ES2595500T3 - Nuevas proteasas que pueden hidrolizar péptidos y proteínas de gluten a un pH ácido, procedentes del actinomiceto Actinoallomurus - Google Patents
Nuevas proteasas que pueden hidrolizar péptidos y proteínas de gluten a un pH ácido, procedentes del actinomiceto Actinoallomurus Download PDFInfo
- Publication number
- ES2595500T3 ES2595500T3 ES12781098.4T ES12781098T ES2595500T3 ES 2595500 T3 ES2595500 T3 ES 2595500T3 ES 12781098 T ES12781098 T ES 12781098T ES 2595500 T3 ES2595500 T3 ES 2595500T3
- Authority
- ES
- Spain
- Prior art keywords
- endopep
- seq
- actinoallomurus
- proteins
- sequence
- 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.)
- Active
Links
- 108090000623 proteins and genes Proteins 0.000 title description 30
- 102000004169 proteins and genes Human genes 0.000 title description 23
- 102000035195 Peptidases Human genes 0.000 title description 22
- 108091005804 Peptidases Proteins 0.000 title description 22
- 235000018102 proteins Nutrition 0.000 title description 21
- 108090000765 processed proteins & peptides Proteins 0.000 title description 19
- 239000004365 Protease Substances 0.000 title description 18
- 102000004196 processed proteins & peptides Human genes 0.000 title description 14
- 241000605656 Actinoallomurus Species 0.000 title description 13
- 108010068370 Glutens Proteins 0.000 title description 8
- 235000021312 gluten Nutrition 0.000 title description 8
- 230000002378 acidificating effect Effects 0.000 title 1
- 241001446247 uncultured actinomycete Species 0.000 title 1
- 102000005593 Endopeptidases Human genes 0.000 abstract description 23
- 108010059378 Endopeptidases Proteins 0.000 abstract description 23
- 239000000203 mixture Substances 0.000 abstract description 15
- 230000002255 enzymatic effect Effects 0.000 abstract description 9
- 239000012634 fragment Substances 0.000 abstract description 7
- FWMNVWWHGCHHJJ-SKKKGAJSSA-N 4-amino-1-[(2r)-6-amino-2-[[(2r)-2-[[(2r)-2-[[(2r)-2-amino-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]piperidine-4-carboxylic acid Chemical compound C([C@H](C(=O)N[C@H](CC(C)C)C(=O)N[C@H](CCCCN)C(=O)N1CCC(N)(CC1)C(O)=O)NC(=O)[C@H](N)CC=1C=CC=CC=1)C1=CC=CC=C1 FWMNVWWHGCHHJJ-SKKKGAJSSA-N 0.000 abstract 1
- 210000004027 cell Anatomy 0.000 description 18
- 150000007523 nucleic acids Chemical group 0.000 description 17
- 102000004190 Enzymes Human genes 0.000 description 15
- 108090000790 Enzymes Proteins 0.000 description 15
- 229940088598 enzyme Drugs 0.000 description 15
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 12
- 229940066758 endopeptidases Drugs 0.000 description 12
- 108020004707 nucleic acids Proteins 0.000 description 12
- 102000039446 nucleic acids Human genes 0.000 description 12
- 150000001413 amino acids Chemical group 0.000 description 11
- 101710118538 Protease Proteins 0.000 description 10
- 239000002609 medium Substances 0.000 description 10
- 238000000034 method Methods 0.000 description 10
- 235000019419 proteases Nutrition 0.000 description 10
- 108010061711 Gliadin Proteins 0.000 description 9
- 102000057297 Pepsin A Human genes 0.000 description 8
- 108090000284 Pepsin A Proteins 0.000 description 8
- 238000011534 incubation Methods 0.000 description 8
- 238000004519 manufacturing process Methods 0.000 description 8
- 229940111202 pepsin Drugs 0.000 description 8
- 230000029087 digestion Effects 0.000 description 7
- 229920001184 polypeptide Polymers 0.000 description 7
- 108091028043 Nucleic acid sequence Proteins 0.000 description 6
- 235000015872 dietary supplement Nutrition 0.000 description 6
- 235000013305 food Nutrition 0.000 description 6
- 244000005700 microbiome Species 0.000 description 6
