Earticle

초록

영어

The catalytic activity of oxygenase-based whole-cell biocatalysts are heavily influenced by substrate and product toxicity because of cell membrane permeabilizing effects and protein denaturating effects of lipophilic substrates and products. In this presentation, we will report a novel approach to increase stability of oxygenase-based whole-cell biocatalyst, a recombinant Escherichia coli expressing chnB the gene of cyclohexanone monooxygenase of Acinetobacter calcoaceticus NCIMB 9871. Oxygenation activity of the recombinant E. coli expressing chnB alone was rapidly decreased during biotransformation of cyclohexanone into ε-caprolactone. However, the catalytic activity was rather maintained when the genes encoding chaperones GroEL-ES, DnaKJ-GrpE or ClpB, IbpAB, DnaKJ-GrpE were coexpressed. The chaperoning proteins were assumed to assist protein folding to the native conformation and/or disaggregating unfolded proteins. Thus, we conclude that stability of oxygenase-based whole-cell biocatalysts can be enhanced via coexpression of the genes encoding chaperones.

키워드

저자

• Ji-Yeong YUN [ Dept. of Food Science & Engineering, Ewha Womans University, Seoul, 120-750. ]
• Ji-Min WOO [ Dept. of Food Science & Engineering, Ewha Womans University, Seoul, 120-750. ]
• Sun-Joo KUM [ Dept. of Food Science & Engineering, Ewha Womans University, Seoul, 120-750. ]
• Seon-Won KIM [ Division of Applied Life Science, Gyeongsang National University, Jinju, 660-701. ]
• Jin-Byung PARK [ Dept. of Food Science & Engineering, Ewha Womans University, Seoul, 120-750. ]

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간행물

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• 간행물명

  한국생물공학회 학술대회

• 간기

  반년간

• 수록기간

  1985~2013

• 십진분류

  KDC 476 DDC 576