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Reference type: Journal
Authors: Cao XW, Yang JK, Shu L, Yu BQ, Yan YJ
Article Title: Improving esterification activity of Burkholderia cepacia lipase encapsulated in silica by bioimprinting with substrate analogues.
Publication date: 2009
Journal: Process Biochemistry
Volume: 44
Issue: (2)
Page numbers: 177-182.
DOI: 10.1016/j.procbio.2008.10.003
Alternative URL: http://www.sciencedirect.com/science/article/B6THB-4TPF4J5-1/2/35cd08a51fb8a7f5ad8b24ac7075a6db

Abstract: Bioimprinting is a promising, though relatively unexplored, approach to improving the performance of enzymes. In this study, bioimprinting with substrate analogues of fatty acids was systematically conducted to improve the esterification activity of Burkholderia cepacia lipase that had undergone a sol-gel immobilization procedure with methyltrimethoxysilane (MTMS) and tetramethoxysilane (TMOS) as the precursors. The specific activity of the bioimprinted lipases was 3682.0μmolh-1mg protein, which was a 47.9- and 2.5-fold increase over the free and non-imprinted immobilized lipases, respectively. Compared to the free and non-imprinted immobilized lipases, bioimprinted lipases exhibited better thermal stability, and their activity did not change after being incubated at 60C for 12h. Bioimprinted lipases were more easily affected by alcohol than the non-imprinted ones, whose specific activity could be markedly enhanced by ethanol, isopropanol and n-butanol by factors of 1.23-, 1.28- and 1.12-fold, respectively. The reasons for the improvement of imprinted enzyme activity are also discussed based on the surface structure, specific surface area and average pore diameter of the silane particles
Author keywords: bioimprinting, lipase, Fatty acid, Silane, esterification, Scanning electron microscope (SEM)

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