JP7035079B2 - 安定なプロテアーゼ変異型 - Google Patents

安定なプロテアーゼ変異型 Download PDF

Info

Publication number
JP7035079B2
JP7035079B2 JP2019555724A JP2019555724A JP7035079B2 JP 7035079 B2 JP7035079 B2 JP 7035079B2 JP 2019555724 A JP2019555724 A JP 2019555724A JP 2019555724 A JP2019555724 A JP 2019555724A JP 7035079 B2 JP7035079 B2 JP 7035079B2
Authority
JP
Japan
Prior art keywords
protease variant
seq
kumamoricin
amino acid
variant according
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
Application number
JP2019555724A
Other languages
English (en)
Japanese (ja)
Other versions
JP2020505944A (ja
JP2020505944A5 (https=
Inventor
アンドレアス ミヒェルス
アンドレアス シャイディク
クリスティアン エレンド
クラウディア クラップ
トーマス ホルン
Original Assignee
イーダブル ニュートリション ゲゼルシャフト ミット ベシュレンクテル ハフツング
Priority date (The priority date 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 date listed.)
Filing date
Publication date
Application filed by イーダブル ニュートリション ゲゼルシャフト ミット ベシュレンクテル ハフツング filed Critical イーダブル ニュートリション ゲゼルシャフト ミット ベシュレンクテル ハフツング
Publication of JP2020505944A publication Critical patent/JP2020505944A/ja
Publication of JP2020505944A5 publication Critical patent/JP2020505944A5/ja
Priority to JP2022031591A priority Critical patent/JP7344329B2/ja
Application granted granted Critical
Publication of JP7035079B2 publication Critical patent/JP7035079B2/ja
Active legal-status Critical Current
Anticipated expiration legal-status Critical

Links

Images

Classifications

    • 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
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16—Organic compounds
    • C11D3/38—Products with no well-defined composition, e.g. natural products
    • C11D3/386—Preparations containing enzymes, e.g. protease or amylase
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23K—FODDER
    • A23K20/00—Accessory food factors for animal feeding-stuffs
    • A23K20/10—Organic substances
    • A23K20/189—Enzymes
    • 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
    • C12N9/54—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from bacteria or Archaea bacteria being Bacillus
    • 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)

Landscapes

  • Chemical & Material Sciences (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Health & Medical Sciences (AREA)
  • Engineering & Computer Science (AREA)
  • Organic Chemistry (AREA)
  • Zoology (AREA)
  • Wood Science & Technology (AREA)
  • Bioinformatics & Cheminformatics (AREA)
  • Genetics & Genomics (AREA)
  • Biochemistry (AREA)
  • General Engineering & Computer Science (AREA)
  • General Health & Medical Sciences (AREA)
  • Polymers & Plastics (AREA)
  • Biomedical Technology (AREA)
  • Medicinal Chemistry (AREA)
  • Molecular Biology (AREA)
  • Biotechnology (AREA)
  • Microbiology (AREA)
  • Animal Husbandry (AREA)
  • Food Science & Technology (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • Oil, Petroleum & Natural Gas (AREA)
  • Enzymes And Modification Thereof (AREA)
  • Detergent Compositions (AREA)
  • Fodder In General (AREA)
  • Micro-Organisms Or Cultivation Processes Thereof (AREA)
  • Preparation Of Compounds By Using Micro-Organisms (AREA)
  • Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
JP2019555724A 2016-12-22 2017-12-22 安定なプロテアーゼ変異型 Active JP7035079B2 (ja)

Priority Applications (1)

Application Number Priority Date Filing Date Title
JP2022031591A JP7344329B2 (ja) 2016-12-22 2022-03-02 安定なプロテアーゼ変異型

Applications Claiming Priority (3)

Application Number Priority Date Filing Date Title
EP16206367.1 2016-12-22
EP16206367 2016-12-22
PCT/EP2017/084452 WO2018115473A2 (en) 2016-12-22 2017-12-22 Stable protease variants

Related Child Applications (1)

Application Number Title Priority Date Filing Date
JP2022031591A Division JP7344329B2 (ja) 2016-12-22 2022-03-02 安定なプロテアーゼ変異型

Publications (3)

Publication Number Publication Date
JP2020505944A JP2020505944A (ja) 2020-02-27
JP2020505944A5 JP2020505944A5 (https=) 2021-02-04
JP7035079B2 true JP7035079B2 (ja) 2022-03-14

