CA2395068A1 - Processes and organisms for the production of anti-freeze proteins - Google Patents
Processes and organisms for the production of anti-freeze proteins Download PDFInfo
- Publication number
- CA2395068A1 CA2395068A1 CA002395068A CA2395068A CA2395068A1 CA 2395068 A1 CA2395068 A1 CA 2395068A1 CA 002395068 A CA002395068 A CA 002395068A CA 2395068 A CA2395068 A CA 2395068A CA 2395068 A1 CA2395068 A1 CA 2395068A1
- Authority
- CA
- Canada
- Prior art keywords
- freeze
- sequence
- protein
- ice
- afp
- 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.)
- Abandoned
Links
- 108010053481 Antifreeze Proteins Proteins 0.000 title claims abstract description 114
- 238000000034 method Methods 0.000 title claims description 34
- 230000008569 process Effects 0.000 title claims description 27
- 238000004519 manufacturing process Methods 0.000 title abstract description 14
- 241000320425 Marinomonas protea Species 0.000 claims abstract description 32
- 241000894006 Bacteria Species 0.000 claims abstract description 28
- 235000009508 confectionery Nutrition 0.000 claims abstract description 9
- 235000015243 ice cream Nutrition 0.000 claims abstract description 9
- 241000589516 Pseudomonas Species 0.000 claims abstract description 5
- 235000013311 vegetables Nutrition 0.000 claims abstract description 4
- 108090000623 proteins and genes Proteins 0.000 claims description 56
- 102000004169 proteins and genes Human genes 0.000 claims description 49
- 238000012360 testing method Methods 0.000 claims description 30
- 230000001580 bacterial effect Effects 0.000 claims description 21
- 230000000694 effects Effects 0.000 claims description 20
- 230000002528 anti-freeze Effects 0.000 claims description 18
- 108020004465 16S ribosomal RNA Proteins 0.000 claims description 17
- 235000013305 food Nutrition 0.000 claims description 15
- 238000012258 culturing Methods 0.000 claims description 9
- 241001135624 Marinomonas Species 0.000 claims description 8
- 108091028043 Nucleic acid sequence Proteins 0.000 claims description 8
- 125000001429 N-terminal alpha-amino-acid group Chemical group 0.000 claims description 4
- 108010029485 Protein Isoforms Proteins 0.000 claims description 3
- 102000001708 Protein Isoforms Human genes 0.000 claims description 3
- 235000013373 food additive Nutrition 0.000 claims description 3
- 239000002778 food additive Substances 0.000 claims description 3
- 150000007523 nucleic acids Chemical group 0.000 claims description 3
- 125000003275 alpha amino acid group Chemical group 0.000 claims 3
- 235000013611 frozen food Nutrition 0.000 abstract description 6
- 108090000765 processed proteins & peptides Proteins 0.000 abstract description 2
- 102000004196 processed proteins & peptides Human genes 0.000 abstract 1
- 235000018102 proteins Nutrition 0.000 description 38
- 210000004027 cell Anatomy 0.000 description 31
- 239000013078 crystal Substances 0.000 description 29
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 28
- 235000002639 sodium chloride Nutrition 0.000 description 21
- 238000003556 assay Methods 0.000 description 17
- 239000000284 extract Substances 0.000 description 17
- 239000000203 mixture Substances 0.000 description 17
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 16
- 238000001953 recrystallisation Methods 0.000 description 15
- 239000006228 supernatant Substances 0.000 description 15
- 239000008188 pellet Substances 0.000 description 14
- 239000000523 sample Substances 0.000 description 14
- 238000005119 centrifugation Methods 0.000 description 12
- 238000002360 preparation method Methods 0.000 description 12
- 238000000751 protein extraction Methods 0.000 description 12
- 239000011780 sodium chloride Substances 0.000 description 12
- 229930006000 Sucrose Natural products 0.000 description 11
- 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 11
