CZ698A3 - Exprese peptidu mořských ryb chránící proti zmrznutí v organizmu vhodném pro potravinářský průmysl a aplikace těchto peptidů v potravinářských produktech - Google Patents
Exprese peptidu mořských ryb chránící proti zmrznutí v organizmu vhodném pro potravinářský průmysl a aplikace těchto peptidů v potravinářských produktech Download PDFInfo
- Publication number
- CZ698A3 CZ698A3 CZ986A CZ698A CZ698A3 CZ 698 A3 CZ698 A3 CZ 698A3 CZ 986 A CZ986 A CZ 986A CZ 698 A CZ698 A CZ 698A CZ 698 A3 CZ698 A3 CZ 698A3
- Authority
- CZ
- Czechia
- Prior art keywords
- afp
- acid sequence
- hplc
- protein
- polypeptide
- Prior art date
Links
- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 109
- 102000004196 processed proteins & peptides Human genes 0.000 title claims abstract description 91
- 230000014509 gene expression Effects 0.000 title claims description 33
- 241000251468 Actinopterygii Species 0.000 title description 15
- 229920001184 polypeptide Polymers 0.000 claims abstract description 75
- 240000004808 Saccharomyces cerevisiae Species 0.000 claims abstract description 72
- 238000000034 method Methods 0.000 claims abstract description 42
- 238000004128 high performance liquid chromatography Methods 0.000 claims abstract description 19
- 108090000623 proteins and genes Proteins 0.000 claims description 88
- 235000014680 Saccharomyces cerevisiae Nutrition 0.000 claims description 68
- 150000001413 amino acids Chemical class 0.000 claims description 68
- 102000004169 proteins and genes Human genes 0.000 claims description 59
- 150000007523 nucleic acids Chemical group 0.000 claims description 39
- 235000013305 food Nutrition 0.000 claims description 37
- 108091028043 Nucleic acid sequence Proteins 0.000 claims description 36
- 108020004414 DNA Proteins 0.000 claims description 35
- 238000004519 manufacturing process Methods 0.000 claims description 27
- 108010076504 Protein Sorting Signals Proteins 0.000 claims description 26
- 230000028327 secretion Effects 0.000 claims description 17
- 102100039555 Galectin-7 Human genes 0.000 claims description 9
- 108091081024 Start codon Proteins 0.000 claims description 8
- 239000012620 biological material Substances 0.000 claims description 8
- 230000003248 secreting effect Effects 0.000 claims description 6
- 108010038049 Mating Factor Proteins 0.000 claims description 5
- 230000001939 inductive effect Effects 0.000 claims description 5
- SBKVPJHMSUXZTA-MEJXFZFPSA-N (2S)-2-[[(2S)-2-[[(2S)-1-[(2S)-5-amino-2-[[2-[[(2S)-1-[(2S)-6-amino-2-[[(2S)-2-[[(2S)-5-amino-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-amino-3-(1H-indol-3-yl)propanoyl]amino]-3-(1H-imidazol-4-yl)propanoyl]amino]-3-(1H-indol-3-yl)propanoyl]amino]-4-methylpentanoyl]amino]-5-oxopentanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]pyrrolidine-2-carbonyl]amino]acetyl]amino]-5-oxopentanoyl]pyrrolidine-2-carbonyl]amino]-4-methylsulfanylbutanoyl]amino]-3-(4-hydroxyphenyl)propanoic acid Chemical compound C([C@@H](C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCCN)C(=O)N1CCC[C@H]1C(=O)NCC(=O)N[C@@H](CCC(N)=O)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(O)=O)NC(=O)[C@@H](N)CC=1C2=CC=CC=C2NC=1)C1=CNC=N1 SBKVPJHMSUXZTA-MEJXFZFPSA-N 0.000 claims description 3
- 101000887163 Gallus gallus Gallinacin-4 Proteins 0.000 claims description 3
- 101000887166 Gallus gallus Gallinacin-7 Proteins 0.000 claims description 3
- 108020005038 Terminator Codon Proteins 0.000 claims description 3
- 210000001557 animal structure Anatomy 0.000 claims description 3
- 235000015243 ice cream Nutrition 0.000 claims description 3
- 244000005700 microbiome Species 0.000 claims description 3
- 230000011664 signaling Effects 0.000 claims description 3
- 102100031181 Glyceraldehyde-3-phosphate dehydrogenase Human genes 0.000 claims description 2
- 238000012258 culturing Methods 0.000 claims description 2
- 235000012465 frozen bakery product Nutrition 0.000 claims description 2
- 235000012470 frozen dough Nutrition 0.000 claims description 2
- 108020004445 glyceraldehyde-3-phosphate dehydrogenase Proteins 0.000 claims description 2
- 230000006698 induction Effects 0.000 claims description 2
- 125000003275 alpha amino acid group Chemical group 0.000 claims 5
- 101710089626 Protein yippee Proteins 0.000 claims 1
- 108010053481 Antifreeze Proteins Proteins 0.000 description 173
- 230000000694 effects Effects 0.000 description 54
- 235000018102 proteins Nutrition 0.000 description 49
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 49
- 239000000047 product Substances 0.000 description 44
- 239000013612 plasmid Substances 0.000 description 43
- 108010029485 Protein Isoforms Proteins 0.000 description 25
- 102000001708 Protein Isoforms Human genes 0.000 description 25
- 235000001014 amino acid Nutrition 0.000 description 25
- 229940024606 amino acid Drugs 0.000 description 25
- 238000001953 recrystallisation Methods 0.000 description 24
- 239000012634 fragment Substances 0.000 description 18
- 238000007710 freezing Methods 0.000 description 18
- 239000002904 solvent Substances 0.000 description 18
- 101710123134 Ice-binding protein Proteins 0.000 description 17
- 101710082837 Ice-structuring protein Proteins 0.000 description 17
- 101710107540 Type-2 ice-structuring protein Proteins 0.000 description 17
- 239000013078 crystal Substances 0.000 description 17
- 230000008014 freezing Effects 0.000 description 17
- 239000000203 mixture Substances 0.000 description 16
- 210000004369 blood Anatomy 0.000 description 14
- 239000008280 blood Substances 0.000 description 14
- 239000000243 solution Substances 0.000 description 14
