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Fully Enzymatic Resolution of Chiral Amines: Acylation and Deacylation in the Presence of Candida antarctica Lipase B
Author(s) -
Ismail Hilda,
Lau Rute Madeira,
van Rantwijk Fred,
Sheldon Roger A.
Publication year - 2008
Publication title -
advanced synthesis and catalysis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.541
H-Index - 155
eISSN - 1615-4169
pISSN - 1615-4150
DOI - 10.1002/adsc.200800091
Subject(s) - candida antarctica , acylation , chemistry , lipase , hydrolysis , heteroatom , catalysis , kinetic resolution , reagent , organic chemistry , enzyme catalysis , enzyme , triacylglycerol lipase , enantioselective synthesis , stereochemistry , ring (chemistry)
A fully enzymatic methodology for the resolution of chiral amines has been demonstrated. Candida antarctica lipase B (CaLB)‐catalyzed acylation with N ‐methyl‐ and N ‐phenylglycine, as well as analogues having the general formula R 1 XCH 2 CO 2 R 2 (R 1 =Me, Ph; X=O, S) afforded the corresponding enantioenriched amides, which were subsequently enzymatically hydrolyzed. Surprisingly, CaLB also proved to be the catalyst of choice for this latter step. The heteroatom in the acyl donor profoundly influences both the enzymatic acylation and deacylation; the O‐substituted reagents performed best with regard to enantioselectivity as well as reaction rate in synthesis and hydrolysis.