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Catalysts 2017, 7(1), 14; doi:10.3390/catal7010014

Lipase B from Candida antarctica Immobilized on a Silica-Lignin Matrix as a Stable and Reusable Biocatalytic System

1
Institute of Chemical Technology and Engineering, Faculty of Chemical Technology, Poznan University of Technology, Berdychowo 4, 60965 Poznan, Poland
2
Institute of Physics, Faculty of Technical Physics, Poznan University of Technology, Piotrowo 3, 60965 Poznan, Poland
3
Institute of Chemical and Environmental Engineering, Faculty of Chemical Technology and Engineering, West Pomeranian University of Technology, Pulaskiego 10, 70322 Szczecin, Poland
*
Author to whom correspondence should be addressed.
Academic Editor: David D. Boehr
Received: 24 November 2016 / Revised: 27 December 2016 / Accepted: 29 December 2016 / Published: 31 December 2016
(This article belongs to the Special Issue Immobilized Enzymes: Strategies for Enzyme Stabilization)
View Full-Text   |   Download PDF [3464 KB, uploaded 31 December 2016]   |  

Abstract

A study was conducted of the possible use of a silica-lignin hybrid as a novel support for the immobilization of lipase B from Candida antarctica. Results obtained by elemental analysis, Fourier transform infrared spectroscopy (FTIR), X-ray photoelectron spectroscopy (XPS), and atomic force microscopy (AFM), as well as the determination of changes in porous structure parameters, confirmed the effective immobilization of the enzyme on the surface of the composite matrix. Based on a hydrolysis reaction, a determination was made of the retention of activity of the immobilized lipase, found to be 92% of that of the native enzyme. Immobilization on a silica-lignin matrix produces systems with maximum activity at pH = 8 and at a temperature of 40 °C. The immobilized enzyme exhibited increased thermal and chemical stability and retained more than 80% of its activity after 20 reaction cycles. Moreover immobilized lipase exhibited over 80% of its activity at pH range 7–9 and temperature from 30 °C to 60 °C, while native Candida antarctica lipase B (CALB) exhibited the same only at pH = 7 and temperature of 30 °C. View Full-Text
Keywords: silica-lignin matrix; lipase; immobilized enzymes; enzyme activity and stability silica-lignin matrix; lipase; immobilized enzymes; enzyme activity and stability
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MDPI and ACS Style

Zdarta, J.; Klapiszewski, L.; Jedrzak, A.; Nowicki, M.; Moszynski, D.; Jesionowski, T. Lipase B from Candida antarctica Immobilized on a Silica-Lignin Matrix as a Stable and Reusable Biocatalytic System. Catalysts 2017, 7, 14.

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