- 108010051210 beta-Fructofuranosidase Proteins 0.000 description 13
- 239000001573 invertase Substances 0.000 description 13
- 235000011073 invertase Nutrition 0.000 description 13
- 241000588724 Escherichia coli Species 0.000 description 12
- 241000269907 Pleuronectes platessa Species 0.000 description 12
- 230000004927 fusion Effects 0.000 description 12
- 108091034117 Oligonucleotide Proteins 0.000 description 11
- 238000010276 construction Methods 0.000 description 11
- 230000002401 inhibitory effect Effects 0.000 description 11
- 239000000178 monomer Substances 0.000 description 11
- 108020004705 Codon Proteins 0.000 description 10
- 241000276457 Gadidae Species 0.000 description 10
- 239000013604 expression vector Substances 0.000 description 10
- 239000002609 medium Substances 0.000 description 10
- 230000008569 process Effects 0.000 description 10
- 238000004007 reversed phase HPLC Methods 0.000 description 10
- 239000013598 vector Substances 0.000 description 10
- 238000002360 preparation method Methods 0.000 description 9
- 238000003556 assay Methods 0.000 description 8
- 238000000855 fermentation Methods 0.000 description 8
- 230000004151 fermentation Effects 0.000 description 8
- 239000006228 supernatant Substances 0.000 description 8
- 241000196324 Embryophyta Species 0.000 description 7
- 108700005078 Synthetic Genes Proteins 0.000 description 7
- JLCPHMBAVCMARE-UHFFFAOYSA-N [3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methyl [5-(6-aminopurin-9-yl)-2-(hydroxymethyl)oxolan-3-yl] hydrogen phosphate Polymers Cc1cn(C2CC(OP(O)(=O)OCC3OC(CC3OP(O)(=O)OCC3OC(CC3O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c3nc(N)[nH]c4=O)C(COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3CO)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cc(C)c(=O)[nH]c3=O)n3cc(C)c(=O)[nH]c3=O)n3ccc(N)nc3=O)n3cc(C)c(=O)[nH]c3=O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)O2)c(=O)[nH]c1=O JLCPHMBAVCMARE-UHFFFAOYSA-N 0.000 description 7
- 238000010586 diagram Methods 0.000 description 7
- 238000012986 modification Methods 0.000 description 7
- 230000004048 modification Effects 0.000 description 7
- 230000009466 transformation Effects 0.000 description 7
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 6
- 101000608772 Homo sapiens Galectin-7 Proteins 0.000 description 6
- SEQKRHFRPICQDD-UHFFFAOYSA-N N-tris(hydroxymethyl)methylglycine Chemical compound OCC(CO)(CO)[NH2+]CC([O-])=O SEQKRHFRPICQDD-UHFFFAOYSA-N 0.000 description 6
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 6
- DTQVDTLACAAQTR-UHFFFAOYSA-N Trifluoroacetic acid Chemical compound OC(=O)C(F)(F)F DTQVDTLACAAQTR-UHFFFAOYSA-N 0.000 description 6
- 239000000654 additive Substances 0.000 description 6
- 230000000996 additive effect Effects 0.000 description 6
- 230000027455 binding Effects 0.000 description 6
- 239000000872 buffer Substances 0.000 description 6
- 210000004027 cell Anatomy 0.000 description 6
- 238000004925 denaturation Methods 0.000 description 6
- 230000036425 denaturation Effects 0.000 description 6
- 230000029087 digestion Effects 0.000 description 6
- 239000000499 gel Substances 0.000 description 6
- 239000000463 material Substances 0.000 description 6
- 108020004707 nucleic acids Proteins 0.000 description 6
- 102000039446 nucleic acids Human genes 0.000 description 6
- 238000012360 testing method Methods 0.000 description 6
- 241000894006 Bacteria Species 0.000 description 5
- 239000007983 Tris buffer Substances 0.000 description 5
- 102000004142 Trypsin Human genes 0.000 description 5
- 108090000631 Trypsin Proteins 0.000 description 5
- 238000004458 analytical method Methods 0.000 description 5
- 230000001747 exhibiting effect Effects 0.000 description 5
- 230000006872 improvement Effects 0.000 description 5
- 238000011534 incubation Methods 0.000 description 5
- 239000012588 trypsin Substances 0.000 description 5
- 102000004190 Enzymes Human genes 0.000 description 4
- 108090000790 Enzymes Proteins 0.000 description 4
- 241001465754 Metazoa Species 0.000 description 4
- 239000012901 Milli-Q water Substances 0.000 description 4
- 229940041514 candida albicans extract Drugs 0.000 description 4
- 238000010790 dilution Methods 0.000 description 4
- 239000012895 dilution Substances 0.000 description 4
- 239000012153 distilled water Substances 0.000 description 4
- 229940088598 enzyme Drugs 0.000 description 4
- 238000010353 genetic engineering Methods 0.000 description 4
- 239000008103 glucose Substances 0.000 description 4
- 230000002209 hydrophobic effect Effects 0.000 description 4
- 230000005764 inhibitory process Effects 0.000 description 4
- 238000012545 processing Methods 0.000 description 4
- 238000006467 substitution reaction Methods 0.000 description 4
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 4
- 239000012138 yeast extract Substances 0.000 description 4
- WEVYAHXRMPXWCK-UHFFFAOYSA-N Acetonitrile Chemical compound CC#N WEVYAHXRMPXWCK-UHFFFAOYSA-N 0.000 description 3
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 3
- 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 3
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 3
- HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 description 3
- AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical compound C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 0.000 description 3
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 3
- 125000001429 N-terminal alpha-amino-acid group Chemical group 0.000 description 3
- 239000001888 Peptone Substances 0.000 description 3
- 108010080698 Peptones Proteins 0.000 description 3
