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

被引：9
作者：
Chen, Peng-Cheng [2 ]
Qian, Yue-Cheng [1 ,3 ]
Fang, Fei [1 ]
Zhu, Xue-Yan [1 ]
Huang, Xiao-Jun [1 ]
机构：
[1] Zhejiang Univ, Dept Polymer Sci & Engn, MOE Key Lab Macromol Synth & Functionalizat, Hangzhou 310027, Zhejiang, Peoples R China
[2] Jiangnan Univ, Sch Biotechnol, Key Lab Ind Biotechnol, Minist Educ, Wuxi 214122, Peoples R China
[3] Zhejiang Jinghuan Environm Technol Co Ltd, Techonol Dept, Jinhua 321000, Peoples R China
来源：
CATALYSTS | 2016年 / 6卷 / 11期
基金：
中国国家自然科学基金;
关键词：
lipase; adsorption; membrane modification; polyphosphazene; activity; ENZYME IMMOBILIZATION; INTERFACIAL ACTIVATION; HYDROGEL; SUPPORTS;
D O I：
10.3390/catal6110174
中图分类号：
O64 [物理化学（理论化学）、化学物理学];
学科分类号：
070304 ; 081704 ;
摘要：
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/m(2)) 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.
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页数：10
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