- 230000035772 mutation Effects 0.000 description 6
- 239000000047 product Substances 0.000 description 6
- 238000006467 substitution reaction Methods 0.000 description 6
- 238000007792 addition Methods 0.000 description 5
- 230000004071 biological effect Effects 0.000 description 5
- 230000000694 effects Effects 0.000 description 5
- 230000014616 translation Effects 0.000 description 5
- 230000015556 catabolic process Effects 0.000 description 4
- 238000006731 degradation reaction Methods 0.000 description 4
- 238000000855 fermentation Methods 0.000 description 4
- 230000004151 fermentation Effects 0.000 description 4
- 235000012054 meals Nutrition 0.000 description 4
- 239000013612 plasmid Substances 0.000 description 4
- 235000019833 protease Nutrition 0.000 description 4
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 4
- 208000015943 Coeliac disease Diseases 0.000 description 3
- 102000001708 Protein Isoforms Human genes 0.000 description 3
- 108010029485 Protein Isoforms Proteins 0.000 description 3
- 241000187747 Streptomyces Species 0.000 description 3
- 238000004458 analytical method Methods 0.000 description 3
- 238000006243 chemical reaction Methods 0.000 description 3
- 238000012217 deletion Methods 0.000 description 3
- 230000037430 deletion Effects 0.000 description 3
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 3
- 230000002496 gastric effect Effects 0.000 description 3
- 239000000499 gel Substances 0.000 description 3
- 239000001963 growth medium Substances 0.000 description 3
- 238000012405 in silico analysis Methods 0.000 description 3
- 239000000463 material Substances 0.000 description 3
- 230000000813 microbial effect Effects 0.000 description 3
- 239000002773 nucleotide Substances 0.000 description 3
- 125000003729 nucleotide group Chemical group 0.000 description 3
- 230000002797 proteolythic effect Effects 0.000 description 3
- 241000093906 Actinoallomurus sp. Species 0.000 description 2
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 2
- 241001001250 Catenulispora Species 0.000 description 2
- 108020004705 Codon Proteins 0.000 description 2
- 201000004624 Dermatitis Diseases 0.000 description 2
- 241000196324 Embryophyta Species 0.000 description 2
- 241001198387 Escherichia coli BL21(DE3) Species 0.000 description 2
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 2
- 206010017533 Fungal infection Diseases 0.000 description 2
- 235000010469 Glycine max Nutrition 0.000 description 2
- 241001430082 Ktedonobacter Species 0.000 description 2
- 241001465754 Metazoa Species 0.000 description 2
- 108010038807 Oligopeptides Proteins 0.000 description 2
- 102000015636 Oligopeptides Human genes 0.000 description 2
- BQCADISMDOOEFD-UHFFFAOYSA-N Silver Chemical compound [Ag] BQCADISMDOOEFD-UHFFFAOYSA-N 0.000 description 2
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 2
- 125000000539 amino acid group Chemical group 0.000 description 2
- 229910052799 carbon Inorganic materials 0.000 description 2
- 235000013339 cereals Nutrition 0.000 description 2
- 238000012512 characterization method Methods 0.000 description 2
- 201000010099 disease Diseases 0.000 description 2
- 238000002474 experimental method Methods 0.000 description 2
- 239000000706 filtrate Substances 0.000 description 2
- 238000001914 filtration Methods 0.000 description 2
- 102000035122 glycosylated proteins Human genes 0.000 description 2
- 108091005608 glycosylated proteins Proteins 0.000 description 2
- 238000000589 high-performance liquid chromatography-mass spectrometry Methods 0.000 description 2
- 230000007062 hydrolysis Effects 0.000 description 2
- 238000006460 hydrolysis reaction Methods 0.000 description 2
