Journal
BIOTECHNOLOGY AND BIOPROCESS ENGINEERING
Volume 24, Issue 1, Pages 41-47Publisher
KOREAN SOC BIOTECHNOLOGY & BIOENGINEERING
DOI: 10.1007/s12257-018-0379-1
Keywords
secondary alcohols; esterification; CAL-B; subtilisin; esters
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Funding
- National Research Foundation of Korea (NRF) - Ministry of Science, ICT and future Planning [NRF-2017R1A2B4004330]
- Marine Biomaterials Research Center grant from the Marine Biotechnology Program - Ministry of Oceans and Fisheries, Republic of Korea [D11013214H480000100]
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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.
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