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A new nitrilase from Bradyrhizobium japonicum USDA 110: Gene cloning, biochemical characterization and substrate specificity

Paper ID Volume ID Publish Year Pages File Format Full-Text
24808 43538 2008 7 PDF Available
Title
A new nitrilase from Bradyrhizobium japonicum USDA 110: Gene cloning, biochemical characterization and substrate specificity
Abstract

A nitrilase gene blr3397 from Bradyrhizobium japonicum USDA110 was cloned and over-expressed in Escherichia coli, and the encoded protein was purified to give a nitrilase with a single band of about 34.5 kD on SDS-PAGE. The molecular weight of the holoenzyme was about 340 kD as determined by light scattering analysis, suggesting that nitrilase blr3397 self-aggregated to an active form with the native structure being a decamer. The Vmax and Km for phenylacetonitrile were 3.15 U/mg and 4.36 mM, respectively. The catalytic constant kcat and specificity constant kcat/Km were 111 min−1 and 2.6 × 104 min−1 M−1. This nitrilase is most active toward the hydrolysis of hydrocinnamonitrile among the tested substrates (4.3 times that of phenylacetonitrile). The nitrilase blr3397 shows higher activity towards the hydrolysis of aliphatic nitriles than that for the aromatic counterparts, and can be characterized as an aliphatic nitrilase in terms of activity. This nitrilase also possesses distinct features from the nitrilase bll6402 of the same microbe.

Keywords
Nitrilase; Aliphatic nitrile; Hydrolysis; Bradyrhizobium japonicum
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A new nitrilase from Bradyrhizobium japonicum USDA 110: Gene cloning, biochemical characterization and substrate specificity
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Biotechnology - Volume 133, Issue 3, 1 February 2008, Pages 327–333
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