- 241000269913 Pseudopleuronectes americanus Species 0.000 description 3
- UZMAPBJVXOGOFT-UHFFFAOYSA-N Syringetin Natural products COC1=C(O)C(OC)=CC(C2=C(C(=O)C3=C(O)C=C(O)C=C3O2)O)=C1 UZMAPBJVXOGOFT-UHFFFAOYSA-N 0.000 description 3
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 3
- 239000004473 Threonine Substances 0.000 description 3
- 239000007997 Tricine buffer Substances 0.000 description 3
- 241000269785 Zoarces americanus Species 0.000 description 3
- 235000004279 alanine Nutrition 0.000 description 3
- 238000013459 approach Methods 0.000 description 3
- 235000015173 baked goods and baking mixes Nutrition 0.000 description 3
- 238000006243 chemical reaction Methods 0.000 description 3
- 239000002299 complementary DNA Substances 0.000 description 3
- 238000001816 cooling Methods 0.000 description 3
- KCFYHBSOLOXZIF-UHFFFAOYSA-N dihydrochrysin Natural products COC1=C(O)C(OC)=CC(C2OC3=CC(O)=CC(O)=C3C(=O)C2)=C1 KCFYHBSOLOXZIF-UHFFFAOYSA-N 0.000 description 3
- 238000004520 electroporation Methods 0.000 description 3
- 238000010828 elution Methods 0.000 description 3
- 229930182830 galactose Natural products 0.000 description 3
- 238000011065 in-situ storage Methods 0.000 description 3
- 239000007788 liquid Substances 0.000 description 3
- 239000002773 nucleotide Substances 0.000 description 3
- 125000003729 nucleotide group Chemical group 0.000 description 3
- 235000019319 peptone Nutrition 0.000 description 3
- 108091008146 restriction endonucleases Proteins 0.000 description 3
- 239000000523 sample Substances 0.000 description 3
- 239000011780 sodium chloride Substances 0.000 description 3
- 238000010561 standard procedure Methods 0.000 description 3
- 238000012546 transfer Methods 0.000 description 3
- 238000001262 western blot Methods 0.000 description 3
- 229920001817 Agar Polymers 0.000 description 2
- 241000473391 Archosargus rhomboidalis Species 0.000 description 2
- 108091026890 Coding region Proteins 0.000 description 2
- 108700010070 Codon Usage Proteins 0.000 description 2
- 108020004635 Complementary DNA Proteins 0.000 description 2
- 102000012410 DNA Ligases Human genes 0.000 description 2
- 108010061982 DNA Ligases Proteins 0.000 description 2
- 108010010803 Gelatin Proteins 0.000 description 2
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 2
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 2
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 2
- 108010014251 Muramidase Proteins 0.000 description 2
- 102000016943 Muramidase Human genes 0.000 description 2
- 108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 description 2
- 108091005804 Peptidases Proteins 0.000 description 2
- ISWSIDIOOBJBQZ-UHFFFAOYSA-N Phenol Chemical compound OC1=CC=CC=C1 ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 description 2
- 108010021757 Polynucleotide 5'-Hydroxyl-Kinase Proteins 0.000 description 2
- 102000008422 Polynucleotide 5'-hydroxyl-kinase Human genes 0.000 description 2
- 239000004365 Protease Substances 0.000 description 2
- 229920005654 Sephadex Polymers 0.000 description 2
- 239000012507 Sephadex™ Substances 0.000 description 2
- 229930006000 Sucrose Natural products 0.000 description 2
- 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 2
- 239000007984 Tris EDTA buffer Substances 0.000 description 2
- 239000008272 agar Substances 0.000 description 2
- 239000011543 agarose gel Substances 0.000 description 2
- 238000003277 amino acid sequence analysis Methods 0.000 description 2
- 239000002518 antifoaming agent Substances 0.000 description 2
- 230000001580 bacterial effect Effects 0.000 description 2
- 230000015572 biosynthetic process Effects 0.000 description 2
- 238000010804 cDNA synthesis Methods 0.000 description 2
- 238000005341 cation exchange Methods 0.000 description 2
- 238000005277 cation exchange chromatography Methods 0.000 description 2
- 239000007795 chemical reaction product Substances 0.000 description 2
- 238000003776 cleavage reaction Methods 0.000 description 2
- 239000012228 culture supernatant Substances 0.000 description 2
- 235000013365 dairy product Nutrition 0.000 description 2
- 238000001962 electrophoresis Methods 0.000 description 2
- 238000005194 fractionation Methods 0.000 description 2
- 239000008273 gelatin Substances 0.000 description 2
- 229920000159 gelatin Polymers 0.000 description 2
- 235000019322 gelatine Nutrition 0.000 description 2
- 235000011852 gelatine desserts Nutrition 0.000 description 2
- 229960002885 histidine Drugs 0.000 description 2
- 238000002169 hydrotherapy Methods 0.000 description 2
- 239000004615 ingredient Substances 0.000 description 2
- 238000002955 isolation Methods 0.000 description 2
- JVTAAEKCZFNVCJ-UHFFFAOYSA-N lactic acid Chemical compound CC(O)C(O)=O JVTAAEKCZFNVCJ-UHFFFAOYSA-N 0.000 description 2
- 238000011031 large-scale manufacturing process Methods 0.000 description 2
- 239000004325 lysozyme Substances 0.000 description 2
- 229960000274 lysozyme Drugs 0.000 description 2
- 235000010335 lysozyme Nutrition 0.000 description 2
- SKEFKEOTNIPLCQ-LWIQTABASA-N mating hormone Chemical compound C([C@@H](C(=O)NC(CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCCN)C(=O)N1[C@@H](CCC1)C(=O)NCC(=O)N[C@@H](CCC(N)=O)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCS(C)=O)C(=O)NC(CC=1C=CC(O)=CC=1)C(O)=O)NC(=O)[C@@H](N)CC=1C2=CC=CC=C2NC=1)C1=CN=CN1 SKEFKEOTNIPLCQ-LWIQTABASA-N 0.000 description 2
- 239000012528 membrane Substances 0.000 description 2
- 230000000051 modifying effect Effects 0.000 description 2
- 230000035772 mutation Effects 0.000 description 2
- 125000001500 prolyl group Chemical group [H]N1C([H])(C(=O)[*])C([H])([H])C([H])([H])C1([H])[H] 0.000 description 2
