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Molecular recognition of an acyl–enzyme intermediate on the lipase B from Candida antarctica

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Abstract

This investigation provides evidence of the acyl enzyme species involved in the interaction of R/S-ketoprofen with the lipase B from Candida antarctica. The interaction between the profen and the enzyme was studied by in situ time-resolved ATR-FTIR under both static and transient conditions. Particularly, modulation excitation spectroscopy (MES) with phase sensitive detection (PSD) allowed us to univocally distinguish the signals belonging to the interaction between ketoprofen and the enzyme from the strong background signals. These experimental tools coupled with theoretical DFT analysis allowed us to propose various species derived from the interaction of ketoprofen with serine through H bonding (without reaction) and the acyl enzyme species (ester bond formation) which are the intermediates in the biocatalytic assisted esterification and hydrolysis using lipases.

Graphical abstract: Molecular recognition of an acyl–enzyme intermediate on the lipase B from Candida antarctica

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Publication details

The article was received on 09 Feb 2017, accepted on 24 Mar 2017 and first published on 28 Mar 2017


Article type: Paper
DOI: 10.1039/C7CY00245A
Citation: Catal. Sci. Technol., 2017, Advance Article
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    Molecular recognition of an acyl–enzyme intermediate on the lipase B from Candida antarctica

    M. V. Toledo, C. R. Llerena Suster, M. L. Ferreira, S. E. Collins and L. E. Briand, Catal. Sci. Technol., 2017, Advance Article , DOI: 10.1039/C7CY00245A

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