- 238000007710 freezing Methods 0.000 description 11
- 230000008014 freezing Effects 0.000 description 11
- 239000000463 material Substances 0.000 description 11
- 239000005720 sucrose Substances 0.000 description 11
- 239000007983 Tris buffer Substances 0.000 description 9
- 239000011324 bead Substances 0.000 description 9
- 230000005764 inhibitory process Effects 0.000 description 9
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 9
- 238000010438 heat treatment Methods 0.000 description 8
- 239000000243 solution Substances 0.000 description 8
- 241000196324 Embryophyta Species 0.000 description 7
- 101710123134 Ice-binding protein Proteins 0.000 description 7
- 239000011536 extraction buffer Substances 0.000 description 7
- 229940041514 candida albicans extract Drugs 0.000 description 6
- 238000010790 dilution Methods 0.000 description 6
- 239000012895 dilution Substances 0.000 description 6
- YBYRMVIVWMBXKQ-UHFFFAOYSA-N phenylmethanesulfonyl fluoride Chemical compound FS(=O)(=O)CC1=CC=CC=C1 YBYRMVIVWMBXKQ-UHFFFAOYSA-N 0.000 description 6
- 239000000047 product Substances 0.000 description 6
- 239000012138 yeast extract Substances 0.000 description 6
- 241000251468 Actinopterygii Species 0.000 description 5
- 102000035195 Peptidases Human genes 0.000 description 5
- 108091005804 Peptidases Proteins 0.000 description 5
- 239000001888 Peptone Substances 0.000 description 5
- 108010080698 Peptones Proteins 0.000 description 5
- 239000004365 Protease Substances 0.000 description 5
- 238000009835 boiling Methods 0.000 description 5
- 238000000605 extraction Methods 0.000 description 5
- 239000011521 glass Substances 0.000 description 5
- 238000011534 incubation Methods 0.000 description 5
- 235000019319 peptone Nutrition 0.000 description 5
- 239000013535 sea water Substances 0.000 description 5
- 239000003643 water by type Substances 0.000 description 5
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 4
- 238000007545 Vickers hardness test Methods 0.000 description 4
- 150000001413 amino acids Chemical group 0.000 description 4
- 238000004458 analytical method Methods 0.000 description 4
- 230000008901 benefit Effects 0.000 description 4
- 238000007373 indentation Methods 0.000 description 4
- 230000006698 induction Effects 0.000 description 4
- 239000007788 liquid Substances 0.000 description 4
- 238000005259 measurement Methods 0.000 description 4
- 239000013642 negative control Substances 0.000 description 4
- 108010091212 pepstatin Proteins 0.000 description 4
- FAXGPCHRFPCXOO-LXTPJMTPSA-N pepstatin A Chemical compound OC(=O)C[C@H](O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)C[C@H](O)[C@H](CC(C)C)NC(=O)[C@H](C(C)C)NC(=O)[C@H](C(C)C)NC(=O)CC(C)C FAXGPCHRFPCXOO-LXTPJMTPSA-N 0.000 description 4
- 241000894007 species Species 0.000 description 4
- 238000004659 sterilization and disinfection Methods 0.000 description 4
- 238000003860 storage Methods 0.000 description 4
- QTBSBXVTEAMEQO-UHFFFAOYSA-M Acetate Chemical compound CC([O-])=O QTBSBXVTEAMEQO-UHFFFAOYSA-M 0.000 description 3
- 229920001817 Agar Polymers 0.000 description 3
- 241000588724 Escherichia coli Species 0.000 description 3
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 3
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 3
- 244000068988 Glycine max Species 0.000 description 3
- 235000010469 Glycine max Nutrition 0.000 description 3
- 241000208474 Protea Species 0.000 description 3
- 239000008272 agar Substances 0.000 description 3
- 239000000872 buffer Substances 0.000 description 3
- 230000001413 cellular effect Effects 0.000 description 3
- UHZZMRAGKVHANO-UHFFFAOYSA-M chlormequat chloride Chemical compound [Cl-].C[N+](C)(C)CCCl UHZZMRAGKVHANO-UHFFFAOYSA-M 0.000 description 3
- 238000006073 displacement reaction Methods 0.000 description 3
- 239000002609 medium Substances 0.000 description 3
