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

Hee Jeong Cha, Jin Byung Park, Seongsoon Park

Research output: Contribution to journalReview articlepeer-review

26 Scopus citations

Abstract

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.

Original languageEnglish
Pages (from-to)41-47
Number of pages7
JournalBiotechnology and Bioprocess Engineering
Volume24
Issue number1
DOIs
StatePublished - 1 Feb 2019

Bibliographical note

Funding Information:
This research was supported by the Basic Science Research Program through the National Research Foundation of Korea (NRF) funded by the Ministry of Science, ICT and future Planning (NRF-2017R1A2B4004330). This study was also supported by the Marine Biomaterials Research Center grant from the Marine Biotechnology Program funded by the Ministry of Oceans and Fisheries, Republic of Korea (No. D11013214H480000100).

Publisher Copyright:
© 2019, The Korean Society for Biotechnology and Bioengineering and Springer.

Keywords

  • CAL-B
  • esterification
  • esters
  • secondary alcohols
  • subtilisin

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