out and remove crude salt point, fibre
Dimension, starch, sugar, fat etc. obtain purer protein peptides, are used as that fruits and vegetables are net or the net ingredient of meal wash.
The protein peptides generated after protein hydrolysis, the fruits and vegetables made of protein peptides are net, are removed to garden stuff pesticide residue,
Under the same terms, garden stuff pesticide residue can not only be effectively removed, and shows superior effect, than traditional by surface
The fruits and vegetables net effect that activating agent is prepared is more preferable.The fruits and vegetables are only without any side effects, can extend to soaking time by 5min
10min even half an hour, removal effect are 1.5 net~2 times or more of traditional fruits and vegetables by surfactant formulatory, effectively
Solves the problems, such as the net secondary pollution of traditional fruits and vegetables by surfactant formulatory.
Specific implementation mode
It elaborates below to the embodiment of the present invention, the present embodiment is carried out lower based on the technical solution of the present invention
Implement, gives detailed embodiment and specific operating process, but protection scope of the present invention is not limited to following implementation
Example.
Embodiment 1
After plant-derived albumen material disintegrating, add 4~12 times of water, preferably 8 times of water, under alkaline condition impregnate 12h~
48h, it is preferably for 24 hours, primary every 4h agitations;Then it is filtered, by filtrate tune PH4~5, protein precipitation comes out, refilters,
Obtain crude protein.
Crude protein is taken, protein content is surveyed with kjeldahl apparatus, sequentially adds 5% papain and bromelain
(its dosage is identical as crude protein quantity when using pawpaw and pineapple), 5~8h of constant temperature, preferably 6h, mixing speed at 55 DEG C
50rpm~500rpm, preferably 100rpm control PH7~8, and protein peptides, the ultrafiltration membrane point of the different cutoff values of protein peptides is made
From, obtain different molecular weight section protein peptides, as oligopeptide (molecular weight≤500D), polypeptide (molecular weight 500D~100000D),
Bigger molecule peptide (molecular weight >=100000D) selects polypeptide (molecular weight 500D~100000D), the protein peptides as needed to lead to
It crosses reduction vaporization or ultra-filtration filters obtains protein concentrate peptide.With pure water regulatory protein peptide content 30%, be made fruits and vegetables it is net or
Meal wash is net.
Comparative example
The preparation method is the same as that of Example 1, is added in manufactured protein peptides a kind of or several in soya-bean oil soap, phosphatide, sugar, starch, protein
Kind.The porcine collagen peptide of soya-bean oil soap, phosphatide, sugar, starch and protein powder and B3 are bought from the market, and sugar selects sucrose.
It is that the fruits and vegetables of the present invention remove the application method and effect experiment of pesticide residue only below:
Application method 1 is put into after being stirred evenly in a kind of edible fruit and vegetable cleaning agent 4g additions 2Kg water of the present invention
Fruit and vegetable impregnates about 5min, after slightly stirring, washes down that it can be served with clear water or cooks.
It is that a kind of edible fruit and vegetable cleaning agent of the present invention removes the effect experiment of pesticide residue below:
Arprocarb, cypermethrin technical material are dissolved in medical ethanol, fruit and vegetable is immersed in 20min in liquid, is then got rid of
Fall drop, dries in the shade 24 hours.It is divided into several groups, uses fruits and vegetables made of embodiment and comparative example net respectively, 4g is added in 2Kg water,
It is put into sample after stirring evenly, impregnates about 5min, after slightly stirring, is washed down with clear water.In the same way sample is washed with clear water.It is shown in Table
1 and table 2:
The removal rate of 1.30% polypeptide molecular weight 500D ~ 100000D, far above by conventional surfactant lauryl sodium sulfate
K12 is the removal rate for the fruits and vegetables net 70% that main component is prepared.Remove soya-bean oil soap, phosphatide, sugar, starch, protein in its composition
Five kinds of components it is any one or several after, the effect for removing pesticide residue maintains an equal level or more effective.