- 238000009928 pasteurization Methods 0.000 description 3
- 230000000717 retained effect Effects 0.000 description 3
- 238000002864 sequence alignment Methods 0.000 description 3
- 229920002379 silicone rubber Polymers 0.000 description 3
- 239000004945 silicone rubber Substances 0.000 description 3
- 238000000527 sonication Methods 0.000 description 3
- 239000001974 tryptic soy broth Substances 0.000 description 3
- 229940123779 Bacterial protease inhibitor Drugs 0.000 description 2
- 108020004414 DNA Proteins 0.000 description 2
- NHTMVDHEPJAVLT-UHFFFAOYSA-N Isooctane Chemical compound CC(C)CC(C)(C)C NHTMVDHEPJAVLT-UHFFFAOYSA-N 0.000 description 2
- 241001135625 Marinomonas communis Species 0.000 description 2
- 102000005741 Metalloproteases Human genes 0.000 description 2
- 108010006035 Metalloproteases Proteins 0.000 description 2
- 241000218902 Pseudomonas synxantha Species 0.000 description 2
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 2
- 102000012479 Serine Proteases Human genes 0.000 description 2
- 108010022999 Serine Proteases Proteins 0.000 description 2
- MGSKVZWGBWPBTF-UHFFFAOYSA-N aebsf Chemical compound NCCC1=CC=C(S(F)(=O)=O)C=C1 MGSKVZWGBWPBTF-UHFFFAOYSA-N 0.000 description 2
- 239000003513 alkali Substances 0.000 description 2
- 235000001014 amino acid Nutrition 0.000 description 2
- 239000006285 cell suspension Substances 0.000 description 2
- 238000001816 cooling Methods 0.000 description 2
- 235000013365 dairy product Nutrition 0.000 description 2
- 229940042399 direct acting antivirals protease inhibitors Drugs 0.000 description 2
- 238000002474 experimental method Methods 0.000 description 2
- 239000012467 final product Substances 0.000 description 2
- 239000000499 gel Substances 0.000 description 2
- 239000012135 ice-cold extraction buffer Substances 0.000 description 2
- 239000004615 ingredient Substances 0.000 description 2
- 238000002955 isolation Methods 0.000 description 2
- 239000008267 milk Substances 0.000 description 2
- 239000000137 peptide hydrolase inhibitor Substances 0.000 description 2
- 239000004033 plastic Substances 0.000 description 2
- 229920003023 plastic Polymers 0.000 description 2
- 238000001742 protein purification Methods 0.000 description 2
- 238000004366 reverse phase liquid chromatography Methods 0.000 description 2
- 150000003839 salts Chemical class 0.000 description 2
- 238000000926 separation method Methods 0.000 description 2
- 239000007787 solid Substances 0.000 description 2
- 238000010257 thawing Methods 0.000 description 2
- MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 description 1
- CGWBIHLHAGNJCX-UHFFFAOYSA-N 2-butylguanidine Chemical compound CCCCNC(N)=N CGWBIHLHAGNJCX-UHFFFAOYSA-N 0.000 description 1
- 102000004400 Aminopeptidases Human genes 0.000 description 1
- 108090000915 Aminopeptidases Proteins 0.000 description 1
- 102000035101 Aspartic proteases Human genes 0.000 description 1
- 108091005502 Aspartic proteases Proteins 0.000 description 1
- VGGGPCQERPFHOB-MCIONIFRSA-N Bestatin Chemical compound CC(C)C[C@H](C(O)=O)NC(=O)[C@@H](O)[C@H](N)CC1=CC=CC=C1 VGGGPCQERPFHOB-MCIONIFRSA-N 0.000 description 1
- VGGGPCQERPFHOB-UHFFFAOYSA-N Bestatin Natural products CC(C)CC(C(O)=O)NC(=O)C(O)C(N)CC1=CC=CC=C1 VGGGPCQERPFHOB-UHFFFAOYSA-N 0.000 description 1
- CURLTUGMZLYLDI-UHFFFAOYSA-N Carbon dioxide Chemical compound O=C=O CURLTUGMZLYLDI-UHFFFAOYSA-N 0.000 description 1
- 240000006766 Cornus mas Species 0.000 description 1
- 235000003363 Cornus mas Nutrition 0.000 description 1
- 102000005927 Cysteine Proteases Human genes 0.000 description 1
- 108010005843 Cysteine Proteases Proteins 0.000 description 1
- 102100035784 Decorin Human genes 0.000 description 1
- 108090000738 Decorin Proteins 0.000 description 1
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 1
- 239000004471 Glycine Substances 0.000 description 1
- 241000238631 Hexapoda Species 0.000 description 1