- 238000011160 research Methods 0.000 description 2
- 238000012552 review Methods 0.000 description 2
- 238000012163 sequencing technique Methods 0.000 description 2
- 230000037432 silent mutation Effects 0.000 description 2
- 235000020183 skimmed milk Nutrition 0.000 description 2
- 238000003756 stirring Methods 0.000 description 2
- 239000000126 substance Substances 0.000 description 2
- 239000005720 sucrose Substances 0.000 description 2
- 239000013595 supernatant sample Substances 0.000 description 2
- 210000001519 tissue Anatomy 0.000 description 2
- 229910021654 trace metal Inorganic materials 0.000 description 2
- 239000011782 vitamin Substances 0.000 description 2
- 235000013343 vitamin Nutrition 0.000 description 2
- 229940088594 vitamin Drugs 0.000 description 2
- 229930003231 vitamin Natural products 0.000 description 2
- 150000003722 vitamin derivatives Chemical class 0.000 description 2
- 210000005253 yeast cell Anatomy 0.000 description 2
- QZNNVYOVQUKYSC-JEDNCBNOSA-N (2s)-2-amino-3-(1h-imidazol-5-yl)propanoic acid;hydron;chloride Chemical compound Cl.OC(=O)[C@@H](N)CC1=CN=CN1 QZNNVYOVQUKYSC-JEDNCBNOSA-N 0.000 description 1
- QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 1
- 238000005084 2D-nuclear magnetic resonance Methods 0.000 description 1
- QRXMUCSWCMTJGU-UHFFFAOYSA-N 5-bromo-4-chloro-3-indolyl phosphate Chemical compound C1=C(Br)C(Cl)=C2C(OP(O)(=O)O)=CNC2=C1 QRXMUCSWCMTJGU-UHFFFAOYSA-N 0.000 description 1
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 1
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 1
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 1
- 101100283604 Caenorhabditis elegans pigk-1 gene Proteins 0.000 description 1
- 241000283707 Capra Species 0.000 description 1
- 241000557626 Corvus corax Species 0.000 description 1
- 238000001712 DNA sequencing Methods 0.000 description 1
- 241000723298 Dicentrarchus labrax Species 0.000 description 1
- 101710121765 Endo-1,4-beta-xylanase Proteins 0.000 description 1
- 241001524679 Escherichia virus M13 Species 0.000 description 1
- 241000233866 Fungi Species 0.000 description 1
- 102000003886 Glycoproteins Human genes 0.000 description 1
- 108090000288 Glycoproteins Proteins 0.000 description 1
- 241000276572 Hemitripterus americanus Species 0.000 description 1
- 101150017040 I gene Proteins 0.000 description 1
- 101150098499 III gene Proteins 0.000 description 1
- ONIBWKKTOPOVIA-BYPYZUCNSA-N L-Proline Chemical compound OC(=O)[C@@H]1CCCN1 ONIBWKKTOPOVIA-BYPYZUCNSA-N 0.000 description 1
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 1
- 241000186660 Lactobacillus Species 0.000 description 1
- 241001625930 Luria Species 0.000 description 1
- 241001529936 Murinae Species 0.000 description 1
- MQUQNUAYKLCRME-INIZCTEOSA-N N-tosyl-L-phenylalanyl chloromethyl ketone Chemical compound C1=CC(C)=CC=C1S(=O)(=O)N[C@H](C(=O)CCl)CC1=CC=CC=C1 MQUQNUAYKLCRME-INIZCTEOSA-N 0.000 description 1
- 102000035195 Peptidases Human genes 0.000 description 1
- BELBBZDIHDAJOR-UHFFFAOYSA-N Phenolsulfonephthalein Chemical compound C1=CC(O)=CC=C1C1(C=2C=CC(O)=CC=2)C2=CC=CC=C2S(=O)(=O)O1 BELBBZDIHDAJOR-UHFFFAOYSA-N 0.000 description 1
- 229920001213 Polysorbate 20 Polymers 0.000 description 1
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 1
- 101000961042 Pseudopleuronectes americanus Ice-structuring protein A Proteins 0.000 description 1
- 102000015097 RNA Splicing Factors Human genes 0.000 description 1
- 108010039259 RNA Splicing Factors Proteins 0.000 description 1
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 1
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 1
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 1
- PHMHDRYYFAYWEG-UHFFFAOYSA-N Rhapontigenin Natural products C1=C(O)C(OC)=CC=C1C=CC1=CC(O)=CC(O)=C1 PHMHDRYYFAYWEG-UHFFFAOYSA-N 0.000 description 1
- 108020001027 Ribosomal DNA Proteins 0.000 description 1
- 101150014136 SUC2 gene Proteins 0.000 description 1
- 241000235070 Saccharomyces Species 0.000 description 1
- 244000253911 Saccharomyces fragilis Species 0.000 description 1
- 235000018368 Saccharomyces fragilis Nutrition 0.000 description 1
- 241000191967 Staphylococcus aureus Species 0.000 description 1
- 241000194017 Streptococcus Species 0.000 description 1
- 108010031299 Type III Antifreeze Proteins Proteins 0.000 description 1
- IXKSXJFAGXLQOQ-XISFHERQSA-N WHWLQLKPGQPMY Chemical compound C([C@@H](C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N1CCC[C@H]1C(=O)NCC(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(O)=O)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(O)=O)NC(=O)[C@@H](N)CC=1C2=CC=CC=C2NC=1)C1=CNC=N1 IXKSXJFAGXLQOQ-XISFHERQSA-N 0.000 description 1
- 240000008042 Zea mays Species 0.000 description 1
- 241000230482 Zoarces Species 0.000 description 1
- YVNQAIFQFWTPLQ-UHFFFAOYSA-O [4-[[4-(4-ethoxyanilino)phenyl]-[4-[ethyl-[(3-sulfophenyl)methyl]amino]-2-methylphenyl]methylidene]-3-methylcyclohexa-2,5-dien-1-ylidene]-ethyl-[(3-sulfophenyl)methyl]azanium Chemical compound C1=CC(OCC)=CC=C1NC1=CC=C(C(=C2C(=CC(C=C2)=[N+](CC)CC=2C=C(C=CC=2)S(O)(=O)=O)C)C=2C(=CC(=CC=2)N(CC)CC=2C=C(C=CC=2)S(O)(=O)=O)C)C=C1 YVNQAIFQFWTPLQ-UHFFFAOYSA-O 0.000 description 1
- 238000002835 absorbance Methods 0.000 description 1
- 238000005273 aeration Methods 0.000 description 1
- 101150055123 afp gene Proteins 0.000 description 1
- AVKUERGKIZMTKX-NJBDSQKTSA-N ampicillin Chemical compound C1([C@@H](N)C(=O)N[C@H]2[C@H]3SC([C@@H](N3C2=O)C(O)=O)(C)C)=CC=CC=C1 AVKUERGKIZMTKX-NJBDSQKTSA-N 0.000 description 1
- 229960000723 ampicillin Drugs 0.000 description 1