- 235000021056 liquid food Nutrition 0.000 description 2
- 238000002703 mutagenesis Methods 0.000 description 2
- 231100000350 mutagenesis Toxicity 0.000 description 2
- 235000015097 nutrients Nutrition 0.000 description 2
- 239000008194 pharmaceutical composition Substances 0.000 description 2
- 238000001556 precipitation Methods 0.000 description 2
- 238000012545 processing Methods 0.000 description 2
- 238000000746 purification Methods 0.000 description 2
- 229910052709 silver Inorganic materials 0.000 description 2
- 239000004332 silver Substances 0.000 description 2
- 239000000243 solution Substances 0.000 description 2
- 238000010186 staining Methods 0.000 description 2
- 238000010561 standard procedure Methods 0.000 description 2
- 239000000126 substance Substances 0.000 description 2
- 239000000758 substrate Substances 0.000 description 2
- 231100000331 toxic Toxicity 0.000 description 2
- 230000002588 toxic effect Effects 0.000 description 2
- 230000009261 transgenic effect Effects 0.000 description 2
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 1
- AUUIARVPJHGTSA-UHFFFAOYSA-N 3-(aminomethyl)chromen-2-one Chemical compound C1=CC=C2OC(=O)C(CN)=CC2=C1 AUUIARVPJHGTSA-UHFFFAOYSA-N 0.000 description 1
- HZWWPUTXBJEENE-UHFFFAOYSA-N 5-amino-2-[[1-[5-amino-2-[[1-[2-amino-3-(4-hydroxyphenyl)propanoyl]pyrrolidine-2-carbonyl]amino]-5-oxopentanoyl]pyrrolidine-2-carbonyl]amino]-5-oxopentanoic acid Chemical compound C1CCC(C(=O)NC(CCC(N)=O)C(=O)N2C(CCC2)C(=O)NC(CCC(N)=O)C(O)=O)N1C(=O)C(N)CC1=CC=C(O)C=C1 HZWWPUTXBJEENE-UHFFFAOYSA-N 0.000 description 1
- 241001001804 Actinospica Species 0.000 description 1
- 229920001817 Agar Polymers 0.000 description 1
- QGZKDVFQNNGYKY-UHFFFAOYSA-O Ammonium Chemical compound [NH4+] QGZKDVFQNNGYKY-UHFFFAOYSA-O 0.000 description 1
- 241000193830 Bacillus <bacterium> Species 0.000 description 1
- 241000193755 Bacillus cereus Species 0.000 description 1
- 244000063299 Bacillus subtilis Species 0.000 description 1
- 235000014469 Bacillus subtilis Nutrition 0.000 description 1
- 240000002791 Brassica napus Species 0.000 description 1
- 235000004977 Brassica sinapistrum Nutrition 0.000 description 1
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 1
- 241000919932 Catenulispora acidiphila Species 0.000 description 1
- 108091026890 Coding region Proteins 0.000 description 1
- 208000011231 Crohn disease Diseases 0.000 description 1
- 102000003779 Dipeptidyl-peptidases and tripeptidyl-peptidases Human genes 0.000 description 1
- 108090000194 Dipeptidyl-peptidases and tripeptidyl-peptidases Proteins 0.000 description 1
- 241000588724 Escherichia coli Species 0.000 description 1
- 241001302160 Escherichia coli str. K-12 substr. DH10B Species 0.000 description 1
- 241000192125 Firmicutes Species 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
- 244000068988 Glycine max Species 0.000 description 1
- 241000238631 Hexapoda Species 0.000 description 1
- 241000282412 Homo Species 0.000 description 1
- 101000610620 Homo sapiens Putative serine protease 29 Proteins 0.000 description 1
- 206010020751 Hypersensitivity Diseases 0.000 description 1
- 241001430080 Ktedonobacter racemifer Species 0.000 description 1
- ONIBWKKTOPOVIA-BYPYZUCNSA-N L-Proline Chemical compound OC(=O)[C@@H]1CCCN1 ONIBWKKTOPOVIA-BYPYZUCNSA-N 0.000 description 1
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 1
- 239000004367 Lipase Substances 0.000 description 1
- 102000004882 Lipase Human genes 0.000 description 1
- 108090001060 Lipase Proteins 0.000 description 1
- 241000219745 Lupinus Species 0.000 description 1
- 241000187708 Micromonospora Species 0.000 description 1
- 208000031888 Mycoses Diseases 0.000 description 1