2, five kinds of soya-bean oil soap in object, phosphatide, sugar, starch, protein components are combined, all after removal, are only contained big
Legumin peptide, the effect for removing pesticide residue is more preferable, and reason is that phosphatide is readily adsorbed in fruit and vegetable surfaces, influences washing effect
Fruit.
3, the protein peptides of other types such as table 2, can also effectively remove pesticide residue.
4, upper table illustrates, the different protein peptides of molecular weight section can remove pesticide residue, and polypeptide removal effect is best, low
The protein peptides of poly- peptide and bigger molecule(Fen Liang≤100000D)Effect is weaker.
The fruits and vegetables of the present invention removal effect to other vegetable and fruit pesticide residues and imitate the removals of other pesticides only
Fruit, it is similar to upper table.With the present invention 30% soya-bean polypeptides molecular weight 500D ~ 100000D, to other vegetable and fruit pesticide residues
Removal effect and removal effect to other pesticides.
Table 2:
After fruit and vegetable surface is sprayed insecticide, sealing storage 2 hours is divided into two parts, sample one and sample two later.Take 4g
The fruits and vegetables of the present invention are net, add 2kg water, sample one is put into, and impregnate after ten minutes, cleaned with clear water.Respectively by sample one and sample
Product two crush, and are sealed.Detect the persticide residue of sample one and sample two.
It is above-mentioned that the experimental data are shown in the following table 3:
Meal wash of the invention net application method and effect experiment:
Application method:Each tableware adds the cleaning agent for dinnerware of the 2-3 drops present invention, and after sponging down, tap water is rinsed well i.e.
It can.
Effect experiment:After peanut oil and milk are mixed, is dipped and be coated onto on tableware with sponge, it is each to eat after drying in the shade 4 hours
The meal wash of tool plus the 2-3 drop present invention are net, and after sponging down, after tap water is rinsed well, all tablewares are all very clean,
Inner wall moisture film is uniform, does not hang droplet, very clean.The effect of Soyprotein peptide is added than commercially available meal good washing effect.
The fruits and vegetables that protein peptides make made from alkaline hydrolysis or acidolysis or hydrolysis crude protein are net and meal wash is net, and removal pesticide is residual
It stays and the effect of degreasing, it is similar to upper table.
In Bioexperiment, with the chlorine cyanogen chrysanthemum in three categories organic insecticidal pesticide pyrethroids class, first ammoniacum class, organic phosphates
Ester, arprocarb, acephatemet are tested, it was surprisingly found now that product of the present invention there is the removing toxic substances of extraordinary attenuation to make fish
With, hence it is evident that mitigate toxicity of the pesticide to fish, the time-to-live is obviously prolonged.It is more stable to illustrate that product of the present invention is bonded to pesticide
Firm conjugate, to make toxicity of pesticide reduce or disappear.And common meal wash is net, small point of protein, 2 ~ 3 amino acid
Sub- peptide does not have attenuating effects or unobvious.And and pesticide combination it is more secured, active force bigger, remove fruit and vegetable above it is residual
Stay the ability of pesticide naturally also just stronger.
It is the attenuation removing toxic substances experiment effect of fish below:
Test method:Prepare the aqueous solution containing pesticide, be divided into five parts, each 1000ml, be experimental group, net group of meal wash, protein group,
2 ~ 3 small-molecular peptides groups, control group.Blank group is that 1000ml water is free of pesticide.The production that 1ml the method for the present invention makes is added in experimental group
Product, meal wash is organized only is added the common net 1ml of meal wash, and the water soluble protein of 1ml30%, 2 ~ 3 small-molecular peptides groups are added in protein group
The small-molecular peptides of 1ml30%2 ~ 3 are added, and stir evenly.6 2cm of each random addition or so small grass carp.After observing 4 groups of different times
Death condition.
Claims (10)
1. a kind of edible fruits and vegetables are net and meal wash is net, which is characterized in that including protein peptides, the molecular weight of protein peptides is 500-
100000D。
2. fruits and vegetables according to claim 1 are net and meal wash is net, which is characterized in that the molecular weight of protein peptides is 1000-
10000D。
3. fruits and vegetables according to claim 1 are net and meal wash is net, which is characterized in that further include auxiliary agent, auxiliary agent is water and surface
Activating agent, soya-bean oil soap, sugar, starch, protein, citrate, EDETATE SODIUM salt, phosphate, Quadrafos water softener, anti-agglomerating agent
With one or more in preservative.