Family

ID=57629395

Family Applications (2)

Application Number Title Priority Date Filing Date
JP2019555724A Active JP7035079B2 (ja) 2016-12-22 2017-12-22 安定なプロテアーゼ変異型
JP2022031591A Active JP7344329B2 (ja) 2016-12-22 2022-03-02 安定なプロテアーゼ変異型

Family Applications After (1)

Application Number Title Priority Date Filing Date
JP2022031591A Active JP7344329B2 (ja) 2016-12-22 2022-03-02 安定なプロテアーゼ変異型

Country Status (10)

Country Link
US (1) US11396648B2 (https=)
EP (2) EP3559225A2 (https=)
JP (2) JP7035079B2 (https=)
KR (2) KR102686572B1 (https=)
CN (1) CN110325636A (https=)
AU (2) AU2017380106B2 (https=)
BR (1) BR112019012980A2 (https=)
CA (1) CA3047868A1 (https=)
MX (2) MX2019007287A (https=)
WO (1) WO2018115473A2 (https=)

Families Citing this family (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US20250064903A1 (en) * 2020-10-30 2025-02-27 University Of Washington Compositions and methods for treating celiac sprue disease
AU2023213894B2 (en) 2022-01-26 2025-04-10 Digestiva, Inc. Blood glucose stabilizing methods and compositions

Citations (4)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2013023151A2 (en) 2011-08-10 2013-02-14 University Of Washington Through Its Center For Commercialization Compositions and methods for treating celiac sprue disease
WO2015023728A1 (en) 2013-08-14 2015-02-19 University Of Washington Through Its Center For Commercialization Compositions and methods for treating celiac sprue disease
WO2016200880A1 (en) 2015-06-08 2016-12-15 University Of Washington Compositions and methods for treating celiac sprue disease
WO2017220776A1 (en) 2016-06-23 2017-12-28 Ew Nutrition Gmbh Feed composition comprising an acid protease

Family Cites Families (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
EP1600141B1 (en) * 2004-05-24 2013-04-17 3M Deutschland GmbH Collagenolytic active enzyme containing compositions for the treatment of dental caries

Patent Citations (4)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2013023151A2 (en) 2011-08-10 2013-02-14 University Of Washington Through Its Center For Commercialization Compositions and methods for treating celiac sprue disease
WO2015023728A1 (en) 2013-08-14 2015-02-19 University Of Washington Through Its Center For Commercialization Compositions and methods for treating celiac sprue disease
WO2016200880A1 (en) 2015-06-08 2016-12-15 University Of Washington Compositions and methods for treating celiac sprue disease
WO2017220776A1 (en) 2016-06-23 2017-12-28 Ew Nutrition Gmbh Feed composition comprising an acid protease

Non-Patent Citations (3)

* Cited by examiner, † Cited by third party
Title
Kumamoliisin-As，Database UniProtKB/Swiss-Prot [online]，2006年11月28日，Accession No. Q8GB88
Peptidase S53 propeptide，Database Uniprot [online]，Accession No. J9HC20, entry version 19，2016年09月07日
TSURUOKA N. et al.，Appl. Environ. Microbiol.，2003年，Vol.69 No.1，p.162-169

Also Published As

Publication number Publication date
JP7344329B2 (ja) 2023-09-13
KR20190095361A (ko) 2019-08-14
WO2018115473A2 (en) 2018-06-28
JP2022081554A (ja) 2022-05-31
EP3559225A2 (en) 2019-10-30
CN110325636A (zh) 2019-10-11
JP2020505944A (ja) 2020-02-27
MX2019007287A (es) 2019-09-27
BR112019012980A2 (pt) 2020-05-26
EP4732675A2 (en) 2026-04-29
AU2017380106B2 (en) 2024-05-09
KR102686572B1 (ko) 2024-07-19
US11396648B2 (en) 2022-07-26
US20190322994A1 (en) 2019-10-24
CA3047868A1 (en) 2018-06-28
WO2018115473A3 (en) 2019-01-31
MX2024000078A (es) 2024-02-23
AU2024202526A1 (en) 2024-05-30
KR20230107898A (ko) 2023-07-18
AU2017380106A1 (en) 2019-07-04
KR102553627B1 (ko) 2023-07-07