- 101100477212 Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) sed4 gene Proteins 0.000 description 1
- 238000012408 PCR amplification Methods 0.000 description 1
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 1
- 101710088675 Proline-rich peptide Proteins 0.000 description 1
- 102000056251 Prolyl Oligopeptidases Human genes 0.000 description 1
- 108700015930 Prolyl Oligopeptidases Proteins 0.000 description 1
- 108010076504 Protein Sorting Signals Proteins 0.000 description 1
- 102100040345 Putative serine protease 29 Human genes 0.000 description 1
- 241001257175 Rugosimonospora Species 0.000 description 1
- 235000019764 Soybean Meal Nutrition 0.000 description 1
- 241000319051 Streptacidiphilus Species 0.000 description 1
- 241000187180 Streptomyces sp. Species 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
- 238000010521 absorption reaction Methods 0.000 description 1
- 239000008351 acetate buffer Substances 0.000 description 1
- 238000005377 adsorption chromatography Methods 0.000 description 1
- 239000008272 agar Substances 0.000 description 1
- 230000004075 alteration Effects 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- 235000013405 beer Nutrition 0.000 description 1
- 235000013361 beverage Nutrition 0.000 description 1
- 238000004166 bioassay Methods 0.000 description 1
- OWMVSZAMULFTJU-UHFFFAOYSA-N bis-tris Chemical compound OCCN(CCO)C(CO)(CO)CO OWMVSZAMULFTJU-UHFFFAOYSA-N 0.000 description 1
- 239000007853 buffer solution Substances 0.000 description 1
- 229940041514 candida albicans extract Drugs 0.000 description 1
- 239000006143 cell culture medium Substances 0.000 description 1
- 239000013592 cell lysate Substances 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 238000004140 cleaning Methods 0.000 description 1
- 238000010367 cloning Methods 0.000 description 1
- 230000000295 complement effect Effects 0.000 description 1
- 239000000306 component Substances 0.000 description 1
- 235000005822 corn Nutrition 0.000 description 1
- 238000012258 culturing Methods 0.000 description 1
- 238000005520 cutting process Methods 0.000 description 1
- 230000007812 deficiency Effects 0.000 description 1
- 230000000593 degrading effect Effects 0.000 description 1
- 239000008121 dextrose Substances 0.000 description 1
- 238000000502 dialysis Methods 0.000 description 1
- 208000035475 disorder Diseases 0.000 description 1
- 239000012153 distilled water Substances 0.000 description 1
- 235000013399 edible fruits Nutrition 0.000 description 1
- 230000003241 endoproteolytic effect Effects 0.000 description 1
- 210000001842 enterocyte Anatomy 0.000 description 1
- 210000003527 eukaryotic cell Anatomy 0.000 description 1
- 238000011156 evaluation Methods 0.000 description 1
- 239000013604 expression vector Substances 0.000 description 1
- 235000012041 food component Nutrition 0.000 description 1
- 239000005428 food component Substances 0.000 description 1
- 238000004108 freeze drying Methods 0.000 description 1
- 230000005714 functional activity Effects 0.000 description 1
- 230000002538 fungal effect Effects 0.000 description 1
- 208000024386 fungal infectious disease Diseases 0.000 description 1
- 210000001035 gastrointestinal tract Anatomy 0.000 description 1
- 238000002523 gelfiltration Methods 0.000 description 1
- 230000002068 genetic effect Effects 0.000 description 1
- 238000000338 in vitro Methods 0.000 description 1
- 238000002347 injection Methods 0.000 description 1
- 239000007924 injection Substances 0.000 description 1
- 238000004255 ion exchange chromatography Methods 0.000 description 1
- 230000005865 ionizing radiation Effects 0.000 description 1
- 238000001155 isoelectric focusing Methods 0.000 description 1
