Esterification of Secondary Alcohols and Multi-hydroxyl Compounds by Candida antarctica Lipase B and Subtilisin
- 주제(키워드) secondary alcohols , esterification , CAL-B , subtilisin , esters
- 주제(기타) Biotechnology & Applied Microbiology
- 설명문(일반) [Cha, Hee-Jeong; Park, Jin-Byung] Ewha Womans Univ, Dept Food Sci & Engn, Seoul 03760, South Korea; [Park, Jin-Byung] Ewha Womans Univ, Inst Mol Microbiol & Biosyst Engn, Seoul 03760, South Korea; [Park, Seongsoon] Sungshin Womens Univ, Ctr NanoBio Appl Technol, Dept Chem, Seoul 01133, South Korea
- 등재 SCIE, SCOPUS, KCI등재
- 발행기관 KOREAN SOC BIOTECHNOLOGY & BIOENGINEERING
- 발행년도 2019
- URI http://www.dcollection.net/handler/ewha/000000160059
- 본문언어 영어
- Published As http://dx.doi.org/10.1007/s12257-018-0379-1
- 저작권 이화여자대학교 논문은 저작권에 의해 보호받습니다.
초록/요약
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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