Stabilization of Candida antarctica lipase B in hydrophilic organic solvent by rational design of hydrogen bond
- Authors
- Park, Hyun June; Joo, Jeong Chan; Park, Kyungmoon; Yoo, Young Je
- Issue Date
- Aug-2012
- Publisher
- KOREAN SOC BIOTECHNOLOGY & BIOENGINEERING
- Keywords
- organic solvent stability; hydrogen bond interaction; Candida antarctica lipase B; protein engineering
- Citation
- BIOTECHNOLOGY AND BIOPROCESS ENGINEERING, v.17, no.4, pp.722 - 728
- Journal Title
- BIOTECHNOLOGY AND BIOPROCESS ENGINEERING
- Volume
- 17
- Number
- 4
- Start Page
- 722
- End Page
- 728
- URI
- https://scholarworks.bwise.kr/hongik/handle/2020.sw.hongik/18919
- DOI
- 10.1007/s12257-012-0092-4
- ISSN
- 1226-8372
- Abstract
- Enzymatic reactions conducted in organic solvents have many advantages. However, organic solvent molecules may replace water molecules at the protein surface and penetrate into the enzyme, which could lead to the denaturation of the enzyme or changes in its reaction kinetics and substrate specificity. Thus, it is important to enhance the stability of enzymes in organic solvents. To date, there has been no efficient rational approach developed to enhance enzyme stability in hydrophilic solvents. We developed a rational approach to enzyme design. The design rules were established by investigating stable mutants from previous studies of directed evolution. Candida antarctica lipase B (CalB) was used as a target enzyme due to its versatile applications in organic solvents. The N97Q, N264Q, and D265E mutants of CalB showed higher organic solvent stability than the wild type.
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Collections - College of Science and Technology > Department of Biological and Chemical Engineering > 1. Journal Articles
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