Biotechnology and Bioprocess Engineering

, Volume 24, Issue 1, pp 41–47 | Cite as

Esterification of Secondary Alcohols and Multi-hydroxyl Compounds by Candida antarctica Lipase B and Subtilisin

  • Hee-Jeong Cha
  • Jin-Byung ParkEmail author
  • Seongsoon ParkEmail author
Review Paper


Enzyme-catalyzed esterification of secondary alcohols and multi-hydroxyl compounds is one of the most valuable reactions in organic synthesis. However, it is often difficult to achieve high reaction rates and high regio-selectivities with commonly used enzymes such as lipases and proteases. One of the reasons may include bulky substituents of the secondary alcohols and multi-hydroxyl compounds (e.g., carbohydrates and flavonoids). The stereospecificity pocket of lipases, which is considered as a pocket for the binding of medium substituent, might not accept a large substituent due to steric hindrance. Thereby, this review has focused on the discussion about literature survey and structural feature of the most commonly used lipase (i.e., Candida antarctica lipase B (CAL-B)) and serine-protease (i.e., subtilisin) for acylation of secondary alcohols and complex molecules.


secondary alcohols esterification CAL-B subtilisin esters 


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Copyright information

© The Korean Society for Biotechnology and Bioengineering and Springer 2019

Authors and Affiliations

  1. 1.Department of Food Science & EngineeringEwha Womans UniversitySeoulKorea
  2. 2.Institute of Molecular Microbiology and Biosystems EngineeringEwha Womans UniversitySeoulKorea
  3. 3.Department of Chemistry, Center for NanoBio Applied TechnologySungshin Women’s UniversitySeoulKorea

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