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Catalysts 2016, 6(5), 66; doi:10.3390/catal6050066

Immobilization of Genetically-Modified d-Amino Acid Oxidase and Catalase on Carbon Nanotubes to Improve the Catalytic Efficiency

1
Department of Biochemical Engineering, Beijing University of Chemical Technology, Beijing 100029, China
2
Department of Chemical Engineering, Beijing University of Chemical Technology, Beijing 100029, China
*
Authors to whom correspondence should be addressed.
Academic Editor: David D. Boehr
Received: 24 March 2016 / Revised: 24 April 2016 / Accepted: 28 April 2016 / Published: 9 May 2016
(This article belongs to the Special Issue Enzyme Catalysis)
View Full-Text   |   Download PDF [4963 KB, uploaded 9 May 2016]   |  

Abstract

d-amino acid oxidase (DAAO) and catalase (CAT) have been genetically modified by fusing them to an elastin-like polypeptide (ELP). ELP-DAAO and ELP-CAT have been separately immobilized on multi-walled carbon nanotubes (MWNTs). It has been found that the secondary structures of the enzymes have been preserved. ELP-DAAO catalyzed the oxidative deamination of d-alanine, and H2O2 was evolved continuously. When the MWNT-supported enzymes were used together, the generated hydrogen peroxide of ELP-DAAO could be decomposed in situ. The catalytic efficiency of the two immobilized enzymes was more than five times greater than that of free ELP-DAAO when the ratio of immobilized ELP-CAT to immobilized ELP-DAAO was larger than 1:1. View Full-Text
Keywords: d-amino acids oxidase; catalase; elastin-like polypeptide; immobilization; carbon nanotubes d-amino acids oxidase; catalase; elastin-like polypeptide; immobilization; carbon nanotubes
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Li, R.; Sun, J.; Fu, Y.; Du, K.; Cai, M.; Ji, P.; Feng, W. Immobilization of Genetically-Modified d-Amino Acid Oxidase and Catalase on Carbon Nanotubes to Improve the Catalytic Efficiency. Catalysts 2016, 6, 66.

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