- 230000003321 amplification Effects 0.000 description 1
- 230000002528 anti-freeze Effects 0.000 description 1
- 235000009582 asparagine Nutrition 0.000 description 1
- 229960001230 asparagine Drugs 0.000 description 1
- 125000000613 asparagine group Chemical group N[C@@H](CC(N)=O)C(=O)* 0.000 description 1
- 238000013475 authorization Methods 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
- 230000008901 benefit Effects 0.000 description 1
- 230000005540 biological transmission Effects 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 235000013351 cheese Nutrition 0.000 description 1
- 239000003153 chemical reaction reagent Substances 0.000 description 1
- 238000004140 cleaning Methods 0.000 description 1
- 239000003653 coastal water Substances 0.000 description 1
- 150000001875 compounds Chemical class 0.000 description 1
- NKLPQNGYXWVELD-UHFFFAOYSA-M coomassie brilliant blue Chemical compound [Na+].C1=CC(OCC)=CC=C1NC1=CC=C(C(=C2C=CC(C=C2)=[N+](CC)CC=2C=C(C=CC=2)S([O-])(=O)=O)C=2C=CC(=CC=2)N(CC)CC=2C=C(C=CC=2)S([O-])(=O)=O)C=C1 NKLPQNGYXWVELD-UHFFFAOYSA-M 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
- 230000009089 cytolysis Effects 0.000 description 1
- 239000000539 dimer Substances 0.000 description 1
- 150000002016 disaccharides Chemical class 0.000 description 1
- 238000001035 drying Methods 0.000 description 1
- 235000013399 edible fruits Nutrition 0.000 description 1
- 239000003797 essential amino acid Substances 0.000 description 1
- 235000020776 essential amino acid Nutrition 0.000 description 1
- 238000001704 evaporation Methods 0.000 description 1
- 230000008020 evaporation Effects 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 239000000284 extract Substances 0.000 description 1
- 239000012526 feed medium Substances 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- 230000004992 fission Effects 0.000 description 1
- 235000013611 frozen food Nutrition 0.000 description 1
- 108020001507 fusion proteins Proteins 0.000 description 1
- 102000037865 fusion proteins Human genes 0.000 description 1
- 238000001502 gel electrophoresis Methods 0.000 description 1
- 230000002068 genetic effect Effects 0.000 description 1
- 235000013922 glutamic acid Nutrition 0.000 description 1
- 239000004220 glutamic acid Substances 0.000 description 1
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 1
- PCHJSUWPFVWCPO-UHFFFAOYSA-N gold Chemical compound [Au] PCHJSUWPFVWCPO-UHFFFAOYSA-N 0.000 description 1
- 239000010931 gold Substances 0.000 description 1
- 229910052737 gold Inorganic materials 0.000 description 1
- 230000009036 growth inhibition Effects 0.000 description 1
- 239000001963 growth medium Substances 0.000 description 1
- 230000009931 harmful effect Effects 0.000 description 1
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 1
- 238000000338 in vitro Methods 0.000 description 1
- 238000012994 industrial processing Methods 0.000 description 1
- 239000003112 inhibitor Substances 0.000 description 1
- 238000011081 inoculation Methods 0.000 description 1
- 239000002054 inoculum Substances 0.000 description 1
- 238000003780 insertion Methods 0.000 description 1
- 230000037431 insertion Effects 0.000 description 1
- 230000010354 integration Effects 0.000 description 1
- 230000007154 intracellular accumulation Effects 0.000 description 1
- 239000004310 lactic acid Substances 0.000 description 1
- 235000014655 lactic acid Nutrition 0.000 description 1
- 229940039696 lactobacillus Drugs 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 108020004999 messenger RNA Proteins 0.000 description 1
- 238000002156 mixing Methods 0.000 description 1
- 238000010369 molecular cloning Methods 0.000 description 1
- 238000012544 monitoring process Methods 0.000 description 1
- 238000002703 mutagenesis Methods 0.000 description 1
- 231100000350 mutagenesis Toxicity 0.000 description 1
- 238000003199 nucleic acid amplification method Methods 0.000 description 1
- 238000004806 packaging method and process Methods 0.000 description 1
- 229960003531 phenolsulfonphthalein Drugs 0.000 description 1
- 229920002401 polyacrylamide Polymers 0.000 description 1
- 238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 1
- 239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 1
- 235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 1
- 239000000843 powder Substances 0.000 description 1
- 230000003161 proteinsynthetic effect Effects 0.000 description 1
- 238000000746 purification Methods 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- -1 restored growth Chemical compound 0.000 description 1
- 239000012723 sample buffer Substances 0.000 description 1
- 239000012898 sample dilution Substances 0.000 description 1
- 230000007017 scission Effects 0.000 description 1
- 239000006152 selective media Substances 0.000 description 1
- 210000002966 serum Anatomy 0.000 description 1
- 238000003860 storage Methods 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 239000003053 toxin Substances 0.000 description 1
- 231100000765 toxin Toxicity 0.000 description 1
- 108700012359 toxins Proteins 0.000 description 1
- 238000013518 transcription Methods 0.000 description 1
- 230000035897 transcription Effects 0.000 description 1
- 238000011426 transformation method Methods 0.000 description 1
- 230000009261 transgenic effect Effects 0.000 description 1
- 238000013519 translation Methods 0.000 description 1
- 210000002700 urine Anatomy 0.000 description 1
- 235000013311 vegetables Nutrition 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
- 235000013618 yogurt Nutrition 0.000 description 1
- DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 description 1