4. fruits and vegetables according to claim 1 are net and meal wash is net, which is characterized in that protein peptides are plant-derived albumen peptide, animal
Source protein peptide or microbial protein peptide.
The preparation method that 5. a kind of claim 1-4 any one of them fruits and vegetables are net and meal wash is net, which is characterized in that including following
Step:
(1)Extract the crude protein in protein material;
(2)Above-mentioned crude protein is digested with protease, alkaline hydrolysis, acidolysis, Ultra filtration membrane obtains molecular weight in 500-
Protein peptides between 100000D;
(3)By above-mentioned protein peptides by vacuum distillation, ultrafiltration membrance filter or spray drying, protein peptides concentrate or pulvis are obtained;
(4)Using above-mentioned protein peptides concentrate or pulvis as raw material heat inactivation, be directly prepared into liquid or solid, powdery fruits and vegetables it is net/
Meal wash is net;
(5)By step(2)In protein peptides purification after, after auxiliary agent is added, obtain liquid or solid, powdery fruits and vegetables it is net/meal wash
Only.
6. preparation method according to claim 5, which is characterized in that the step(2)In protease be selected from pawpaw egg
One or more in white enzyme, bromelain and ficin.
7. preparation method according to claim 5, which is characterized in that the step(2)In, protease is selected from peptase or protein
Enzyme.
8. the fruits and vegetables described in a kind of one of claim 1-4 are net and meal wash is only in the application to degrease.
9. fruits and vegetables described in a kind of one of claim 1-4 are net and the meal wash application in removing pesticide residue only.
10. fruits and vegetables described in a kind of one of claim 1-4 are net and the meal wash application in reducing toxicity of pesticide only.
Applications Claiming Priority (2)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
CN201710285990.1A CN107325900A (en) | 2017-04-22 | 2017-04-22 | Edible fruits and vegetables are net and meal wash only and its manufacture method |
CN2017102859901 | 2017-04-22 |
Publications (1)
Publication Number | Publication Date |
---|---|
CN108485842A true CN108485842A (en) | 2018-09-04 |
Family
ID=60192662
Family Applications (2)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
CN201710285990.1A Pending CN107325900A (en) | 2017-04-22 | 2017-04-22 | Edible fruits and vegetables are net and meal wash only and its manufacture method |
CN201810358619.8A Pending CN108485842A (en) | 2017-04-22 | 2018-04-20 | A kind of edible fruits and vegetables are net and meal wash is net and its preparation method and application |
Family Applications Before (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
CN201710285990.1A Pending CN107325900A (en) | 2017-04-22 | 2017-04-22 | Edible fruits and vegetables are net and meal wash only and its manufacture method |
Country Status (1)
Country | Link |
---|---|
CN (2) | CN107325900A (en) |
Cited By (2)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CN110477402A (en) * | 2019-08-09 | 2019-11-22 | 质每堂(武汉)健康科技有限公司 | Fish peptide, fish-bone peptide, sea cucumber peptide and ginseng peptide compound nutritional product and preparation method thereof |
CN111117790A (en) * | 2020-02-25 | 2020-05-08 | 沈阳垚采科技有限公司 | Preparation method of washing-free cleaning agent |
Families Citing this family (1)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CN110982639A (en) * | 2019-12-17 | 2020-04-10 | 河南绿澳化工科技有限公司 | Water-based cleaning agent for industrial oil stains and preparation method thereof |
Citations (4)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JPS51116806A (en) * | 1975-04-07 | 1976-10-14 | Dai Ichi Kogyo Seiyaku Co Ltd | Detergent compositions |
US6048835A (en) * | 1997-10-06 | 2000-04-11 | Colgate-Palmolive Co. | Animal and/or vegetable protein containing cleaning compositions |
CN104804905A (en) * | 2015-04-09 | 2015-07-29 | 广西大学 | Transparent gingko polypeptide handmade soap and manufacturing method thereof |