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 1
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 description 1
- 240000008415 Lactuca sativa Species 0.000 description 1
- 235000003228 Lactuca sativa Nutrition 0.000 description 1
- 239000006137 Luria-Bertani broth Substances 0.000 description 1
- 235000007688 Lycopersicon esculentum Nutrition 0.000 description 1
- 241000577079 Marinomonas sp. Species 0.000 description 1
- 238000007476 Maximum Likelihood Methods 0.000 description 1
- 229920002274 Nalgene Polymers 0.000 description 1
- 108020005187 Oligonucleotide Probes Proteins 0.000 description 1
- 239000002033 PVDF binder Substances 0.000 description 1
- 101710115215 Protease inhibitors Proteins 0.000 description 1
- 241000192142 Proteobacteria Species 0.000 description 1
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 1
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 1
- 229920005654 Sephadex Polymers 0.000 description 1
- 239000012507 Sephadex™ Substances 0.000 description 1
- BDMWLJLPPUCLNV-XGEHTFHBSA-N Ser-Thr-Val Chemical compound [H]N[C@@H](CO)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](C(C)C)C(O)=O BDMWLJLPPUCLNV-XGEHTFHBSA-N 0.000 description 1
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 1
- 240000003768 Solanum lycopersicum Species 0.000 description 1
- 235000021307 Triticum Nutrition 0.000 description 1
- 244000098338 Triticum aestivum Species 0.000 description 1
- OBTCMSPFOITUIJ-FSPLSTOPSA-N Val-Asp Chemical compound CC(C)[C@H](N)C(=O)N[C@H](C(O)=O)CC(O)=O OBTCMSPFOITUIJ-FSPLSTOPSA-N 0.000 description 1
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 description 1
- 240000008042 Zea mays Species 0.000 description 1
- 235000016383 Zea mays subsp huehuetenangensis Nutrition 0.000 description 1
- 235000002017 Zea mays subsp mays Nutrition 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 230000009471 action Effects 0.000 description 1
- 230000001464 adherent effect Effects 0.000 description 1
- 210000004102 animal cell Anatomy 0.000 description 1
- 239000007798 antifreeze agent Substances 0.000 description 1
- 238000013459 approach Methods 0.000 description 1
- 239000012062 aqueous buffer Substances 0.000 description 1
- 238000005452 bending Methods 0.000 description 1
- 235000011089 carbon dioxide Nutrition 0.000 description 1
- 230000005779 cell damage Effects 0.000 description 1
- 230000006037 cell lysis Effects 0.000 description 1
- 210000002421 cell wall Anatomy 0.000 description 1
- 235000013339 cereals Nutrition 0.000 description 1
- 239000002738 chelating agent Substances 0.000 description 1
- 231100000481 chemical toxicant Toxicity 0.000 description 1
- 238000010224 classification analysis Methods 0.000 description 1
- 239000011248 coating agent Substances 0.000 description 1
- 238000000576 coating method Methods 0.000 description 1
- 230000002860 competitive effect Effects 0.000 description 1
- 239000012141 concentrate Substances 0.000 description 1
- 239000000356 contaminant Substances 0.000 description 1
- 239000000287 crude extract Substances 0.000 description 1
- 235000011950 custard 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
- 230000006378 damage Effects 0.000 description 1
- 238000004925 denaturation Methods 0.000 description 1
- 230000036425 denaturation Effects 0.000 description 1
- 229940111685 dibasic potassium phosphate Drugs 0.000 description 1
- ZPWVASYFFYYZEW-UHFFFAOYSA-L dipotassium hydrogen phosphate Chemical compound [K+].[K+].OP([O-])([O-])=O ZPWVASYFFYYZEW-UHFFFAOYSA-L 0.000 description 1
- 238000005553 drilling Methods 0.000 description 1
- 241001233957 eudicotyledons Species 0.000 description 1
- 238000002270 exclusion chromatography Methods 0.000 description 1
- 239000013604 expression vector Substances 0.000 description 1
- 239000000706 filtrate Substances 0.000 description 1
