• Title/Summary/Keyword: biocatalyst

검색결과 148건 처리시간 0.02초

광학활성 Styrene Oxide 제조를 위한 고기능성 유전자 재조합 Epoxide Hydrolase 생촉매 개발

  • 이수정;이지원;이은정;김희숙;이은열
    • 한국생물공학회:학술대회논문집
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    • 한국생물공학회 2003년도 생물공학의 동향(XII)
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    • pp.435-438
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    • 2003
  • Epoxide hydrolase(EH) catalyze the enantioselective hydrolysis of racemic epoxides to corresponding diols. A recombinant Pichia pastoris with EH from Rhodotorula glutinis has been constructed by reverse transcriptase-polymerase chain reaction(RT-PCR). The recombinant biocatalyst enantioselectively hydrolyze (R)-styrene oxide faster than (S)-enantiomer. The catalytic activity of recombinant biocatalyst was 7-fold higher than that of wild-type strain. The recombinant EH biocatalyst can be used for kinetic resolution for the production of enantiopure styrene oxide.

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Selection and Directed Evolution of New Microbial Biocatalysts and Their Application to Organic Synthesis

  • Asano, Yasuhisa
    • Journal of Applied Biological Chemistry
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    • 제43권4호
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    • pp.207-210
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    • 2000
  • As a typical example of the screening for a microbial biocatalyst from nature, isolation of nitrilesynthesizing microorganisms, characterization of a new enzyme aldoxime dehydratase, and its function in the aldoxime-nitrile pathway are introduced. Catalytic properties of some of our enzymes were improved through a direct evolutionary approach.

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생촉매 반응기에서의 활성도 추정 (Activity estimation in a biocatalyst reactor)

  • 이중헌;유영제;홍주안
    • 제어로봇시스템학회:학술대회논문집
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    • 제어로봇시스템학회 1987년도 한국자동제어학술회의논문집; 한국과학기술대학, 충남; 16-17 Oct. 1987
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    • pp.637-642
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    • 1987
  • In immobilized cell reactors, effective cell mass is a very important parameter which must be estimated during operation for control and regeneration of biocatalyst. In this report, the effective cell mass in immobilized cell reactor was studied using a sequential estimation method. An immobilized yeast reactor was operated in batch recycle mode. The states of the immobilized cell reactor could be estimated from the process data using an extended Kalman filter.

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식품 폐기물을 이용한 친환경 생촉매의 발굴과 인디고 환원에 응용 (Utilization of Food Waste Extract as an Eco-friendly Biocatalyst for Indigo Reduction)

  • 손경희;류동일;신윤숙
    • 한국염색가공학회지
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    • 제32권4호
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    • pp.193-198
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    • 2020
  • In this study, the validity of extracts from food waste as biocatalyst for indigo reduction was examined. Dried food wastes such as apple peel and corn waste were water-extracted and freeze-dried. The reducing power of extracts for indigo was evaluated by the oxidation-reduction potential(ORP) measurement of reduction bath and color strength(K/S value) of the fabrics dyed in the indigo reduction bath. Total sugar contents of the apple peel and corn waste extracts were 60.56% and 62.36%, respectively. Antioxidant activity was 64.78% for the extract of apple peel and 7.96% for the extract of corn waste. Indigo reduction took place quickly with both extracts, and maximum color strength was obtained up to 15.91 and 12.11 within 1-3 days, respectively. The oxidation-reduction potential of reduction bath was stabilized in the range of -500 ~ -620 mV according to the kinds of food waste and the extract concentration. At higher concentration of the extracts, reduction power was maintained for longer time and stronger color strength was obtained. Compared to sodium dithionite, the reducing power of the studied extracts was lower, but the reduction stability was superior to it. The studied extracts were effective biocatalyst as biodegradable and safe alternatives to sodium dithionite for indigo reduction.

미생물 알데히드 환원효소에 의한 선택적 환원 (Selective Reduction by Microbial Aldehyde Reductase)

  • 이영수;김경순
    • 생명과학회지
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    • 제16권3호
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    • pp.375-381
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    • 2006
  • Saccharomyces cerevisiae 로부터 알데히드 환원효소를 정제하였다. 정제된 알데히드 환원효소를 biocatalyst로 사용하여 치환기가 있는 카르보닐 화합물의 선택적 환원을 시도하였다. 효소를 이용한 환원반응의 생성물의 구조를 TLC, GC, Mass, NMR, FT-IR을 이용하여 확인하였으며 효소를 이용한 환원반응이 높은 선택성을 가지고 진행됨을 확인하였다. 또한 이 반응은 알데히드 환원효소의 억제제인 벤조산에 의해 크게 억제되었다. 치환기가 있는 카르보닐 화합물의 선택적 환원반응은 의약품 제조 분야에서 매우 중요한 반응이며 미생물에서 정제한 알데히드 환원효소가 biocatalyst 로서 선택적 환원반응에 이용될 수 있으리라 사료된다.

