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Heterologous expression of the methyl carbamate-degrading hydrolase MCD

Paper ID Volume ID Publish Year Pages File Format Full-Text
24441 43515 2009 7 PDF Available
Title
Heterologous expression of the methyl carbamate-degrading hydrolase MCD
Abstract

The methyl carbamate-degrading hydrolase (MCD) of Achromobacter WM111 has considerable potential as a pesticide bioremediation agent. However this potential has been unrealisable until now because of an inability to express MCD in heterologous hosts such as Escherichia coli. Herein, we describe the first successful attempt to express appreciable quantities of MCD in active form in E. coli, and the subsequent characterisation of the heterologously expressed material. We find that the properties of this material closely match the previously reported properties of MCD produced from Achromobacter WM111. This includes the presence of two distinct forms of the enzyme that we show are most likely due to the presence of two functional translational start sites. The purified enzyme catalyses the hydrolysis of a carbamate (carbaryl), a carboxyl ester (α-naphthyl acetate) and a phophotriester (dimethyl umbelliferyl phosphate) and it is relatively resistant to thermal and solvent-mediated denaturation. The robust nature and catalytic promiscuity of MCD suggest that it could be exploited for various biotechnological applications.

Keywords
Bioremediation; Insecticide; Catabolic enzyme; Promiscuous activity; Phosphotriestease; Evolution
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Heterologous expression of the methyl carbamate-degrading hydrolase MCD
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Biotechnology - Volume 144, Issue 2, 26 October 2009, Pages 89–95
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