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

• Published in: Catalysts
• Main Authors: Jakub Zdarta, Lukasz Klapiszewski, Artur Jedrzak, Marek Nowicki, Dariusz Moszynski, Teofil Jesionowski
• Format: Article in Journal/Newspaper
• Language: English
• Published: MDPI AG 2016
• Subjects: silica-lignin matrix; lipase; immobilized enzymes; enzyme activity and stability; Chemical technology; TP1-1185; Chemistry; QD1-999; Antarc*; Antarctica
• Online Access: https://doi.org/10.3390/catal7010014; https://doaj.org/article/09dfd68236a54ed1ae652280d6f54dd8

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.