CN105586178A (en) * | 2016-01-25 | 2016-05-18 | 王家高 | Non-toxic detergent and preparation method thereof |
-
2017
- 2017-04-22 CN CN201710285990.1A patent/CN107325900A/en active Pending
-
2018
- 2018-04-20 CN CN201810358619.8A patent/CN108485842A/en active Pending
Patent Citations (4)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JPS51116806A (en) * | 1975-04-07 | 1976-10-14 | Dai Ichi Kogyo Seiyaku Co Ltd | Detergent compositions |
US6048835A (en) * | 1997-10-06 | 2000-04-11 | Colgate-Palmolive Co. | Animal and/or vegetable protein containing cleaning compositions |
CN104804905A (en) * | 2015-04-09 | 2015-07-29 | 广西大学 | Transparent gingko polypeptide handmade soap and manufacturing method thereof |
CN105586178A (en) * | 2016-01-25 | 2016-05-18 | 王家高 | Non-toxic detergent and preparation method thereof |
Cited By (2)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CN110477402A (en) * | 2019-08-09 | 2019-11-22 | 质每堂(武汉)健康科技有限公司 | Fish peptide, fish-bone peptide, sea cucumber peptide and ginseng peptide compound nutritional product and preparation method thereof |
CN111117790A (en) * | 2020-02-25 | 2020-05-08 | 沈阳垚采科技有限公司 | Preparation method of washing-free cleaning agent |
Also Published As
Publication number | Publication date |
---|---|
CN107325900A (en) | 2017-11-07 |
Similar Documents
Publication | Publication Date | Title |
---|---|---|
JP3466189B2 (en) | Rice bran stabilization method and rice bran product | |
CN100477923C (en) | Method for producing soymilk of removed anti-nutrition factor type | |
CN108485842A (en) | A kind of edible fruits and vegetables are net and meal wash is net and its preparation method and application | |
CN102845710A (en) | Method for preparing a proteinaceous vegetable flavor enhancer | |
KR101586768B1 (en) | Manufacturing method of feed ingredient using animal byproduct and feed ingredient manufactured thereby | |
SK18272000A3 (en) | Method for producing hydrolysate flavouring agent and hydrolysate flavouring agent | |
US20200345032A1 (en) | Enzymatic-Based Process for the Extraction of Value Added Products from Raw Biomasses | |
US7297512B2 (en) | Method for producing amino acid components by enzymatic hydrolysis of fish egg skin | |
CN109173946A (en) | A kind of sodium alginate chitosan microcapsules and preparation method thereof containing polylysine and Nisin | |
CN110353248A (en) | A kind of scallop powder processing method | |
CN105316127A (en) | Composite enzyme preparation used for removing tableware dirt and fruit and vegetable surface pesticide residue | |
CN104862364B (en) | Bee pollen form cole Oligopeptide Compositions and preparation method thereof | |
JP3888539B2 (en) | Novel biological material and method for producing the same | |
Matter et al. | Industrial Applications of Microbial Protease: A Review | |
Ibraheem et al. | Characterization of detergent-stable proteases isolated from Citrus sinensis fruit peel | |
Ibraheem et al. | Partial characterization of proteases from Citrus sinensis fruit peel | |
Singh et al. | 2 Microbial Proteases | |
KR100345618B1 (en) | Manufacturing method of corbicula extract | |
US20220264916A1 (en) | Process for increasing yield in production of plant based products | |
JPH03244366A (en) | Preparation of food and drink and food and drink prepared thereby | |
Singh et al. | Microbial Proteases: A Significant Tool for Industrial Applications | |
CN114717287A (en) | Process for extracting peptide from shellfish | |
RO135638A2 (en) | Protein hydrolysate with bioactive properties isolated from fish by-products and process for preparing the same | |
CN1162645A (en) | Method for producing compounded amino acids by hologenzymes process from beer yeast | |
JPH1046196A (en) | Detergent for removing blood stain |
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 | ||
RJ01 | Rejection of invention patent application after publication |
Application publication date: 20180904 |
|
RJ01 | Rejection of invention patent application after publication |