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Catalysts 2016, 6(11), 166; doi:10.3390/catal6110166

Enhancing the Enzymatic Activity of a Heme-Dependent Peroxidase through Genetic Modification

Department of Biochemical Engineering, Beijing University of Chemical Technology, Beijing 100029, China
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Author to whom correspondence should be addressed.
Academic Editors: David D. Boehr and Keith Hohn
Received: 28 August 2016 / Revised: 14 October 2016 / Accepted: 18 October 2016 / Published: 27 October 2016
(This article belongs to the Special Issue Immobilized Enzymes: Strategies for Enzyme Stabilization)
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Abstract

A heme-dependent peroxidase (HDP) catalyzes the ortho-hydroxylation of l-tyrosine to l-3,4-dihydroxyphenylalanine (l-DOPA) in the presence of hydrogen peroxide. l-DOPA can be used for the treatment of Parkinson's disease. In this work, to improve the catalytic efficiency, the heme-dependent peroxidase has been genetically modified with an elastin-like polypeptide (ELP). bicinchoninic acid (BCA) assay demonstrated that HDP-ELP has a higher solubility in aqueous solutions than HDP. Circular dichroism (CD) spectra showed that HDP-ELP has a higher stability than HDP. Enzyme kinetics has been investigated over a range of substrate concentrations. It has been demonstrated that HDP-ELP exhibited a catalytic efficiency 2.4 times that of HDP. View Full-Text
Keywords: heme-dependent peroxidase; elastin-like polypeptide; hydrogen peroxide; solubility; stability heme-dependent peroxidase; elastin-like polypeptide; hydrogen peroxide; solubility; stability
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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Liu, W.; Li, R.; Liu, D.; Feng, W. Enhancing the Enzymatic Activity of a Heme-Dependent Peroxidase through Genetic Modification. Catalysts 2016, 6, 166.

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