Classifications
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23G—COCOA; COCOA PRODUCTS, e.g. CHOCOLATE; SUBSTITUTES FOR COCOA OR COCOA PRODUCTS; CONFECTIONERY; CHEWING GUM; ICE-CREAM; PREPARATION THEREOF
- A23G9/00—Frozen sweets, e.g. ice confectionery, ice-cream; Mixtures therefor
- A23G9/32—Frozen sweets, e.g. ice confectionery, ice-cream; Mixtures therefor characterised by the composition containing organic or inorganic compounds
- A23G9/38—Frozen sweets, e.g. ice confectionery, ice-cream; Mixtures therefor characterised by the composition containing organic or inorganic compounds containing peptides or proteins
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- C07K14/461—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from fish
Landscapes
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Zoology (AREA)
- Organic Chemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Biochemistry (AREA)
- Polymers & Plastics (AREA)
- General Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- Gastroenterology & Hepatology (AREA)
- Toxicology (AREA)
- Inorganic Chemistry (AREA)
- Engineering & Computer Science (AREA)
- Food Science & Technology (AREA)
- Biophysics (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Coloring Foods And Improving Nutritive Qualities (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Freezing, Cooling And Drying Of Foods (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
- Meat, Egg Or Seafood Products (AREA)
- General Preparation And Processing Of Foods (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| EP95201842 | 1995-07-05 | ||
| EP95202732 | 1995-10-10 |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CZ698A3 true CZ698A3 (cs) | 1998-05-13 |
Family
ID=26139472
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CZ986A CZ698A3 (cs) | 1995-07-05 | 1996-07-01 | Exprese peptidu mořských ryb chránící proti zmrznutí v organizmu vhodném pro potravinářský průmysl a aplikace těchto peptidů v potravinářských produktech |
Country Status (17)
| Country | Link |
|---|---|
| US (2) | US6914043B1 (ja) |
| EP (2) | EP0836646B1 (ja) |
| JP (2) | JP3926843B2 (ja) |
| CN (1) | CN1149285C (ja) |
| AT (1) | ATE305509T1 (ja) |
| AU (1) | AU723039B2 (ja) |
| BR (1) | BR9609325A (ja) |
| CA (1) | CA2226101C (ja) |
| CZ (1) | CZ698A3 (ja) |
| DE (1) | DE69635225T2 (ja) |
| DK (1) | DK0836646T3 (ja) |
| ES (2) | ES2248819T3 (ja) |
| HU (1) | HUP9802321A3 (ja) |
| PL (1) | PL324437A1 (ja) |
| SK (1) | SK179497A3 (ja) |
| TR (1) | TR199701752T1 (ja) |
| WO (1) | WO1997002343A1 (ja) |
Families Citing this family (66)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| GB2315661B (en) | 1996-07-26 | 2000-05-03 | Unilever Plc | Frozen food product |
| EP0959689B1 (en) * | 1996-07-26 | 2007-01-17 | Unilever N.V. | Frozen confectionery products |
| GB2315662A (en) * | 1996-07-26 | 1998-02-11 | Unilever Plc | Antifreeze peptides in frozen foods |
| AU7207998A (en) * | 1997-03-14 | 1998-10-12 | Unilever Plc | Frozen food product |
| BR9808009B1 (pt) * | 1997-03-14 | 2009-01-13 | processo para a produção de um produto alimentìcio congelado, e, produto congelado. | |
| WO1998041109A1 (en) * | 1997-03-14 | 1998-09-24 | Unilever N.V. | Frozen food product containing anti-freeze peptides |
| GB9801410D0 (en) | 1998-01-22 | 1998-03-18 | Unilever Plc | Frozen food product |
| DE60034970T2 (de) * | 1999-03-10 | 2008-02-21 | Unilever N.V. | Gefrierschutzprotein enthaltendes Speiseeis |
| GB9929696D0 (en) | 1999-12-15 | 2000-02-09 | Unilever Plc | Processes and organisms for the production of anti-freeze proteins |
| HU228689B1 (hu) | 2000-12-13 | 2013-05-28 | Unilever Nv | Eljárás heterológ fehérjék gombasejtekkel történõ elõállítására |
| JP4228068B2 (ja) * | 2001-11-21 | 2009-02-25 | 独立行政法人産業技術総合研究所 | 魚類由来の不凍タンパク質 |
| BRPI0315943B1 (pt) * | 2002-12-20 | 2019-07-09 | Unilever N.V. | Método para a produção de proteína anticongelante |
| US7098589B2 (en) | 2003-04-15 | 2006-08-29 | Luminus Devices, Inc. | Light emitting devices with high light collimation |
| JP2004344033A (ja) * | 2003-05-21 | 2004-12-09 | National Institute Of Advanced Industrial & Technology | 魚類が有する不凍タンパク質 |
| WO2005058058A1 (en) * | 2003-12-10 | 2005-06-30 | Unilever Plc | Frozen confectionery product comprising ice structuring proteins |
| EP1541034A1 (en) * | 2003-12-10 | 2005-06-15 | Unilever Plc | Frozen confectionery product |
| EP1926399B2 (en) * | 2005-09-23 | 2014-03-12 | Unilever PLC | Process for producing a frozen aerated composition |
| EP1926398B1 (en) * | 2005-09-23 | 2011-01-05 | Unilever PLC | Aerated products with reduced creaming |
| ES2317579T3 (es) * | 2005-09-23 | 2009-04-16 | Unilever N.V. | Productos aireados de ph bajo. |
| DE602005006829D1 (de) * | 2005-12-21 | 2008-06-26 | Unilever Nv | Gefrorene belüftete Süssspeisen |
| ZA200802445B (en) * | 2006-01-31 | 2009-09-30 | Unilever Plc | Aerated compositions comprising hydrophobin |
| AU2007225747A1 (en) | 2006-03-13 | 2007-09-20 | Nippon Suisan Kaisha, Ltd. | Protein having ice nucleation activity |
| ATE550948T1 (de) * | 2006-10-20 | 2012-04-15 | Nestec Sa | Eisstrukturierende peptiden aus milch |
| BRPI0705417B1 (pt) * | 2006-12-20 | 2016-08-16 | Unilever Nv | produto alimentício aerado e processos para a produção de um produto alimentício aerado |
| BRPI0808588A2 (pt) * | 2007-03-26 | 2014-08-12 | Unilever Nv | "produtos alimentícios aerados e processo para produzir um produto alimentício aerado" |
| MX2009010365A (es) * | 2007-03-26 | 2009-10-16 | Unilever Nv | Productos alimenticios aereados que estan tibios contenidos solidos solubles y/o insolubles y metodos para producirlos. |
