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Highly efficient covalent immobilization of catalase on titanate nanotubes

Paper ID Volume ID Publish Year Pages File Format Full-Text
3185 156 2014 8 PDF Available
Title
Highly efficient covalent immobilization of catalase on titanate nanotubes
Abstract

•Titanate nanotubes (TNTs) were synthesized and used for enzyme immobilization.•Catalase was covalently immobilized on the TNTs surface in a facile way.•Immobilized catalase showed high loading capacity, catalytic activity and stability.

In this study, titanate nanotubes (TNTs) with desirable biocompatibility and hydrophilicity have been synthesized by a facile and cost-effective alkaline hydrothermal method, and used to immobilize the enzyme. The characterization results reveal that the prepared TNTs have a regular tubular morphology with a length about 100–180 nm and an outer diameter about 10 nm, and a BET specific surface area of 305.4 m2 g−1. Catalase (CAT), as the model enzyme, was pre-modified by 3-(3,4-dihydroxyphenyl) propionic acid (3,4-diHPP) via 1-ethyl-3-[3-dimethylaminopropyl] carbodiimide hydrochloride (EDC) and N-hydroxysuccinimide (NHS) coupling chemistry, and then covalently immobilized on the TNTs surface by the chelation of catechol groups with Ti4+ ions. It is found that TNTs exhibits excellent performances as the immobilized supporter of enzyme: the enzyme loading is as high as 820 mg g of support−1; the relative activity of immobilized enzyme is about 60% of that of free enzyme; the immobilized CAT demonstrates enhanced storage and recycling stability.

Keywords
Enzymes; Immobilization; Titanate nanotubes; Chelation; Enzyme technology; Biocatalysis
First Page Preview
Highly efficient covalent immobilization of catalase on titanate nanotubes
Publisher
Database: Elsevier - ScienceDirect
Journal: Biochemical Engineering Journal - Volume 83, 15 February 2014, Pages 8–15
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering