KR960702008A - 효소생성방법(processes for producing an enzyme) - Google Patents

효소생성방법(processes for producing an enzyme)

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KR960702008A
KR960702008A KR1019950704898A KR19950704898A KR960702008A KR 960702008 A KR960702008 A KR 960702008A KR 1019950704898 A KR1019950704898 A KR 1019950704898A KR 19950704898 A KR19950704898 A KR 19950704898A KR 960702008 A KR960702008 A KR 960702008A
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South Korea
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protease
proenzyme
enzyme
active enzyme
nucleic acid
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KR1019950704898A
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하스트룹 스벤
브란너 스벤
라븐 요르겐센 비르테
크리스텐센 토베
보예르 요르겐센 비르기테
알. 슈스터 제프레이
마덴 마크
엘. 모이어 도나
푸글상 클라우스
Original Assignee
안네 제케르
노보 노르디스크 아크티에 셀스카브
원본미기재
노보 노르디스크 바이오테크 인코오퍼레이티드
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Publication of KR960702008A publication Critical patent/KR960702008A/ko

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Abstract

본 발명은 활성효소와 다르고 프로효소를 활성효소로 전환시킬 수 있는 단백질 분해 효소의 존재하에서 활성효소의 프로형태를 발효시키는 것으로 이루어지는 활성효소의 생성 방법, 뿐만아니라 숙주세포, 재조합 발현벡터 그리고 본 방법에서 사용하는데 적합한 숙주 세포에 관한 것이다.

Description

효소생성방법(PROCESSES FOR PRODUCING AN ENZYME)
본 내용은 요부공개 건이므로 전문내용을 수록하지 않았음
제1도는 재조합 트립신-유사 F.oxysporum 프로테아제의 발현에 사용된 발현 플라스미드 pSX183의 구성을 나타내며, 하기의 실시예에서 더 자세히 기술된다.
제2도는 프로 F.oxysporum 프로테아제를 프로세싱하는데 사용된 Bacillus 성숙효소(maturase)와, F.oxysporum 단백질 분해 효소 활성의 비교를 나타낸다.
제3A도는 cDNA의 시퀀싱으로부터 결정된 p45의 게놈 DNA 서열 및 추론된 아미노산 서열을 나타낸다.
제4도는 플라스미드 pDM120의 유전자 지도를 나타낸다.

Claims (25)

