Earticle

초록

영어

The elastin-like polypeptides (ELPs) are artificial polypeptides based on the amino acid sequence of elastin. ELPs have a distinctive thermal property which leads to reversible phase transition within a very narrow temperature. At a temperature below transition temperature (Tt), ELPs are highly soluble in aqueous solutions. However, upon a temperature shift to above Tt, ELPs become insoluble and form an aggregate of polypeptides. The epoxide hydrolases (EHs) catalyze the addition of water molecule to an epoxide to form the corresponding vicinal diol. A marine epoxide hydrolase from Mugil cephalus (McEH) has enantioselective hydrolysis activity toward (R)-enantiomer of racemic epoxide, resulting in the preparation of enantiopure (S)-enantiomer. McEH showed higher enantioselectivity and stability at lower temperature. In order to develop a novel EH biocatalyst system that catalyzes enantioselective hydrolysis reaction at low temperature and can be recycled by thermo-responsive reversible aggregation at high temperature, ELP-tagged McEH was developed. The recombinant McEH fused with elastin-like polypeptides was cloned and characterized at the molecular level.

키워드

저자

• A Leum KIM [ Department of Chemical Engineering, Kyung Hee University, Gyeonggi-do 446-701, Korea. ]
• Eun Yeol LEE [ Department of Chemical Engineering, Kyung Hee University, Gyeonggi-do 446-701, Korea. ]

참고문헌

발행기관

간행물

표지보기 관심저널 등록

• 간행물명

  한국생물공학회 학술대회

• 간기

  반년간

• 수록기간

  1985~2013

• 십진분류

  KDC 476 DDC 576