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Open AccessArticle

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
Catalysts 2016, 6(11), 166; https://doi.org/10.3390/catal6110166
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)
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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MDPI and ACS Style

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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