| BRPI0816506A2 (pt) * | 2007-10-18 | 2014-10-14 | Unilever Nv | "método para produzir um agente espumante" |
| KR101700711B1 (ko) | 2007-11-21 | 2017-01-31 | 로스킬드 유니베르시테트 | 얼음-결합 활성을 포함하는 폴리펩티드 |
| US20100112139A1 (en) * | 2008-03-28 | 2010-05-06 | Conopco, Inc., D/B/A Unilever | Foaming Agents Comprising Hydrophobin |
| AU2009304092B2 (en) * | 2008-10-16 | 2013-09-05 | Unilever Plc | Hydrophobin solution containing antifoam |
| CN102245628B (zh) * | 2008-12-16 | 2014-05-28 | 荷兰联合利华有限公司 | 从溶液中提取疏水蛋白的方法 |
| CN102317299A (zh) * | 2009-02-13 | 2012-01-11 | 株式会社钟化 | 含冰结晶化抑制物质的植物提取物及其制造方法 |
| US8357420B2 (en) * | 2009-05-29 | 2013-01-22 | Conopco, Inc. | Oil-in-water emulsion |
| US8394444B2 (en) * | 2009-05-29 | 2013-03-12 | Conopco, Inc. | Oil-in-water emulsion |
| CA2704702C (en) * | 2009-06-02 | 2018-06-12 | Unilever Plc | Aerated baked products |
| ES2536232T3 (es) | 2009-12-21 | 2015-05-21 | Unilever N.V. | Producto de confitería helado en partículas |
| ES2392150T3 (es) | 2010-01-22 | 2012-12-05 | Unilever N.V. | Procedimiento de fabricación de partículas congeladas |
| JP2011229504A (ja) * | 2010-04-30 | 2011-11-17 | National Institute Of Advanced Industrial Science & Technology | 生産性および不凍活性を向上させた改変型不凍タンパク質とその製造方法 |
| WO2012026596A1 (ja) * | 2010-08-26 | 2012-03-01 | 株式会社ニチレイフーズ | 熱ヒステリシス活性増加方法、熱ヒステリシス活性の熱失活の低減方法、及び熱ヒステリシス活性増加用組成物 |
| EP2731452B1 (en) | 2011-07-11 | 2015-08-12 | Unilever PLC | Frozen confection with gel coating |
| US9513045B2 (en) | 2012-05-03 | 2016-12-06 | Whirlpool Corporation | Heater-less ice maker assembly with a twistable tray |
| US10426159B1 (en) | 2012-05-24 | 2019-10-01 | The Trustees Of California State University | Highly efficient enhancers for antifreeze protein activity |
| US8925335B2 (en) * | 2012-11-16 | 2015-01-06 | Whirlpool Corporation | Ice cube release and rapid freeze using fluid exchange apparatus and methods |
| US9410723B2 (en) | 2012-12-13 | 2016-08-09 | Whirlpool Corporation | Ice maker with rocking cold plate |
| US9518773B2 (en) | 2012-12-13 | 2016-12-13 | Whirlpool Corporation | Clear ice maker |
| US9500398B2 (en) | 2012-12-13 | 2016-11-22 | Whirlpool Corporation | Twist harvest ice geometry |
| US9518770B2 (en) | 2012-12-13 | 2016-12-13 | Whirlpool Corporation | Multi-sheet spherical ice making |
| US9470448B2 (en) | 2012-12-13 | 2016-10-18 | Whirlpool Corporation | Apparatus to warm plastic side of mold |
| US9557087B2 (en) | 2012-12-13 | 2017-01-31 | Whirlpool Corporation | Clear ice making apparatus having an oscillation frequency and angle |
| US9310115B2 (en) | 2012-12-13 | 2016-04-12 | Whirlpool Corporation | Layering of low thermal conductive material on metal tray |
| US9476629B2 (en) | 2012-12-13 | 2016-10-25 | Whirlpool Corporation | Clear ice maker and method for forming clear ice |
| US9759472B2 (en) | 2012-12-13 | 2017-09-12 | Whirlpool Corporation | Clear ice maker with warm air flow |
| WO2014202089A2 (en) | 2013-06-18 | 2014-12-24 | Roskilde Universitet | Variants of anti-freeze polypeptides |
| ES2706742T3 (es) | 2013-12-02 | 2019-04-01 | Dsm Ip Assets Bv | Proteína estructuradora del hielo |
| US9624418B2 (en) | 2014-04-15 | 2017-04-18 | Baker Hughes Incorporated | Antifreeze proteins for use in downhole fluids |
| WO2016065269A2 (en) | 2014-10-23 | 2016-04-28 | Whirlpool Corporation | Method and apparatus for increasing rate of ice production in an automatic ice maker |
| 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 |
| US11110176B2 (en) | 2016-11-25 | 2021-09-07 | The Board Of Trustees Of The California State University | Composition and method for the protection of proteins, cell components and cells during temperature stress |
| CN108118077A (zh) * | 2016-11-30 | 2018-06-05 | 中南大学 | 一种酶法水解三文鱼胶原制备抗氧化肽与抗冻肽的工艺 |
| CN107746870A (zh) * | 2017-10-26 | 2018-03-02 | 浙江海洋大学 | 一种金枪鱼鱼骨明胶抗冻肽及其制备方法 |
| US10739053B2 (en) | 2017-11-13 | 2020-08-11 | Whirlpool Corporation | Ice-making appliance |
| JP2021517143A (ja) * | 2018-03-14 | 2021-07-15 | バ、ヨン | Ｐｅｇ化不凍タンパク質およびそれを作製する方法およびそれを使用する方法 |
| US10907874B2 (en) | 2018-10-22 | 2021-02-02 | Whirlpool Corporation | Ice maker downspout |
| CN111808903B (zh) * | 2020-07-06 | 2023-03-31 | 浙江工业大学 | 一种安全高效蛋白抗冻剂及其制备方法和应用 |
| WO2024076237A1 (en) | 2022-10-06 | 2024-04-11 | Wageningen Universiteit | Improved ice-binding proteins based on twist constrained helices |
| CN116064709B (zh) * | 2022-11-02 | 2024-05-24 | 山东省海洋科学研究院(青岛国家海洋科学研究中心) | 一种天然抗冻肽及其制备方法和应用 |
Family Cites Families (12)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5118792A (en) * | 1989-05-10 | 1992-06-02 | Dna Plant Technology Corporation | Ice crystal growth suppression polypeptides and method of making |
| US5849537A (en) * | 1989-09-19 | 1998-12-15 | Miller Brewing Company | Method of expressing antifreeze proteins in yeast |
| ATE165208T1 (de) * | 1990-01-17 | 1998-05-15 | Univ California | Zusammensetzung zur verbesserung der lebenserhaltung biologischer materialien |
| WO1991012718A1 (en) * | 1990-03-01 | 1991-09-05 | Agouron Pharmaceuticals, Inc. | Enhanced cryopreservation with thermal hysteresis peptide |
| WO1994003617A1 (en) * | 1992-07-29 | 1994-02-17 | Unilever N.V. | Process for producing anti-freeze peptides |
| US5676985A (en) * | 1994-10-12 | 1997-10-14 | Hsc Research And Development Limited Partnership | Antifreeze polypeptide-expressing microorganisms useful in fermentation and freezing of foods |
| EP0959689B1 (en) | 1996-07-26 | 2007-01-17 | Unilever N.V. | Frozen confectionery products |
| GB2315661B (en) | 1996-07-26 | 2000-05-03 | Unilever Plc | Frozen food product |
