KR870000425A - 효소의 고정화방법, 구체적으로는 세포결합효소를 세포군입자로 전환시키는 방법 - Google Patents

효소의 고정화방법, 구체적으로는 세포결합효소를 세포군입자로 전환시키는 방법 Download PDF

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KR870000425A
KR870000425A KR1019860004716A KR860004716A KR870000425A KR 870000425 A KR870000425 A KR 870000425A KR 1019860004716 A KR1019860004716 A KR 1019860004716A KR 860004716 A KR860004716 A KR 860004716A KR 870000425 A KR870000425 A KR 870000425A
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cell
enzymatically active
active microbial
enzyme
cells
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KR940004542B1 (ko
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뵘펠만 모겐스
뷤펠만 모겐스
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노보 노르디스크 아크티에 셀스카브
윌리암 앤더슨
노보인두스트리 에이/에스
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    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
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    • C12N11/00Carrier-bound or immobilised enzymes; Carrier-bound or immobilised microbial cells; Preparation thereof
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    • C12P19/00Preparation of compounds containing saccharide radicals
    • C12P19/24Preparation of compounds containing saccharide radicals produced by the action of an isomerase, e.g. fructose
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    • C12N11/00Carrier-bound or immobilised enzymes; Carrier-bound or immobilised microbial cells; Preparation thereof
    • C12N11/02Enzymes or microbial cells immobilised on or in an organic carrier
    • C12N11/08Enzymes or microbial cells immobilised on or in an organic carrier the carrier being a synthetic polymer
    • C12N11/089Enzymes or microbial cells immobilised on or in an organic carrier the carrier being a synthetic polymer obtained otherwise than by reactions only involving carbon-to-carbon unsaturated bonds
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    • C12N9/00Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/88Lyases (4.)
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    • C12PFERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
    • C12P13/00Preparation of nitrogen-containing organic compounds
    • C12P13/04Alpha- or beta- amino acids
    • C12P13/22Tryptophan; Tyrosine; Phenylalanine; 3,4-Dihydroxyphenylalanine
    • C12P13/227Tryptophan

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Abstract

내용 없음

Description

효소의 고정화방법, 구체적으로는 세포결합효소를 세포군입자로 전환시키는 방법
본 내용은 요부공개 건이므로 전문내용을 수록하지 않았음

Claims (9)

  1. 효소학적활성 미생물 세포와 세포물질의 수성분산액을 수성폴리아제티딘 전중합체와 이러한 분산액을 혼합시키고 이어서 숙성시키는 것을 수반하는, 고정화시키는 방법에 있어서,
    효소학적 활성 미생물 세포슬러지를 글루타르알데히드로 처리하여 이로써 부분 가교결합이 일어나도록 하며, 그후 부분 가교결합된 세포 슬러지를 70-90%범위의 수분함량으로 수분제거시키고, 이로써 반죽상 세포군을 발생시키며, 상기 반죽상 세포군을 수성 폴리아제티딘 전중합체와 혼합한 다음 혼합된 반죽상 세포군과 수성 폴리아제티딘 전중합체를 세분하고, 이어서 전술한 숙성을 시켜 이로써 입자형태 고정화 효소 생성물을 가져오는 것을 특징으로하는 효소학적 활성미생물세포와 세포물질의 수성분산액을 고정화시키는 방법.
  2. 제1항에 있어서, 과립혼합물의 수분함량은 숙성의 동안에 약 25중량%이하로 감소되는 것을 특징으로하는 방법.
  3. 제1항에 있어서, 글루타르 알데히드는 세포슬러지 건조물질의 5%-40중량%로 이루어지는 것을 특징으로 하는 방법.
  4. 제1항에 있어서, 폴리아제티딘은 세포슬러지 건조 물질의 5-30중량%로 이루어지는 것을 특징으로 하는 방법.
  5. 제1항에 있어서, 효소학적 활성 미생물 세포는 스트렙토미세스 뮤리너스 집락의 글루코오스 이성화 효소 생성주로 부터의 세포로 이루어지는 것을 특징으로 하는 방법.
  6. 제1항에 있어서, 효소학적활성 미생물세포는 트립토판 합성효소생성 미생물 주로부터의 세포로 이루어지는 것을 특징으로 하는 방법.
  7. 제6항에 있어서, 세포는 E. coli의 주로부터 인것을 특징으로 하는 방법.
  8. 제1항에 있어서, 부분 가교결합된 세포슬러지는 80-85%w/w 범위의 수분함량으로 수분제거되는 것을 특징으로 하는 방법.
  9. 제1항에 있어서, 글루타르알데히드는 세포슬러지 건조물질의 10-20%로 이루어지는 것을 특징으로 하는 방법.
    ※ 참고사항 : 최초출원 내용에 의하여 공개하는 것임.
KR1019860004716A 1985-06-14 1986-06-13 효소의 고정화방법, 구체적으로는 세포결합효소를 세포군입자로 전환시키는 방법 KR940004542B1 (ko)