- 229930027917 kanamycin Natural products 0.000 description 1
- SBUJHOSQTJFQJX-NOAMYHISSA-N kanamycin Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CN)O[C@@H]1O[C@H]1[C@H](O)[C@@H](O[C@@H]2[C@@H]([C@@H](N)[C@H](O)[C@@H](CO)O2)O)[C@H](N)C[C@@H]1N SBUJHOSQTJFQJX-NOAMYHISSA-N 0.000 description 1
- 229960000318 kanamycin Drugs 0.000 description 1
- 229930182823 kanamycin A Natural products 0.000 description 1
- 235000019421 lipase Nutrition 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 238000012423 maintenance Methods 0.000 description 1
- 210000004962 mammalian cell Anatomy 0.000 description 1
- 239000011159 matrix material Substances 0.000 description 1
- 230000001404 mediated effect Effects 0.000 description 1
- 229930182817 methionine Natural products 0.000 description 1
- 239000003471 mutagenic agent Substances 0.000 description 1
- 229910052757 nitrogen Inorganic materials 0.000 description 1
- 239000003960 organic solvent Substances 0.000 description 1
- 108091033319 polynucleotide Proteins 0.000 description 1
- 102000040430 polynucleotide Human genes 0.000 description 1
- 239000002157 polynucleotide Substances 0.000 description 1
- 239000000843 powder Substances 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 230000002265 prevention Effects 0.000 description 1
- 210000001236 prokaryotic cell Anatomy 0.000 description 1
- 125000001500 prolyl group Chemical group [H]N1C([H])(C(=O)[*])C([H])([H])C([H])([H])C1([H])[H] 0.000 description 1
- 238000003259 recombinant expression Methods 0.000 description 1
- 238000005185 salting out Methods 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 239000000523 sample Substances 0.000 description 1
- 239000012723 sample buffer Substances 0.000 description 1
- 230000028327 secretion Effects 0.000 description 1
- 238000012807 shake-flask culturing Methods 0.000 description 1
- 238000002741 site-directed mutagenesis Methods 0.000 description 1
- 239000011780 sodium chloride Substances 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 239000004455 soybean meal Substances 0.000 description 1
- 241000894007 species Species 0.000 description 1
- 238000001228 spectrum Methods 0.000 description 1
- 230000001954 sterilising effect Effects 0.000 description 1
- 108010043175 succinylalanylalanyl-prolyl-phenylalanine-4-methylcoumaryl-7-amide Proteins 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 208000011580 syndromic disease Diseases 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- 238000012546 transfer Methods 0.000 description 1
- 238000013519 translation Methods 0.000 description 1
- 230000013819 transposition, DNA-mediated Effects 0.000 description 1
- 238000000108 ultra-filtration Methods 0.000 description 1
- 239000013598 vector Substances 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
- 230000004584 weight gain Effects 0.000 description 1
- 235000019786 weight gain Nutrition 0.000 description 1
- 210000005253 yeast cell Anatomy 0.000 description 1
- 239000012138 yeast extract Substances 0.000 description 1
Classifications
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/43—Enzymes; Proenzymes; Derivatives thereof
- A61K38/46—Hydrolases (3)
- A61K38/48—Hydrolases (3) acting on peptide bonds (3.4)
- A61K38/482—Serine endopeptidases (3.4.21)
-
- 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
- A23J3/346—Working-up of proteins for foodstuffs by hydrolysis using chemical agents using enzymes of vegetable proteins
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES, NOT OTHERWISE PROVIDED FOR; PREPARATION OR TREATMENT THEREOF
- A23L2/00—Non-alcoholic beverages; Dry compositions or concentrates therefor; Preparation or treatment thereof
