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2010 (English)In: Journal of Molecular Catalysis B: Enzymatic, ISSN 1381-1177, E-ISSN 1873-3158, Vol. 65, no 1-4, p. 3-10Article in journal (Refereed) Published
Abstract [en]
A rational design approach was used to create the mutant Candida antarctica lipase B (CALB, also known as Pseudozyma antarctica lipase B) V190A having a k(cat) three times higher compared to that of the wild type (wt) enzyme for the transacylation of the industrially important compound methyl methacrylate. The enzymatic contribution to the transacylation of various acrylates and corresponding saturated esters was evaluated by comparing the reaction catalysed by CALB wt with the acid (H2SO4) catalysed reaction. The performances of CALB wt and mutants were compared to two other hydrolases, Humicola insolens cutinase and Rhizomucor mihei lipase. The low reaction rates of enzyme catalysed transacylation of acrylates were found to be caused mainly by electronic effects due to the double bond present in this class of molecules. The reduction in rate of enzyme catalysed transacylation of acrylates compared to that of the saturated ester methyl propionate was however less than what could be predicted from the energetic cost of breaking the pi-system of acrylates solely. The nature and concentration of the acyl acceptor was found to have a profound effect on the reaction rate. (C) 2009 Elsevier B.V. All rights reserved.
Keywords
Lipase, CALB, Point mutations, Kinetics, Proficiency
National Category
Biochemistry and Molecular Biology Biochemistry and Molecular Biology Physical Chemistry
Identifiers
urn:nbn:se:kth:diva-29688 (URN)10.1016/j.molcatb.2009.11.016 (DOI)000278926300002 ()2-s2.0-77952673518 (Scopus ID)
Note
QC 201102182011-02-182011-02-112024-03-18Bibliographically approved