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Stabilization of Candida antarctica lipase B in hydrophilic organic solvent by rational design of hydrogen bond

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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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Authors and Affiliations

  1. Graduate Program of Bioengineering, Seoul National University, Seoul, 151-742, Korea

    Hyun June Park & Young Je Yoo

  2. School of Chemical and Biological Engineering, Seoul National University, Seoul, 151-742, Korea

    Jeong Chan Joo & Young Je Yoo

  3. Department of Biological and Chemical Engineering, Hongik University, Chungnam, 339-701, Korea

    Kyungmoon Park

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  1. Hyun June Park
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  2. Jeong Chan Joo
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  3. Kyungmoon Park
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  4. Young Je Yoo
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Correspondence to Young Je Yoo.

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Park, H.J., Joo, J.C., Park, K. et al. Stabilization of Candida antarctica lipase B in hydrophilic organic solvent by rational design of hydrogen bond. Biotechnol Bioproc E 17, 722–728 (2012). https://doi.org/10.1007/s12257-012-0092-4

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  • DOI: https://doi.org/10.1007/s12257-012-0092-4

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