Immobilization of horseradish peroxidase (HRP) on polyimide nanofibers blending with carbon nanotubes

被引:21
作者
Zhang, Teng [1 ,3 ]
Xu, Xiao-Ling [1 ,3 ]
Jin, Yi-Ning [2 ]
Wu, Jian [1 ]
Xu, Zhi-Kang [2 ]
机构
[1] Zhejiang Univ, Dept Chem, Hangzhou 310027, Zhejiang, Peoples R China
[2] Zhejiang Univ, Dept Polymer Sci & Engn, MOE Key Lab Macromol Synth & Functionalizat, Hangzhou 310027, Zhejiang, Peoples R China
[3] Zhejiang Univ, Cyrus Tang Ctr Sensor Mat & Applicat, Hangzhou 310027, Zhejiang, Peoples R China
基金
中国国家自然科学基金;
关键词
Enzyme immobilization; Horseradish peroxidase; Nanofibers; MWCNTs; Polyimide nanofibers; ELECTROSPUN POLYMER NANOFIBERS; ENZYME IMMOBILIZATION; POLY(ACRYLONITRILE-CO-MALEIC ACID); LIPASE IMMOBILIZATION; CATALYTIC-PROPERTIES; REACTIVE GROUPS; HIGH-STRENGTH; REDOX ENZYME; MEMBRANES; NANOPARTICLES;
D O I
10.1016/j.molcatb.2014.04.015
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Carbon nanotubes are widely applied in electronics, which offers great potential for enhancing the activity of redox enzyme. In this work, polyimide (PI) was blended with multiwalled carbon nanotubes (MWCNTs) and then electrospun into nanofibers for the immobilization of horseradish peroxidase (HRP), a redox enzyme. SEM and TEM were used to characterize the surface morphology of the PI/MWCNTs nanofibers and to analyze the protruding parts induced by the blending of MWCNT. The results indicate that, compared to the virgin PI nanofibers, the blending of MWCNTs increases the retention activity of immobilized HRP from 2.38% to 12.50%. Circular dichroism and UV-vis molecular absorption spectrometry were used to explore the interactions between HRP and MWCNTs. It seems that MWCNTs increase the enzyme activity by the facilitation of electron transfer among the catalytic intermediates "HRP I", "HRP II" and MWCNTs. (C) 2014 Elsevier B.V. All rights reserved.
引用
收藏
页码:56 / 62
页数:7
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