Candida antarctica lipase A and Pseudomonas stutzeri lipase as a pair of stereocomplementary enzymes for the resolution of 1,2-diarylethanols and 1,2-diarylethanamines

Candida antarctica lipase A (CALA) and Pseudomonas stutzeri lipase (PSL) displayed opposite enantioselectivities in the acylation of 1,2-diphenylethanol and 1,2-diphenylethanamine. CALA was (S)-selective while PSL was (R)-selective. In addition, fourteen different 1,2-diarylethanols were tested as t...

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Bibliographic Details
Published in:Tetrahedron Letters
Main Authors: Sol Kim, Yoon Kyung Choi, Jieun Hong, Park, J, KIM, MAHN JOO
Other Authors: 화학과, 10052207
Format: Article in Journal/Newspaper
Language:English
Published: Elsevier Ltd. 2013
Subjects:
DYNAMIC KINETIC RESOLUTION
ALCOHOL REACTS FASTER
ACTIVE-SITE MODEL
SECONDARY ALCOHOLS
ENANTIOSELECTIVE ACYLATION
RACEMIZATION CATALYSTS
ENANTIOMER
IDENTIFY
DERIVATIVES
HYDROLYSIS
Enzymatic catalysis
Lipase
Resolution
Alcohol
Amine
Antarc*
Antarctica
Online Access:https://oasis.postech.ac.kr/handle/2014.oak/15119
https://doi.org/10.1016/J.TETLET.2012.11.147
Description
Summary:Candida antarctica lipase A (CALA) and Pseudomonas stutzeri lipase (PSL) displayed opposite enantioselectivities in the acylation of 1,2-diphenylethanol and 1,2-diphenylethanamine. CALA was (S)-selective while PSL was (R)-selective. In addition, fourteen different 1,2-diarylethanols were tested as the substrates of CALA. It was found that most of them were accepted by CALA with high enantioselectivity. The DKR of five representative substrates by the combination of CALA and a ruthenium-based racemization catalyst provided good yields (82-91%) and acceptable enantiopurities (87-94% ee). (C) 2012 Elsevier Ltd. All rights reserved. X 1 1 16 14 scie scopus

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