期刊
TETRAHEDRON LETTERS
卷 54, 期 10, 页码 1185-1188出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.tetlet.2012.11.147
关键词
Enzymatic catalysis; Lipase; Resolution; Alcohol; Amine
资金
- National Research Foundation of Korea [2009-0074357, 2012R1A1A2006595]
- National Research Foundation of Korea [2009-0074357, 2012R1A1A2006595] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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.
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