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

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. Partic...

Full description

Bibliographic Details
Main Authors: Toledo, María Victoria, Llerena Suster, Carlos Rafael, Ferreira, María L., Collins, Sebastián E., Briand, Laura Estefanía
Format: Article in Journal/Newspaper
Language:Spanish
Published: 2017
Subjects:
Online Access:http://sedici.unlp.edu.ar/handle/10915/105708
https://pubs.rsc.org/en/content/articlelanding/2017/CY/C7CY00245A
Description
Summary: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. Centro de Investigación y Desarrollo en Ciencias Aplicadas Facultad de Ciencias Exactas