- 238000009472 formulation Methods 0.000 description 1
- 238000002194 freeze distillation Methods 0.000 description 1
- 235000013572 fruit purees Nutrition 0.000 description 1
- 238000012812 general test Methods 0.000 description 1
- 239000008103 glucose Substances 0.000 description 1
- 239000010438 granite Substances 0.000 description 1
- 238000007542 hardness measurement Methods 0.000 description 1
- 238000004128 high performance liquid chromatography Methods 0.000 description 1
- -1 hypersaline) lakes Chemical compound 0.000 description 1
- 230000000415 inactivating effect Effects 0.000 description 1
- 239000003112 inhibitor Substances 0.000 description 1
- 230000002401 inhibitory effect Effects 0.000 description 1
- 230000002147 killing effect Effects 0.000 description 1
- 238000012332 laboratory investigation Methods 0.000 description 1
- 230000000670 limiting effect Effects 0.000 description 1
- 238000011068 loading method Methods 0.000 description 1
- 239000006166 lysate Substances 0.000 description 1
- 235000009973 maize Nutrition 0.000 description 1
- 238000002844 melting Methods 0.000 description 1
- 230000008018 melting Effects 0.000 description 1
- 239000012528 membrane Substances 0.000 description 1
- 238000001471 micro-filtration Methods 0.000 description 1
- 244000005700 microbiome Species 0.000 description 1
- 235000013336 milk Nutrition 0.000 description 1
- 210000004080 milk Anatomy 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 238000000465 moulding Methods 0.000 description 1
- 238000002887 multiple sequence alignment Methods 0.000 description 1
- ZIUHHBKFKCYYJD-UHFFFAOYSA-N n,n'-methylenebisacrylamide Chemical compound C=CC(=O)NCNC(=O)C=C ZIUHHBKFKCYYJD-UHFFFAOYSA-N 0.000 description 1
- 239000002773 nucleotide Substances 0.000 description 1
- 125000003729 nucleotide group Chemical group 0.000 description 1
- 235000015097 nutrients Nutrition 0.000 description 1
- 239000002751 oligonucleotide probe Substances 0.000 description 1
- 238000013021 overheating Methods 0.000 description 1
- 238000013081 phylogenetic analysis Methods 0.000 description 1
- 229920002981 polyvinylidene fluoride Polymers 0.000 description 1
- 238000004321 preservation Methods 0.000 description 1
- 238000003825 pressing Methods 0.000 description 1
- 238000012545 processing Methods 0.000 description 1
- 238000000746 purification Methods 0.000 description 1
- 238000000275 quality assurance Methods 0.000 description 1
- 108700022487 rRNA Genes Proteins 0.000 description 1
- 230000002829 reductive effect Effects 0.000 description 1
- 235000015067 sauces Nutrition 0.000 description 1
- 238000013341 scale-up Methods 0.000 description 1
- 239000007289 sea water agar Substances 0.000 description 1
- 235000011888 snacks Nutrition 0.000 description 1
- 235000014347 soups Nutrition 0.000 description 1
- 238000003892 spreading Methods 0.000 description 1
- 230000007480 spreading Effects 0.000 description 1
- 238000010561 standard procedure Methods 0.000 description 1
- 238000013517 stratification Methods 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 238000004781 supercooling Methods 0.000 description 1
- 230000008685 targeting Effects 0.000 description 1
- UEUXEKPTXMALOB-UHFFFAOYSA-J tetrasodium;2-[2-[bis(carboxylatomethyl)amino]ethyl-(carboxylatomethyl)amino]acetate Chemical compound [Na+].[Na+].[Na+].[Na+].[O-]C(=O)CN(CC([O-])=O)CCN(CC([O-])=O)CC([O-])=O UEUXEKPTXMALOB-UHFFFAOYSA-J 0.000 description 1
- 231100000331 toxic Toxicity 0.000 description 1
- 230000002588 toxic effect Effects 0.000 description 1
- 239000003440 toxic substance Substances 0.000 description 1
- 238000013518 transcription Methods 0.000 description 1
- 230000035897 transcription Effects 0.000 description 1
- 238000013519 translation Methods 0.000 description 1
- 108010050327 trypticase-soy broth Proteins 0.000 description 1