| WO1998004699A1 (en) | 1996-07-26 | 1998-02-05 | Unilever N.V. | Frozen food product containing heat stable antifreeze protein |
| DE60034970T2 (de) | 1999-03-10 | 2008-02-21 | Unilever N.V. | Gefrierschutzprotein enthaltendes Speiseeis |
| GB9929696D0 (en) * | 1999-12-15 | 2000-02-09 | Unilever Plc | Processes and organisms for the production of anti-freeze proteins |
| EP2751630B1 (en) | 2011-08-29 | 2019-03-13 | Crown Equipment Corporation | Vehicular navigation control interface |
-
1996
- 1996-07-01 PL PL96324437A patent/PL324437A1/xx unknown
- 1996-07-01 ES ES96924879T patent/ES2248819T3/es not_active Expired - Lifetime
- 1996-07-01 ES ES05075582T patent/ES2420105T3/es not_active Expired - Lifetime
- 1996-07-01 TR TR97/01752T patent/TR199701752T1/xx unknown
- 1996-07-01 DK DK96924879T patent/DK0836646T3/da active
- 1996-07-01 JP JP50482897A patent/JP3926843B2/ja not_active Expired - Fee Related
- 1996-07-01 CN CNB961965010A patent/CN1149285C/zh not_active Expired - Fee Related
- 1996-07-01 DE DE69635225T patent/DE69635225T2/de not_active Expired - Lifetime
- 1996-07-01 SK SK1794-97A patent/SK179497A3/sk unknown
- 1996-07-01 EP EP96924879A patent/EP0836646B1/en not_active Expired - Lifetime
- 1996-07-01 CZ CZ986A patent/CZ698A3/cs unknown
- 1996-07-01 CA CA002226101A patent/CA2226101C/en not_active Expired - Fee Related
- 1996-07-01 HU HU9802321A patent/HUP9802321A3/hu unknown
- 1996-07-01 BR BR9609325A patent/BR9609325A/pt not_active Application Discontinuation
- 1996-07-01 AT AT96924879T patent/ATE305509T1/de not_active IP Right Cessation
- 1996-07-01 WO PCT/EP1996/002936 patent/WO1997002343A1/en active IP Right Grant
- 1996-07-01 EP EP05075582.6A patent/EP1614753B1/en not_active Expired - Lifetime
- 1996-07-01 AU AU65190/96A patent/AU723039B2/en not_active Ceased
- 1996-07-02 US US08/673,876 patent/US6914043B1/en not_active Expired - Fee Related
-
2003
- 2003-08-08 JP JP2003290511A patent/JP3921461B2/ja not_active Expired - Fee Related
-
2004
- 2004-09-03 US US10/934,009 patent/US7297516B2/en not_active Expired - Fee Related
Also Published As
| Publication number | Publication date |
|---|---|
| SK179497A3 (en) | 1998-07-08 |
| AU6519096A (en) | 1997-02-05 |
| HUP9802321A2 (hu) | 1999-02-01 |
| EP1614753A3 (en) | 2006-07-19 |
| ATE305509T1 (de) | 2005-10-15 |
| JP2004043484A (ja) | 2004-02-12 |
| CN1193999A (zh) | 1998-09-23 |
| DE69635225T2 (de) | 2006-03-16 |
| JPH11508451A (ja) | 1999-07-27 |
| WO1997002343A1 (en) | 1997-01-23 |
| AU723039B2 (en) | 2000-08-17 |
| EP1614753A2 (en) | 2006-01-11 |
| DE69635225D1 (de) | 2006-02-09 |
| CA2226101A1 (en) | 1997-01-23 |
| BR9609325A (pt) | 1999-05-25 |
| PL324437A1 (en) | 1998-05-25 |
| ES2248819T3 (es) | 2006-03-16 |
| JP3921461B2 (ja) | 2007-05-30 |
| HUP9802321A3 (en) | 2000-10-30 |
| EP0836646B1 (en) | 2005-09-28 |
| CN1149285C (zh) | 2004-05-12 |
| DK0836646T3 (da) | 2005-12-19 |
| EP0836646A1 (en) | 1998-04-22 |
| US6914043B1 (en) | 2005-07-05 |
| MX9800016A (es) | 1998-07-31 |
| JP3926843B2 (ja) | 2007-06-06 |
| US7297516B2 (en) | 2007-11-20 |
| CA2226101C (en) | 2009-06-23 |
| TR199701752T1 (xx) | 1998-05-21 |
| ES2420105T3 (es) | 2013-08-22 |
| EP1614753B1 (en) | 2013-05-29 |
| US20050205833A1 (en) | 2005-09-22 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| US7297516B2 (en) | Recombinant peptide | |
| CN101918437B (zh) | 具有冰结合活性的多肽 | |
| Yuan et al. | Site-directed mutagenesis of the hinge region of nisinZ and properties of nisinZ mutants | |
| Tsujimoto et al. | Cryoprotective effect of the serine-rich repetitive sequence in silk protein sericin | |
| Ásgeirsdóttir et al. | Expression of Two Closely Linked Hydrophobin Genes ofCoprinus cinereusIs Monokaryon-Specific and Down-Regulated by theoid-1Mutation | |
| Akca et al. | Genes and derived amino acid sequences of S-layer proteins from mesophilic, thermophilic, and extremely thermophilic methanococci | |
| EP0941332B1 (en) | Carrot antifreeze polypeptides | |
| US6855518B2 (en) | Anti-listeria bacteriocin | |
| US5470971A (en) | Stress-induced proteins, genes coding therefor, transformed cells of organisms, methods and applications | |
| JP2002507889A (ja) | Ｔｅｎｅｂｒｉｏ不凍タンパク質 | |
| JP2002504316A (ja) | 凍結された食品 | |
| Simons et al. | Overproduction of bovine β-casein in Escherichia coli and engineering of its main chymosin cleavage site | |
| US5939317A (en) | Use of a Sec-dependent secretion system for secreting proteins that are usually secreted by a Sec-independent secretion system, bacteria containing it and their use | |
| Inokoshi et al. | Molecular cloning of actinohivin, a novel anti-HIV protein from an actinomycete, and its expression in Escherichia coli | |
| MXPA98000016A (en) | Expression of ocean fish antifreeze peptide in a food grade organism and its application in alimentic products | |
| Sumisa et al. | Molecular properties of mycelial aggregate-specific lectin of Pleurotus cornucopiae | |
| EP0633316A1 (en) | Lys-aminopeptidase PepN from lactobacillus delbruckii ssp. Lactis, nucleic acids coding for it, and its use in fermentation processes | |
| WO1994004682A1 (en) | Bacteriocin | |
| JP4592387B2 (ja) | イヌリン分解酵素及びその遺伝子 | |
| WO1994016082A1 (en) | X-prolyl-dipeptidyl-aminopeptidase from lactobacillus delbrückii ssp. lactis, nucleic acids coding for the same and its use in fermented foodstuff preparation processes | |
| EP0323489A1 (en) | Preparation of novel protein sweeteners | |
| CN101665533A (zh) | 蛋白质活性多肽及其编码基因、表达载体、表达菌及应用 | |
| ZA200209666B (en) | Anti-listeria bacteriocin. |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| PD00 | Pending as of 2000-06-30 in czech republic |