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Purification and characterization of fenitrothion hydrolase from Burkholderia sp. NF100

Paper ID Volume ID Publish Year Pages File Format Full-Text
22247 43263 2006 3 PDF Available
Title
Purification and characterization of fenitrothion hydrolase from Burkholderia sp. NF100
Abstract

The organophosphorus pesticide hydrolase was purified to homogeneity from Burkholderia sp. NF100 by detergent extraction of the cell membrane fraction, anion-exchange, chromatofocusing, and gel filtration chromatographies. The purified enzyme had a molecular mass of 55 kDa and a pI 5.8, and the hydrolase activity was strongly inhibited by EDTA, dithiothreitol (DTT), Hg2+ and 1,10-phenanthroline. The optimum pH and temperature for the enzyme activity were 8.0 and 40°C, respectively. The enzyme hydrolyzed five organophosphorus pesticides.

Keywords
fenitrothion; hydrolase; organophosphorus pesticides; Burkholderia
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Purification and characterization of fenitrothion hydrolase from Burkholderia sp. NF100
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Bioscience and Bioengineering - Volume 101, Issue 1, January 2006, Pages 80–82
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