- A23L2/52—Adding ingredients
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES, NOT OTHERWISE PROVIDED FOR; PREPARATION OR TREATMENT THEREOF
- A23L33/00—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof
- A23L33/10—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof using additives
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/43—Enzymes; Proenzymes; Derivatives thereof
- A61K38/46—Hydrolases (3)
- A61K38/48—Hydrolases (3) acting on peptide bonds (3.4)
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P1/00—Drugs for disorders of the alimentary tract or the digestive system
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P17/00—Drugs for dermatological disorders
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
- A61P37/02—Immunomodulators
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
- C12N9/50—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25)
- C12N9/52—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from bacteria or Archaea
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23V—INDEXING SCHEME RELATING TO FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES AND LACTIC OR PROPIONIC ACID BACTERIA USED IN FOODSTUFFS OR FOOD PREPARATION
- A23V2002/00—Food compositions, function of food ingredients or processes for food or foodstuffs
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y304/00—Hydrolases acting on peptide bonds, i.e. peptidases (3.4)
- C12Y304/21—Serine endopeptidases (3.4.21)
- C12Y304/21026—Prolyl oligopeptidase (3.4.21.26), i.e. proline-specific endopeptidase
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Animal Behavior & Ethology (AREA)
- Organic Chemistry (AREA)
- Pharmacology & Pharmacy (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Immunology (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Polymers & Plastics (AREA)
- Food Science & Technology (AREA)
- Nutrition Science (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Gastroenterology & Hepatology (AREA)
- Genetics & Genomics (AREA)
- Epidemiology (AREA)
- Wood Science & Technology (AREA)
- Zoology (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Biochemistry (AREA)
- General Engineering & Computer Science (AREA)
- Biomedical Technology (AREA)
- Microbiology (AREA)
- Molecular Biology (AREA)
- Biotechnology (AREA)
- Mycology (AREA)
- Dermatology (AREA)
- Enzymes And Modification Thereof (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Coloring Foods And Improving Nutritive Qualities (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| EP11425291 | 2011-12-06 | ||
| EP11425291 | 2011-12-06 | ||
| PCT/EP2012/071816 WO2013083338A1 (en) | 2011-12-06 | 2012-11-05 | New proteases able to hydrolyze gluten peptides and proteins at acidic ph, from the actinomycete actinoallomurus |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| ES2595500T3 true ES2595500T3 (es) | 2016-12-30 |
Family
ID=47137719
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| ES12781098.4T Active ES2595500T3 (es) | 2011-12-06 | 2012-11-05 | Nuevas proteasas que pueden hidrolizar péptidos y proteínas de gluten a un pH ácido, procedentes del actinomiceto Actinoallomurus |
Country Status (11)
| Country | Link |
|---|---|
| US (2) | US20140356345A1 (https=) |
| EP (1) | EP2788018B1 (https=) |
| JP (1) | JP6203743B2 (https=) |
| CN (1) | CN104039345B (https=) |
| AU (1) | AU2012348782B2 (https=) |
| BR (1) | BR112014012100B1 (https=) |
| CA (1) | CA2852365C (https=) |
| EA (1) | EA028228B1 (https=) |
| ES (1) | ES2595500T3 (https=) |
| IN (1) | IN2014CN04131A (https=) |
| WO (1) | WO2013083338A1 (https=) |