An Approach for Lactulose Production Using the CotX-Mediated Spore-Displayed β-Galactosidase as a Biocatalyst

  • Wang, He;Yang, Ruijin;Hua, Xiao;Zhang, Wenbin;Zhao, Wei
    • Journal of Microbiology and Biotechnology
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    • 제26권7호
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    • pp.1267-1277
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    • 2016
  • Currently, enzymatic synthesis of lactulose, a synthetic prebiotic disaccharide, is commonly performed with glycosyl hydrolases. In this work, a new type of lactulose-producing biocatalyst was developed by displaying β-galactosidase from Bacillus stearothermophilus IAM11001 (Bs-β-Gal) on the surface of Bacillus subtilis 168 spores. Localization of β-Gal on the spore surface as a fusion to CotX was verified by western blot analysis, immunofluorescence microscopy, and flow cytometry. The optimum pH and temperature for the resulting spore-displayed β-Gal was 6.0 and 75℃, respectively. Under optimal conditions, it showed maximum activity of 0.42 U/mg spores (dry weight). Moreover, the spore-displayed CotX-β-Gal was employed as a whole cell biocatalyst to produce lactulose, yielding 8.8 g/l from 200 g/l lactose and 100 g/l fructose. Reusability tests showed that the spore-displayed CotX-β-Gal retained around 30.3% of its initial activity after eight successive conversion cycles. These results suggest that the CotX-mediated spore-displayed β-Gal may provide a promising strategy for lactulose production.

Cofactor Regeneration Using Permeabilized Escherichia coli Expressing NAD(P)+-Dependent Glycerol-3-Phosphate Dehydrogenase

  • Rho, Ho Sik;Choi, Kyungoh
    • Journal of Microbiology and Biotechnology
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    • 제28권8호
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    • pp.1346-1351
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    • 2018
  • Oxidoreductases are effective biocatalysts, but their practical use is limited by the need for large quantities of NAD(P)H. In this study, a whole-cell biocatalyst for NAD(P)H cofactor regeneration was developed using the economical substrate glycerol. This cofactor regeneration system employs permeabilized Escherichia coli cells in which the glpD and gldA genes were deleted and the gpsA gene, which encodes $NAD(P)^+-dependent$ glycerol-3-phosphate dehydrogenase, was overexpressed. These manipulations were applied to block a side reaction (i.e., the conversion of glycerol to dihydroxyacetone) and to switch the glpD-encoding enzyme reaction to a gpsA-encoding enzyme reaction that generates both NADH and NADPH. We demonstrated the performance of the cofactor regeneration system using a lactate dehydrogenase reaction as a coupling reaction model. The developed biocatalyst involves an economical substrate, bifunctional regeneration of NAD(P)H, and simple reaction conditions as well as a stable environment for enzymes, and is thus applicable to a variety of oxidoreductase reactions requiring NAD(P)H regeneration.

Alginate-enclosed Microspheres를 이용한 배당체 합성에 관한 연구 (A Study on Glycoside Synthesis Using Alginate-enclosed Microspheres)

  • 김해성;김우식
    • KSBB Journal
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    • 제8권4호
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    • pp.320-327
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    • 1993
  • 스티렌/아크렬 라텍스 폴리머를 폴리에릴렌이민으 로 표면처 리하여 얻은 PEI-microspheres는 그 표면 화학적 특성이 효소의 고정화에 적합하여 배당체의 합성반응에 서 필요로 하는 alginate-enclosed micro­s spheres biocatalyst를 제조할 수 있었고 라텍스 폴리머 표변에 형성된 폴리에틸렌이민 피막은 효소 부근에 친수성 분위기를 유지하여 높은 효소활성을 나 타내었을 뿐만 아니라, 생성된 배당체가 효소에 접 근하여 가수분해되는 반응을 억제하여 배당체의 수 율과 농도를 크게 증가시 켰으므로 alginate-en closed microspheres에 의한 배당체의 합성반응이 연속생산공정으로 연구개발 될 수 있다.

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고정화된 Bacillus Brevis에 의한 큐놀린 분해의 증가 (Enhanced Degradation of Quinoline by Immobilized Bacillus Brevis)

  • S., Balasubramaniyan;M., Swaminathan
    • 대한화학회지
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    • 제51권2호
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    • pp.154-159
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    • 2007
  • 유리 및 고정화된 Bacillus brevis에 의한 큐놀린의 분해를 조사하였다. 코코넛 껍질 탄소에 고정화된 Bacillus brevis에 의한 큐놀린 분해 속도는 폼조각에 고정화되었거나 유리된 미생물에 의한 속도보다 빠르다. 시료에 존재하는 큐놀린 100 ppm을 완전히 제거하기 위해서는 코코넛 껍질 탄소에 고정화된 Bacillus brevis로 만든 생촉매를 물속에서 20시간 유지시키면 되었다. 이 생촉매는 꽤 긴 보존기간과 적절한 재생력을 가지고 있었다.