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Substrate-binding Site Engineering of Candida antarctica Lipase B to Improve Selectivity for Synthesis of 1-monoacyl-sn-glycerols
- Title
- Substrate-binding Site Engineering of Candida antarctica Lipase B to Improve Selectivity for Synthesis of 1-monoacyl-sn-glycerols
- Authors
- Woo J.-M.; Kang Y.-S.; Lee S.-M.; Park S.; Park J.-B.
- Ewha Authors
- 박진병; 우지민
- SCOPUS Author ID
- 박진병; 우지민
- Issue Date
- 2022
- Journal Title
- Biotechnology and Bioprocess Engineering
- ISSN
- 1226-8372
- Citation
- Biotechnology and Bioprocess Engineering vol. 27, no. 2, pp. 234 - 243
- Keywords
- Candida antarctica lipase B; glycerol; medium chain fatty acids; monoacyl glycerol
- Publisher
- Korean Society for Biotechnology and Bioengineering
- Indexed
- SCIE; SCOPUS; KCI
- Document Type
- Article
- Abstract
- Lipases are extensively used for regiospecific esterification of polyols with fatty acids. However, side reactions generating byproducts limited the enzymes for industrial applications. Here, we have engineered the substrate-binding site of Candida antarctica lipase B (CALB) to improve selectivity for monoacylation of glycerol using medium chain fatty acids (e.g., nonanoic acid) as acyl donors. The enzyme engineering was based on the substrate-binding region of a lipase from Penicillium camemberti (i.e., Lipase G), which showed very high selectivity for monoacylation of glycerol with medium chain fatty acids (e.g., decanoic acid) but low reaction rates. One of the CALB variants (e.g., CALBA282E/I285F), which was designed to have a narrow substrate binding region, has exhibited ca. 2-fold greater selectivity for the synthesis of 1-monoacyl-sn-glycerol with n-nonanoic acid. The double mutant allowed the production of 1-nonanoyl-glycerol to a concentration of 2.27 M in glycerol to a reaction rate of 1.0 M/h. This study will contribute to the use of lipases for regiospecific esterification of polyols with carboxylic acids. © 2022, The Korean Society for Biotechnology and Bioengineering and Springer.
- DOI
- 10.1007/s12257-021-0156-4
- Appears in Collections:
- 공과대학 > 식품생명공학과 > Journal papers
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