Earticle

초록

영어

Candida antarctica lipase B (CALB) is one of the most versatile hydolases used in industrial processes. Despite of its heat resistance, further thermostabilization of the CALB is desirable to catalyze effectively biotransformation operated at high temperature. In this study, remarkably improved thermostabilization of the CALB was achieved by simple R1 silaffin-mediated biosilicification rather than laborious protein engineering approach. The CALB was fused with the R1 silaffin peptide and the CALB-R1 fusion protein was expressed successfully in Pichia pastoris expression host. The CALB-R1 fusion protein was immobilized on a macroporous polyacrylate carrier through physical adsorption and then subsequently coated with tetramethyl orthosilicate (TMOS). After R1 silaffinmediated biosilicification, the thermostability of the immobilized CALB-R1 was improved successfully. The T50 60 of the biosilicificated and immobilized CALB-R1 was increased drastically from 45℃ to 72℃, which was 14℃ and 10℃ higher than that of immobilized CALB-R1 and commercial Novozym 435, respectively. The optimum pH condition for biosilicification was determined to be pH 5 by comparison of the T50 60 values at various pH values. This simple R1-mediated biosilicification method for CALB could be useful to improve the thermostability of industrial enzymes which are not easily stabilized through protein engineering.

키워드

저자

• Chanha JEON [ Department of Chemical Engineering, Kwangwoon University, Seoul, 139-701. ]
• Jeong Chan JOO [ Department of Chemical Engineering, Kwangwoon University, Seoul, 139-701. ]
• Yong Hwan KIM [ Department of Chemical Engineering, Kwangwoon University, Seoul, 139-701. ]

참고문헌

발행기관

간행물

표지보기 관심저널 등록

• 간행물명

  한국생물공학회 학술대회

• 간기

  반년간

• 수록기간

  1985~2013

• 십진분류

  KDC 476 DDC 576