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Catalysts 2016, 6(10), 149; doi:10.3390/catal6100149

Immobilized Aspergillus niger Lipase with SiO2 Nanoparticles in Sol-Gel Materials

1,†
,
1,†
,
2
and
1,2,*
1
Key Laboratory of Molecular Biophysics of the Ministry of Education, College of Life Science and Technology, Huazhong University of Science and Technology, Wuhan 430074, China
2
Shenzhen R & D Center of Huazhong University of Science and Technology, Shenzhen 518060, China
*
Author to whom correspondence should be addressed.
Academic Editor: David D. Boehr
Received: 9 June 2016 / Revised: 30 July 2016 / Accepted: 21 September 2016 / Published: 24 September 2016
(This article belongs to the Special Issue Immobilized Enzymes: Strategies for Enzyme Stabilization)
View Full-Text   |   Download PDF [2207 KB, uploaded 24 September 2016]   |  

Abstract

Lipase from Aspergillus niger was “doubly immobilized” with SiO2 nanoparticles in sol-gel powders prepared via the base-catalyzed polymerization of tetramethoxysilane (TMOS) and methyltreimethoxysilane (MTMS). The hydrolytic activity of the immobilized lipase was measured using the p-nitrophenyl palmitate hydrolysis method. The results showed that the optimum preparation conditions for the gels were made using a MTMS/TMOS molar ratio of 5, 60 mg of SiO2 nanoparticles, a water/silane molar ratio of 12, 120 mg of enzyme supply, and 120 μL of PEG400. Under the optimal conditions, the immobilized lipase retained 92% of the loading protein and 94% of the total enzyme activity. Characteristic tests indicated that the immobilized lipase exhibited much higher thermal and pH stability than its free form, which shows great potential for industrial applications. View Full-Text
Keywords: sol-gel; SiO2 nanoparticles; lipase; immobilization; stability sol-gel; SiO2 nanoparticles; lipase; immobilization; stability
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Xu, L.; Ke, C.; Huang, Y.; Yan, Y. Immobilized Aspergillus niger Lipase with SiO2 Nanoparticles in Sol-Gel Materials. Catalysts 2016, 6, 149.

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