Families Citing this family (14)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CA2882502A1 (en) | 2011-08-10 | 2013-02-14 | University Of Washington Through Its Center For Commercialization | Compositions and methods for treating celiac sprue disease |
| US10266815B2 (en) * | 2013-08-14 | 2019-04-23 | University Of Washington Through Its Center For Commercialization | Compositions and methods for treating celiac sprue disease |
| WO2015032620A1 (en) | 2013-09-05 | 2015-03-12 | Dsm Ip Assets B.V. | Use of an acidic soft drink to enhance the efficacy of a gluten-digesting enzyme |
| EP3074426B1 (en) * | 2013-11-26 | 2020-07-08 | Novozymes A/S | Milling process |
| RU2741080C2 (ru) * | 2014-10-24 | 2021-01-22 | ДюПон НЬЮТРИШН БАЙОСАЙЕНСИЗ АпС | Трипептидилпептидазы, способные воздействовать на связи с участием пролина, и их применения |
| NZ737500A (en) | 2015-06-08 | 2025-02-28 | Univ Washington | Compositions and methods for treating celiac sprue disease |
| WO2017139659A1 (en) | 2016-02-11 | 2017-08-17 | Trustees Of Boston University | Rothia subtilisins, s8a family proteases, as therapeutic enzymes for application in gluten-intolerance disorders |
| IT201900012942A1 (it) | 2019-07-25 | 2021-01-25 | Nemysis Ltd | Metodo per la produzione di una composizione enzimatica comprendente una endopeptidasi ricombinante |
| JP2022542835A (ja) * | 2019-07-25 | 2022-10-07 | ネミシス リミテッド | 組換えエンドペプチダーゼを含む酵素組成物の製造方法 |
| CN111172138B (zh) * | 2020-02-14 | 2022-03-25 | 江南大学 | 一种蛋白水解酶及其在蛋白肽生产中的应用 |
| IT202100018254A1 (it) | 2021-07-12 | 2023-01-12 | Nemysis Ltd | New systems for producing recombinant proteins/ nuovi sistemi di produzione di proteine ricombinanti |
| CN114438044B (zh) * | 2022-01-14 | 2024-03-29 | 南昌大学 | 一种高效降解麸质蛋白的多酶复合体及其应用 |
| EP4709834A1 (en) * | 2023-05-11 | 2026-03-18 | Digestiva, Inc. | Wine dehazing methods and compositions |
| WO2025067635A1 (en) * | 2023-09-26 | 2025-04-03 | Amyra Biotech Ag | Pharmaceutical compositions comprising exopeptidases and uses thereof |
Family Cites Families (12)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP3104935B2 (ja) | 1992-05-28 | 2000-10-30 | 株式会社ブリヂストン | 空気入りタイヤ |
| US7320788B2 (en) | 2002-02-14 | 2008-01-22 | The Board Of Trustees Of The Leland Stanford Junior University | Enzyme treatment of foodstuffs for Celiac Sprue |
| AU2003215272B2 (en) * | 2002-02-14 | 2008-04-03 | The Board Of Trustees Of The Leland Stanford Junior University | Enzyme treatment of foodstuffs for celiac sprue |
| US7265093B2 (en) * | 2002-05-14 | 2007-09-04 | The Board Of Trustees Of The Leland Stanford Junior University | Drug therapy for Celiac Sprue |
| EP1673457B1 (en) | 2003-08-25 | 2011-05-18 | Funzyme Biotechnologies SA | Novel fungal proteins and nucleic acids encoding same |
| HUE044812T2 (hu) | 2003-09-23 | 2019-11-28 | Dsm Ip Assets Bv | Prolinspecifikus endoproteázok alkalmazása peptidek és fehérjék hidrolízisére |
| NL1027650C1 (nl) | 2004-12-03 | 2006-06-07 | Leonardus Antonius Luttikhold | Transporthulpmiddel voor deuren en panelen. |
| EP1985698A1 (en) * | 2007-04-25 | 2008-10-29 | Nestec S.A. | Peptidases from basidiomycetes |
| US20120276075A1 (en) * | 2009-12-21 | 2012-11-01 | Centre Hospitalier Universitaire Vaudois (Chuv) | Synergic action of a prolyl protease and tripeptidyl proteases |
| EP2531521B1 (en) * | 2010-02-02 | 2017-09-06 | Amano Enzyme USA., Ltd. | Use of proteases for gluten intolerance |
| US20130045195A1 (en) * | 2010-03-30 | 2013-02-21 | Alvine Pharmaceuticals, Inc. | Proteases for Degrading Gluten |
| JP2011211997A (ja) * | 2010-04-02 | 2011-10-27 | Astellas Pharma Inc | アントラサイクリン化合物を生産する微生物 |
-
2012
- 2012-11-05 ES ES12781098.4T patent/ES2595500T3/es active Active
- 2012-11-05 WO PCT/EP2012/071816 patent/WO2013083338A1/en not_active Ceased
