@article{2981749, title = "Study of the removal of allyl esters by Candida antarctica lipase B (CAL-B) and pig liver esterase (PLE)", author = "Thodi, K. and Barbayianni, E. and Fotakopoulou, I. and Bornscheuer, U.T. and Constantinou-Kokotou, V. and Moutevelis-Minakakis, P. and Kokotos, G.", journal = "Journal of Molecular Catalysis B: Enzymatic", year = "2009", volume = "61", number = "3-4", pages = "241-246", issn = "1381-1177", doi = "10.1016/j.molcatb.2009.07.012", keywords = "Candida antarctica lipase B; Deprotection; Diesters; Ester groups; Ethyl esters; Monocarboxylic acids; Pig liver esterase; Protecting group, Amines; Amino acids; Carboxylic acids; Esterification; Esters; Fluorine containing polymers; Isomers; Liver; Organic acids, Enzymatic hydrolysis, allyl compound; amino acid; carboxylic acid; carboxylic acid derivative; ester derivative; esterase; glutamic acid; lipase B, article; Candida antarctica; controlled study; hydrolysis; synthesis, Candida antarctica; Suidae", abstract = "A number of allyl esters of various carboxylic acids and N-protected amino acids were synthesized and their hydrolysis by Candida antarctica lipase B and pig liver esterase was studied. In order to test the selectivity, the enzymatic hydrolysis of the corresponding methyl and ethyl esters was also examined. Both enzymes easily remove the allyl esters of monocarboxylates. The chemo- and regio-selectivity for the hydrolysis of glutamate diesters was studied, too, and it was found that the preference for the hydrolysis of a particular ester group depends not only on the ease of the hydrolysis observed for the esters of monocarboxylic acids, but also on the position (α- or γ-). © 2009 Elsevier B.V. All rights reserved." }