  1. 프로효소의 형태로 효소를 발현하는 세포의 발효에 의해 활성효소를 생성하는 방법에 있어서, 이 방법은 활성효소와 다르고 프로효소를 활성효소로 전환시킬 수 있는 단백질 분해효소의 존재하에서 발효를 수행하고, 발효액으로부터 활성효소를 회수하는 것으로 이루어지고, 단백질 분해효소는 발효전에 및/또는 발효도중에 발효액에 첨가되는 것을 특징으로 하는 방법.
  2. 프로효소의 형태로 효소를 발현하는 세포의 발효에 의해 활성효소를 생성하는 방법에 있어서, 이 방법은 활성효소와 다르고 프로효소를 활성효소로 전환시킬 수 있는 단백질 분해효소의 존재하에서 발효를 수행하고, 발효액으로부터 활성효소를 회수하는 것으로 이루어지고, 단백질 분해효소는 프로효소가 발현되는 세포에 존재하는 재조합 DNA 서열에 의해 코드화되고 이것으로부터 발현되는 것을 특징으로 하는 방법.
  3. 제2항에 있어서, 상기 단백질 분해효소의 추가의 양이 세포배양 도중에 첨가되는 것을 특징으로 하는 방법.
  4. 제1항 또는 제2항에 있어서, 발효액에서 세포로부터 발현된 프로효소가 활성효소보다 덜 안정한 것을특징으로 하는 방법.
  5. 제1항 또는 제2항에 있어서, 프로효소를 발현하는 세포는 프로효소를 코드화하는 핵산 서열로 형질전환된 것을 특징으로 하는 방법.
  6. 제1항 또는 제2항에 있어서, 생성되는 효소는 히드룰라제, 옥시도리덕타재, 이소메라제, 옥시다제 또는 트란스페라제인 것을 특징으로 하는 방법.
  7. 제6항에 있어서, 생성되는 효소는 프로테아제, 리파제, 아밀라제, 셀룰라제, 크실란아재, 떽펙틴아제, 퍼옥시다제, 락카제 또는 트란스글루타미나제인 것을 특징으로 하는 방법.
  8. 제7항에 있어서, 생성되는 효소는 트립신-유사 프로테아제인 것을 특징으로 하는 방법.
  9. 제8항에 있어서, 생성되는 효소는 F.oxysporum, F.merismoides, F. redolens, F.samb-ucinum, F.solani 또는 F. verticilloides의 균주 같은 속 Fusarium의 균주로부터 얻을 수 있는 것을 특징으로 하는 방법.
  10. 제9항에 있어서, 생성되는 효소는 독일 괴팅젠 도이췌 잠룽 폰 미크로오르가니스멘에서 수탁번호 DSM2672 하에 기탁된 F.oxysporum 균주로부터 얻을 수 있는 트립신-유사 프로테아제인 것을 특징으로 하는 방법.
  11. 제1항 또는 제2항에 있어서, 프로효소는 프레프로 효소로서 발현되는 것을 특징으로 하는 방법.
  12. 제1항 또는 제2항에 있어서, 단백질 분해효소는 금속-프로테아제, 세린 프로테아제, 아스파르트 프로테아제 또는 시스테인 프로테아제인 것을 특징으로 하는 방법.
  13. 제8항 내지 제10항 중 어느 한항에 있어서, 단백질 분해효소는 중성 금속-프로테아제, 알칼리 프로테아제 또는 서브틸리신인 것을 특징으로 하는 방법.
  14. 제1항 또는 제3항에 있어서, 단백질 분해효소는 단백질 분해효소를 코드화하는 핵산 서열로 형질전환된 숙주세포를 단백질 분해효소를 생성하는데 적합한 조건하에서 배양하고, 배양물로부터 단백질 분해효소를 회수함으로써 생성되는 것을 특징으로 하는 방법.
  15. 제1항 또는 제2항에 있어서, 프로효소 및/또는 단백질 분해효소를 발현하는 세포가 미생물인 것을 특징으로 하는 방법.
  16. 제15항에 있어서, 미생물이 세균 또는 곰팡이인 것을 특징으로 하는 방법.
  17. 제16항에 있어서, 미생물은 가령 속 Bacillus 또는 Streptomyces의 그람-양성 세균, 가령 속 Escherichia의 그람-음성세균, 가령 속 Saccharomyces의 효모, 또는 가령 속 Asperg-illus 또는 Fusarium의 사상 곰팡이인 것을 특징으로 하는 방법.
  18. 활성효소 보다 덜 안정한 프로효소를 활성효로로 전환시킬 수 있는 단백질 분해효소를 코드화하는 핵산서열 및 프로효소를 코드화하는 핵산서열을 함유하는 재조합 숙주세포에 있어서, 핵산서열 중 적어도 하나가 재조합 핵산서열인 것을 특징으로 하는 재조합 숙주세포.
  19. 제18항에 있어서, 프로효소를 코드화하는 핵산서열 및/또는 단백질 분해효소를 코드화하는 핵산서열이 발현 벡터상에서 운반되는 것을 특징으로 하는 재조합 숙주세포.
  20. 활성효소보다 덜 안정한 프로효소를 활성효소로 전환시킬 수 있는 단백질 분해효소를 코드화하는 DNA서열 및 프로효소를 코드화하는 DNA 서열을 함유하는 DNA 구조체.
  21. 제20항에서 정의된 DNA 구조체를 함유하는 재조합 발현 벡터.
  22. 제20항에 따른 DNA 구조체 또는 제21항에 따른 재조합 발현 벡터를 함유하는 재조합 숙주세포.
  23. 제18항 또는 제22항에 있어서, 세균 또는 곰팡이인 것을 특징으로 하는 재조합 숙주 세포.
  24. 제23항에 있어서, 가령 속 Bacillus 또는 Streptomyces의 그람-양성 세균, 가령 속 Escherichia의 그람-음성세균, 가령 속 Saccharomyces의 효모, 또는 가령 속 Aspergillus 또는 Fusarium의 사상 곰팡이인 것을 특징으로 하는 재조합 숙주세포.
  25. 제1항 내지 제17항 중 어느 한 항에 따른 방법에 의해 생성된 활성효소.
    ※ 참고사항 : 최초출원 내용에 의하여 공개하는 것임.
KR1019950704898A 1993-05-05 1994-05-04 효소생성방법(processes for producing an enzyme) KR960702008A (ko)

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US5843753A (en) * 1994-05-04 1998-12-01 Novo Nordisk A/S Metalloprotease having increased activity
AU4114596A (en) * 1994-12-09 1996-06-26 Novo Nordisk A/S A process of producing extracellular proteins in bacteria
US5700686A (en) * 1995-06-06 1997-12-23 Iogen Corporation Protease-treated and purified cellulase compositions and methods for reducing backstaining during enzymatic stonewashing
ATE414775T1 (de) 1997-05-16 2008-12-15 Novozymes Inc Polypeptide mit prolyldipeptidylaminopeptidase- aktivität und dafür kodierende nukleinsäuren
AU6188599A (en) 1998-10-26 2000-05-15 Novozymes A/S Constructing and screening a dna library of interest in filamentous fungal cells
AU2001242299A1 (en) 2000-03-14 2001-09-24 Novozymes A/S Fungal transcriptional activator useful in methods for producing polypeptides
AU2003275172A1 (en) * 2002-09-24 2004-04-19 Novozymes Biotech, Inc. Microbial trypsin variants having chymotrypsin activity and nucleic acids encoding same
JP4880469B2 (ja) 2003-10-23 2012-02-22 ノボザイムス アクティーゼルスカブ 洗剤中で改良された安定性を有するプロテアーゼ
JP4834554B2 (ja) * 2003-11-06 2011-12-14 ジェネンコー・インターナショナル・インク 糸状菌におけるプロテアーゼ抑制剤及びその変異体の発現
EP1756275A1 (en) * 2004-04-23 2007-02-28 Novozymes A/S Method for obtaining mature protease by enzymatic digestion
US20070010416A1 (en) * 2004-10-22 2007-01-11 Novozymes A/S Protease with improved stability in detergents
DK2390321T3 (en) * 2005-10-12 2015-02-23 Procter & Gamble The use and manufacture of a storage stable neutral metalloprotease
US8222372B2 (en) * 2007-04-16 2012-07-17 Novozymes A/S Whey protein hydrolysate
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US5077204A (en) * 1984-06-21 1991-12-31 Chiron Corporation Yeast endopeptidase for basic amino-acid site cleavage, preparation and use
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