- 239000012137 tryptone Substances 0.000 description 1
- 229950009811 ubenimex Drugs 0.000 description 1
- 239000004474 valine Substances 0.000 description 1
- 239000002966 varnish Substances 0.000 description 1
- 239000013598 vector Substances 0.000 description 1
- 238000003260 vortexing Methods 0.000 description 1
- 235000013618 yogurt Nutrition 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/195—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/195—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
- C07K14/21—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria from Pseudomonadaceae (F)
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S530/00—Chemistry: natural resins or derivatives; peptides or proteins; lignins or reaction products thereof
- Y10S530/82—Proteins from microorganisms
- Y10S530/825—Bacteria
Landscapes
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Biophysics (AREA)
- General Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Life Sciences & Earth Sciences (AREA)
- Molecular Biology (AREA)
- Biochemistry (AREA)
- Gastroenterology & Hepatology (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Peptides Or Proteins (AREA)
- Enzymes And Modification Thereof (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Freezing, Cooling And Drying Of Foods (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| GBGB9929696.4A GB9929696D0 (en) | 1999-12-15 | 1999-12-15 | Processes and organisms for the production of anti-freeze proteins |
| GB9929696.4 | 1999-12-15 | ||
| PCT/EP2000/012396 WO2001044275A2 (en) | 1999-12-15 | 2000-12-05 | Processes and organisms for the production of anti-freeze proteins |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CA2395068A1 true CA2395068A1 (en) | 2001-06-21 |
Family
ID=10866404
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA002395068A Abandoned CA2395068A1 (en) | 1999-12-15 | 2000-12-05 | Processes and organisms for the production of anti-freeze proteins |
Country Status (12)
Families Citing this family (11)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| ES2248819T3 (es) * | 1995-07-05 | 2006-03-16 | Unilever N.V. | Peptidos anticongelantes de peces marinos como aditivos para productos alimentarios. |
| AU2002352231A1 (en) * | 2002-01-04 | 2003-07-15 | Unilever Plc | Antifreeze proteins in vegetables |
| US7012475B2 (en) | 2003-12-30 | 2006-03-14 | Raytheon Company | Method and apparatus for effecting high-frequency amplification or oscillation |
| EP1809120B1 (en) * | 2004-10-18 | 2013-06-26 | Unilever PLC | Low fat frozen confectionery product |
| EP1917865B1 (en) | 2006-10-20 | 2012-03-28 | Nestec S.A. | Ice-structuring peptides of lactic origin |
| CA2706550C (en) | 2007-11-21 | 2021-12-14 | Roskilde Universitet | Polypeptides comprising an ice-binding activity |
| CN101695346B (zh) * | 2009-09-25 | 2011-10-26 | 徐州工程学院 | 一种冷冻食品基料-地衣培养液的制备与应用方法 |
| US9394327B1 (en) * | 2013-03-15 | 2016-07-19 | The Trustees Of California State University | Nucleoside crystals, crystal nucleation and growth control with antifreeze proteins |
| CN103710288B (zh) * | 2013-12-26 | 2015-09-30 | 中国海洋大学 | 一种芳基硫酸酯酶的生产菌株及其应用 |
| AU2016273208B2 (en) * | 2015-06-02 | 2021-01-21 | Dsm Ip Assets B.V. | Use of ice structuring protein AFP19 expressed in filamentous fungal strains for preparing food |
| IT201900014121A1 (it) | 2019-08-06 | 2021-02-06 | Univ Degli Studi Di Camerino | Marinomonas ef1 e rhodococcus ef1 per la produzione di metaboliti secondari |
Family Cites Families (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| ES2248819T3 (es) | 1995-07-05 | 2006-03-16 | Unilever N.V. | Peptidos anticongelantes de peces marinos como aditivos para productos alimentarios. |
| KR20000029561A (ko) | 1996-07-26 | 2000-05-25 | 알 브이 테이트 (로드니 비버스 테이트);에이치 드로이. 씨. 지. 오닌크;이. 에디, 산드라 웨드워즈 (에스 제이 에드워즈) | 냉동제과제품 |