Applications Claiming Priority (3)

Application Number Priority Date Filing Date Title
DK2692 1985-06-14
DK8502692 1985-06-14
DK269285A DK152764C (da) 1985-06-14 1985-06-14 Fremgangsmaade til fremstilling af et immobiliseret enzymprodukt

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KR870000425A true KR870000425A (ko) 1987-02-18
KR940004542B1 KR940004542B1 (ko) 1994-05-25

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KR1019860004716A KR940004542B1 (ko) 1985-06-14 1986-06-13 효소의 고정화방법, 구체적으로는 세포결합효소를 세포군입자로 전환시키는 방법

Country Status (8)

Country Link
US (1) US4892825A (ko)
EP (1) EP0206687B1 (ko)
JP (1) JPS6255083A (ko)
KR (1) KR940004542B1 (ko)
DE (1) DE3666837D1 (ko)
DK (1) DK152764C (ko)
ES (1) ES8707763A1 (ko)
FI (1) FI83973C (ko)

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DK336987D0 (da) * 1987-07-01 1987-07-01 Novo Industri As Immobiliseringsmetode
US5801022A (en) * 1990-08-03 1998-09-01 Vertex Pharmaceuticals, Incorporated Method of producing a product with crosslinked crystals of thermolysin
US5618710A (en) * 1990-08-03 1997-04-08 Vertex Pharmaceuticals, Inc. Crosslinked enzyme crystals
CA2180826A1 (en) 1994-01-13 1995-07-20 Richard J. Ii Stoner Organic disease control system
FR2755143B1 (fr) * 1996-10-25 1998-11-27 Rhone Poulenc Nutrition Animal Procede de preparation de l'acide 2-hydroxy-4-methylthio-butyrique par utilisation d'une nitrilase
US6465227B1 (en) * 1997-09-09 2002-10-15 Biochemie Gesellschaft M.B.H. Spherical particles containing microorganism cells having enzyme activity
EP1167521A1 (en) * 2000-06-30 2002-01-02 Aventis Animal Nutrition S.A. Coated enzyme-containing catalyst
JP4866112B2 (ja) * 2005-07-27 2012-02-01 三菱化学株式会社 生体物質構造体及び生体物質構造体の製造方法、並びに、生体物質担持体、対象物質の精製方法、アフィニティークロマトグラフィー用容器、分離用チップ、対象物質の解析方法、対象物質の解析用分離装置、及び、センサーチップ
JP2007101520A (ja) * 2005-09-09 2007-04-19 Mitsubishi Chemicals Corp 生体物質複合体、並びに、生体物質複合体担持体、対象物質の精製方法、アフィニティークロマトグラフィー用容器、分離用チップ、対象物質の解析方法、対象物質の解析用分離装置及びセンサーチップ
JP5209478B2 (ja) 2005-09-30 2013-06-12 ノボザイムス アクティーゼルスカブ 酵素の固定化
EP2313501A4 (en) * 2008-03-17 2012-04-04 Immortazyme Company PROCESS FOR PRODUCING BIO-GEL AND CORRESPONDING BIO-GEL
WO2014067933A1 (en) 2012-10-31 2014-05-08 C-Lecta Gmbh Bioactive carrier preparation for enhanced safety in care products and food
CN110982708B (zh) * 2019-12-23 2022-09-06 云南大学 一株丽灰球真菌及其在重金属污染环境生物修复中的应用

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US3779869A (en) * 1971-05-13 1973-12-18 Miles Lab Enzyme stabilization
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Publication number Publication date
US4892825A (en) 1990-01-09
EP0206687B1 (en) 1989-11-08
DK152764C (da) 1988-10-03
DK269285A (da) 1986-12-15
FI862533A0 (fi) 1986-06-13
DK269285D0 (da) 1985-06-14
ES8707763A1 (es) 1987-08-16
FI862533A (fi) 1986-12-15
FI83973B (fi) 1991-06-14
DE3666837D1 (en) 1989-12-14
EP0206687A1 (en) 1986-12-30
FI83973C (fi) 1991-09-25
DK152764B (da) 1988-05-09
KR940004542B1 (ko) 1994-05-25
ES556019A0 (es) 1987-08-16
JPS6255083A (ja) 1987-03-10

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