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Catalysts 2016, 6(11), 174; doi:10.3390/catal6110174

Adsorption and Activity of Lipase on Polyphosphazene-Modified Polypropylene Membrane Surface

1
MOE Key Laboratory of Macromolecular Synthesis and Functionalization, Department of Polymer Science and Engineering, Zhejiang University, Hangzhou 310027, China
2
The Key Laboratory of Industrial Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, Wuxi 214122, China
3
Techonology Department, Zhejiang Jinghuan Environmental Technology Co., Ltd., Jinhua 321000, China
*
Author to whom correspondence should be addressed.
Academic Editor: David D. Boehr
Received: 22 September 2016 / Revised: 26 October 2016 / Accepted: 27 October 2016 / Published: 8 November 2016
(This article belongs to the Special Issue Immobilized Enzymes: Strategies for Enzyme Stabilization)
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Abstract

In this work, poly(n-butylamino)(allylamino)phosphazene (PBAP) was synthesized and tethered on polypropylene microporous membrane (PPMM) with the aim of offering a biocompatible and, at the same time, moderately hydrophobic microenvironment to lipase for the first time. Lipase from Candida rugosa was used and the influence of membrane surface conditions on the activities of immobilized lipases was evaluated. Water contact angle measurement as well as field emission scanning electron microscopy were used to characterize the morphology of the modified membranes. The results showed an improvement in the adsorption capacity (26.0 mg/m2) and activity retention (68.2%) of the immobilized lipases on the PBAP-modified PPMM. Moreover, the lipases immobilized on the modified PPMM showed better thermal and pH stability. View Full-Text
Keywords: lipase; adsorption; membrane modification; polyphosphazene; activity lipase; adsorption; membrane modification; polyphosphazene; activity
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Chen, P.-C.; Qian, Y.-C.; Fang, F.; Zhu, X.-Y.; Huang, X.-J. Adsorption and Activity of Lipase on Polyphosphazene-Modified Polypropylene Membrane Surface. Catalysts 2016, 6, 174.

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