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Current Topics in Catalysis   Volumes    Volume 10 
Abstract
Hydrolysis of allylglycidyl ether by marine fungus Trichoderma sp. Gc1 and the enzymatic resolution of allylchlorohydrin by Candida antarctica lipase type B
Mariana P. Martins, Ana M. Mouad, André L. M. Porto
Pages: 27 - 33
Number of pages: 7
Current Topics in Catalysis
Volume 10 

Copyright © 2012 Research Trends. All rights reserved

ABSTRACT
 
Enzymatic hydrolysis of (±)-2-((allyloxy)methyl) oxirane (1) using whole cells of the marine fungus Trichoderma sp. Gc1 that had been grown in artificial seawater produced (S)-(+)-2-(allyloxymethyl)oxirane (1) (34% ee) in 23% yield, together with (R)-(-)-3-(allyloxy)propane-1,2-diol (2) in 60% yield (10% ee). The fungal hydrolases exhibited selectivity with preference for oxirane (R)-1, while the concomitant formation of (R)-diol 2 indicated that the mechanism involved retention of configuration. The esterification of (±)-1-(allyloxy)-3-chloropropan-2-ol (4) by lipase type B from Candida antarctica  resulted in (R)-(+)-4 (72% ee) and 45% yield, and (S)-(+)-1-(allyloxy)-3-chloropropan-2-yl acetate (5) (77% ee) and 41% yield. The enzyme showed acceptable selectivity with an enantiomeric ratio (E) of 16 for the resolution of the chlorohydrin rac-4.
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