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2,4-Dichlorophenol hydroxylase for chlorophenol removal: Substrate specificity and catalytic activity

Paper ID Volume ID Publish Year Pages File Format Full-Text
16898 42621 2016 8 PDF Available
Title
2,4-Dichlorophenol hydroxylase for chlorophenol removal: Substrate specificity and catalytic activity
Abstract

•Cold-active hydroxylase for high efficient chlorophenol removal.•Broad chlorophenol specificity and high enzymatic activity.•Propose a preliminary assumption on the CPs metabolic pathway.•The nomenclature of enzyme previously might be inappropriate.

Chlorophenols (CPs) are common environmental pollutants. As such, different treatments have been assessed to facilitate their removal. In this study, 2,4-dichlorophenol (2,4-DCP) hydroxylase was used to systematically investigate the activity and removal ability of 19CP congeners at 25 and 0 °C. Results demonstrated that 2,4-DCP hydroxylase exhibited a broad substrate specificity to CPs. The activities of 2,4-DCP hydroxylase against specific CP congeners, including 3-CP, 2,3,6-trichlorophenol, 2-CP, and 2,3-DCP, were higher than those against 2,4-DCP, which is the preferred substrate of previously reported 2,4-DCP hydroxylase. To verify whether cofactors are necessary to promote hydroxylase activity against CP congeners, we added FAD and found that the added FAD induced a 1.33-fold to 5.13-fold significant increase in hydroxylase activity against different CP congeners. The metabolic pathways of the CP degradation in the enzymatic hydroxylation step were preliminarily proposed on the basis of the analyses of the enzymatic activities against 19CP congeners. We found that the high activity and removal rate of 2,4-DCP hydroxylase against CPs at 0 °C enhance the low-temperature-adaptability of this enzyme to the CP congeners; as such, the proposed removal process may be applied to biochemical, bioremediation, and industrial processes, particularly in cold environments.

Graphical abstractThe hydroxylase exhibited broad substrate specificity for chlorophenols at both mild and cold temperatures which might make the enzymatic removal process more attractive for biochemical, bioremediation, and industrial processes.Figure optionsDownload full-size imageDownload as PowerPoint slide

Keywords
2,4-Dichlorophenol hydroxylase; Cold-active; Chlorophenols; Removal; Substrate specificity
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Publisher
Database: Elsevier - ScienceDirect
Journal: Enzyme and Microbial Technology - Volume 82, January 2016, Pages 74–81
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us