Similar Documents

Publication Publication Date Title
Klomklao et al. Trypsins from yellowfin tuna (Thunnus albacores) spleen: purification and characterization
Lufrano et al. Molecular cloning and characterization of procirsin, an active aspartic protease precursor from Cirsium vulgare (Asteraceae)
Ren et al. Improving the catalytic performance of Proteinase K from Parengyodontium album for use in feather degradation
JP7344329B2 (ja) 安定なプロテアーゼ変異型
CN107208077A (zh) 裂解镰孢毒素的多肽变体、包含所述多肽变体的添加剂和所述添加剂的用途，以及用于裂解镰孢毒素的方法
Beigi et al. Optimization of an extracellular zinc-metalloprotease (SVP2) expression in Escherichia coli BL21 (DE3) using response surface methodology
Yamada et al. A cysteine protease from maize isolated in a complex with cystatin
Teo et al. Cloning and characterization of a metalloprotease from Vibrio harveyi strain AP6
Tarrahimofrad et al. Structural and biochemical characterization of a novel thermophilic Coh01147 protease
Mandujano-González et al. Biochemical study of the extracellular aspartyl protease Eap1 from the phytopathogen fungus Sporisorium reilianum
Park et al. Chlorophyte aspartyl aminopeptidases: ancient origins, expanded families, new locations, and secondary functions
Chen et al. Purification and characterization of a new rhizopuspepsin from Rhizopus oryzae NBRC 4749
Hang et al. Structural insight into a novel neutral metalloproteinase from Paenibacillus spp. BD3526: Implications for mechanisms of rapid inactivation and calcium-dependent stability
EP0970225B1 (en) Improved metallo-endopeptidases
US7776579B2 (en) Method of degrading hardly degradable protein
US20230092791A1 (en) Stable protease variants
Nishikawa et al. Isolation and characterization of a salt-tolerant γ-glutamyl transpeptidase from xerophilic Aspergillus sydowii
Song et al. Functional expression and characterization of a novel aminopeptidase B from Aspergillus niger in Pichia pastoris
Klomklao et al. Trypsin from the Pyloric Ceca of Pectoral Rattail (Coryphaenoides pectoralis): purification and characterization
Oda et al. Overview of the Properties of Glutamic Peptidases That Are Present in Plant and Bacterial Pathogens and Play a Role in Celiac Disease and Cancer
Cao et al. Pepsinogens and pepsins from Japanese seabass (Lateolabrax japonicus)
Li et al. Site-directed mutagenesis of myofibril-bound serine proteinase from Crucian carp: Possible role of Pro95, A127 and I130 on thermal stability
Yamamoto et al. Molecular characterization of a prolyl endopeptidase from a feather-degrading thermophile Meiothermus ruber H328
US7355004B2 (en) Protein lipase inhibitor for flour and dough
WO2015165472A2 (en) Cold-active alpha-amylase

Legal Events

Date Code Title Description
A521 Request for written amendment filed

Free format text: JAPANESE INTERMEDIATE CODE: A523

Effective date: 20201221

A621 Written request for application examination

Free format text: JAPANESE INTERMEDIATE CODE: A621

Effective date: 20201221

A977 Report on retrieval

Free format text: JAPANESE INTERMEDIATE CODE: A971007

Effective date: 20211004

A131 Notification of reasons for refusal

Free format text: JAPANESE INTERMEDIATE CODE: A131

Effective date: 20211026

A521 Request for written amendment filed

Free format text: JAPANESE INTERMEDIATE CODE: A523

Effective date: 20220126

TRDD Decision of grant or rejection written
A01 Written decision to grant a patent or to grant a registration (utility model)

Free format text: JAPANESE INTERMEDIATE CODE: A01

Effective date: 20220201

A61 First payment of annual fees (during grant procedure)

Free format text: JAPANESE INTERMEDIATE CODE: A61

Effective date: 20220302

R150 Certificate of patent or registration of utility model

Ref document number: 7035079

Country of ref document: JP

Free format text: JAPANESE INTERMEDIATE CODE: R150

R250 Receipt of annual fees

Free format text: JAPANESE INTERMEDIATE CODE: R250

R250 Receipt of annual fees

Free format text: JAPANESE INTERMEDIATE CODE: R250