Solvent as a competitive inhibitor for Candida antarctica lipase B
2007 (English)In: Biochimica et Biophysica Acta - Proteins and Proteomics, ISSN 1570-9639, E-ISSN 1878-1454, Vol. 1774, no 8, 1052-1057 p.Article in journal (Refereed) Published
In enzyme-catalyzed reactions, the choice of solvent often has a marked effect on the reaction outcome. In this paper, it is shown that solvent effects could be explained by the ability of the solvent to act as a competitive inhibitor to the substrate. Experimentally, the effect of six solvents, 2-pentanone, 3-pentanone, 2-methyl-2-pentanol, 3-methyl-3-pentanot, 2-methylpentane and 3-methylpentane, was studied in a solid/gas reactor. As a model reaction, the CALB-catalyzed transacylation between methyl propanoate and I -propanol, was studied. It was shown that both ketones inhibited the enzyme activity whereas the tertiary alcohols and the hydrocarbons did not. Alcohol inhibition constants, K-il were changed to "K-i", determined in presence of 2-pentanone, 3-pentanone, and 3-methyl-3-pentanol, confirmed the marked inhibitory character of the ketones and an absence of inhibition of 3-methyl-3-pentanol. The molecular modeling study was performed on three solvents, 2-pentanone, 2-methyl-2-pentanol and 2-methyl pentane. It showed a clear inhibitory effect for the ketone and the tertiary alcohol, but no effect for the hydrocarbon. No change in enzyme conformation was seen during the simulations. The study led to the conclusion that the effect of added organic component on lipase catalyzed transacylation could be explained by the competitive inhibitory character of solvents towards the first binding substrate methyl propanoate.
Place, publisher, year, edition, pages
2007. Vol. 1774, no 8, 1052-1057 p.
kinetics, organic solvent, molecular modeling, solid/gas biocatalysis, conformational change, solubility
IdentifiersURN: urn:nbn:se:kth:diva-14179DOI: 10.1016/j.bbapap.2007.05.013ISI: 000249149600012ScopusID: 2-s2.0-34547544566OAI: oai:DiVA.org:kth-14179DiVA: diva2:331462
QC 201007222010-07-222010-07-222010-07-22Bibliographically approved