- 2012-11-05 BR BR112014012100-1A patent/BR112014012100B1/pt active IP Right Grant
- 2012-11-05 US US14/356,122 patent/US20140356345A1/en not_active Abandoned
- 2012-11-05 EP EP12781098.4A patent/EP2788018B1/en active Active
- 2012-11-05 CA CA2852365A patent/CA2852365C/en active Active
- 2012-11-05 CN CN201280060514.5A patent/CN104039345B/zh active Active
- 2012-11-05 EA EA201491117A patent/EA028228B1/ru not_active IP Right Cessation
- 2012-11-05 AU AU2012348782A patent/AU2012348782B2/en active Active
- 2012-11-05 IN IN4131CHN2014 patent/IN2014CN04131A/en unknown
- 2012-11-05 JP JP2014545146A patent/JP6203743B2/ja active Active
-
2015
- 2015-11-23 US US14/949,503 patent/US10201593B2/en active Active
Also Published As
| Publication number | Publication date |
|---|---|
| US20160114009A1 (en) | 2016-04-28 |
| WO2013083338A1 (en) | 2013-06-13 |
| CA2852365C (en) | 2021-01-26 |
| IN2014CN04131A (https=) | 2015-07-17 |
| US10201593B2 (en) | 2019-02-12 |
| EA028228B1 (ru) | 2017-10-31 |
| AU2012348782B2 (en) | 2017-10-26 |
| US20140356345A1 (en) | 2014-12-04 |
| CN104039345B (zh) | 2016-11-09 |
| CA2852365A1 (en) | 2013-06-13 |
| JP6203743B2 (ja) | 2017-09-27 |
| BR112014012100A2 (pt) | 2020-10-27 |
| EA201491117A1 (ru) | 2014-09-30 |
| EP2788018A1 (en) | 2014-10-15 |
| AU2012348782A1 (en) | 2014-05-15 |
| CN104039345A (zh) | 2014-09-10 |
| EP2788018B1 (en) | 2016-06-29 |
| HK1198244A1 (en) | 2015-03-20 |
| BR112014012100B1 (pt) | 2023-04-18 |
| JP2015500641A (ja) | 2015-01-08 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| ES2595500T3 (es) | Nuevas proteasas que pueden hidrolizar péptidos y proteínas de gluten a un pH ácido, procedentes del actinomiceto Actinoallomurus | |
| CA2536635C (en) | Novel fungal proteins and nucleic acids encoding same | |
| Zaghloul et al. | Biodegradation of chicken feathers waste directed by Bacillus subtilis recombinant cells: Scaling up in a laboratory scale fermentor | |
| Alvarez-Sieiro et al. | Generation of food-grade recombinant Lactobacillus casei delivering Myxococcus xanthus prolyl endopeptidase | |
| KR102778820B1 (ko) | 콜라겐을 분해할 수 있는 균주 및 이의 응용 | |
| CN116064492A (zh) | 一种具有高活性的重组酰胺水解酶及其编码基因、重组载体及应用 | |
| Abidi et al. | MS analysis and molecular characterization of Botrytis cinerea protease Prot-2. Use in bioactive peptides production | |
| WO2021200955A1 (ja) | コラゲナーゼ剤及びその用途 | |
| KR101756769B1 (ko) | 서열번호 1의 살조활성 단백질분해효소, 이를 코딩하는 유전자 및 이를 포함하는 살조제제 | |
| WO2023054315A1 (ja) | コラーゲントリペプチド製造又は軟骨分解のための酵素剤 | |
| US20220162619A1 (en) | Preparation of wheat cysteine protease triticain-alpha produced in soluble form and method of producing same | |
| CN1732259B (zh) | 分解难分解性蛋白质的方法 | |
| CN108070605A (zh) | 多菌灵降解酶CbmA及其编码基因和应用 | |
| AU2020318422A1 (en) | Method for the production of an enzymatic composition comprising a recombinant endopeptidase | |
| Tamilmani et al. | Production of an extra cellular feather degrading enzyme by Bacillus licheniformis isolated from poultry farm soil in Namakkal district (Tamilnadu) | |
| CN111607579A (zh) | 一种赭曲霉毒素水解酶及其编码基因、重组载体及应用 | |
| JP6218512B2 (ja) | アユ冷水病菌由来毒素 | |
| KR101608977B1 (ko) | 서열번호 4를 포함하는 살조활성 단백질분해효소, 이를 코딩하는 유전자 및 이를 포함하는 살조제제 | |
| KR101608979B1 (ko) | 서열번호 5를 포함하는 살조활성 단백질분해효소, 이를 코딩하는 유전자 및 이를 포함하는 살조제제 | |
| KR101617362B1 (ko) | 서열번호 6를 포함하는 살조활성 단백질분해효소, 이를 코딩하는 유전자 및 이를 포함하는 살조제제 | |
| CN109913435B (zh) | 一种羧肽酶及其编码基因、重组载体、重组菌及应用 | |
| KR20100028357A (ko) | 스트렙토마이세스 그리세우스 변이주 및 이를 이용한 트립신 함량이 높은 프로네이즈 생산방법 | |
| KR20150014425A (ko) | 서열번호 7를 포함하는 살조활성 단백질분해효소, 이를 코딩하는 유전자 및 이를 포함하는 살조제제 | |
| HK1198244B (en) | New proteases able to hydrolyze gluten peptides and proteins at acidic ph, from the actinomycete actinoallomurus |