| BR9710519A (pt) * | 1996-07-26 | 1999-08-17 | Unilever Nv | Processo para produ-Æo de produto alimenticio congelado produto de confeitaria congelado e mistura para sorvete |
| GB9801408D0 (en) | 1998-01-22 | 1998-03-18 | Unilever Plc | Frozen food product |
-
1999
- 1999-12-15 GB GBGB9929696.4A patent/GB9929696D0/en not_active Ceased
-
2000
- 2000-12-05 AU AU26726/01A patent/AU774941B2/en not_active Ceased
- 2000-12-05 IL IL15023200A patent/IL150232A0/xx unknown
- 2000-12-05 WO PCT/EP2000/012396 patent/WO2001044275A2/en active Search and Examination
- 2000-12-05 MX MXPA02005954A patent/MXPA02005954A/es unknown
- 2000-12-05 CN CN00819030A patent/CN1434859A/zh active Pending
- 2000-12-05 CA CA002395068A patent/CA2395068A1/en not_active Abandoned
- 2000-12-05 BR BR0016475-5A patent/BR0016475A/pt not_active IP Right Cessation
- 2000-12-05 EP EP00989964A patent/EP1240188A2/en not_active Withdrawn
- 2000-12-14 IN IN1118MU2000 patent/IN189994B/en unknown
- 2000-12-15 US US09/737,297 patent/US6887984B2/en not_active Expired - Fee Related
-
2002
- 2002-06-14 ZA ZA200204816A patent/ZA200204816B/xx unknown
Also Published As
| Publication number | Publication date |
|---|---|
| WO2001044275A3 (en) | 2002-03-21 |
| US20020072108A1 (en) | 2002-06-13 |
| WO2001044275A2 (en) | 2001-06-21 |
| US6887984B2 (en) | 2005-05-03 |
| AU2672601A (en) | 2001-06-25 |
| EP1240188A2 (en) | 2002-09-18 |
| CN1434859A (zh) | 2003-08-06 |
| IN189994B (GUID-C5D7CC26-194C-43D0-91A1-9AE8C70A9BFF.html) | 2003-05-31 |
| AU774941B2 (en) | 2004-07-15 |
| MXPA02005954A (es) | 2002-10-23 |
| ZA200204816B (en) | 2004-01-28 |
| BR0016475A (pt) | 2002-11-12 |
| GB9929696D0 (en) | 2000-02-09 |
| IL150232A0 (en) | 2002-12-01 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| JP4175520B2 (ja) | 冷凍菓子製品 | |
| Yamashita et al. | Identification of an antifreeze lipoprotein from Moraxella sp. of Antarctic origin | |
| US9241511B2 (en) | Polypeptides comprising an ice-binding activity | |
| AU774941B2 (en) | Processes and organisms for the production of anti-freeze proteins | |
| EP1917865B1 (en) | Ice-structuring peptides of lactic origin | |
| EP1276763B1 (en) | Anti-freeze proteins, their production and use | |
| US6774210B1 (en) | Frozen food product | |
| KR20000016268A (ko) | 가문비나무 모충 부동화 단백질, 유전자 및 이들을 사용하는방법 | |
| EP0843010A1 (en) | Carrot anti-freeze polypeptides | |
| CA2296005C (en) | Tenebrio antifreeze proteins | |
| Kim et al. | Effect of Cold Shock on Protein Synthesis and on Cryotolerance of Cells Frozen for Long Periods inLactococcus lactis | |
| Prosekov et al. | The proteolytic activity research of the lactic acid microorganisms of different taxonomic groups | |
| JP2017043551A (ja) | 生体材料保護用ペプチド | |
| JP2004161761A (ja) | 微生物由来の不凍タンパク質 | |
| JP3993521B2 (ja) | 氷結晶成長阻害活性を有する担子菌の培養液 | |
| EP1535999B1 (en) | Milk-coagulating enzyme originating in bacterium and process for producing cheese using the same | |
| Muryoi et al. | Properties of a novel extracellular cell-free ice nuclei from ice-nucleating Pseudomonas antarctica IN-74 | |
| Yin et al. | Properties of extracellular ice-nucleating substances from Pseudomonas fluorescens MACK-4 and its effect on the freezing of some food materials | |
| Vanderveer | The function, characterization of expression, localization and activity of a divergent ice nucleating protein from Pseudomonas borealis | |
| CN115975005B (zh) | 一种犁齿鲷鱼鳞抗冻肽及其筛选方法和应用 | |
| CN120365359A (zh) | 冰晶重结晶抑制肽及其应用 | |
| Pattnaik et al. | Bacterial ice nucleation: Prospects and perspectives | |
| Miller | The Raw Data of AFM for Bacteria Investigation | |
| Hassan | Effect of Heat Shock Treatment on Heat Resistance of Microorganisms and Biogenic Amine Synthesis | |
| TH53987A (th) | กระบวนการและสิ่งมีชีวิต (organism) สำหรับการผลิตโปรตีนต้านการแข็งตัวเป็นน้ำแข็ง |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| EEER | Examination request | ||
| FZDE | Discontinued |