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Discovery of a mandelonitrile hydrolase from Bradyrhizobium japonicum USDA110 by rational genome mining

Paper ID Volume ID Publish Year Pages File Format Full-Text
25363 43570 2007 6 PDF Available
Title
Discovery of a mandelonitrile hydrolase from Bradyrhizobium japonicum USDA110 by rational genome mining
Abstract

A mandelonitrile hydrolase bll6402 from Bradyrhizobium japonicum USDA110 was predicted by rational genome mining, i.e. combining traditional genome mining with functional analysis of the genetic organization of the putative nitrilase gene within the chromosome of microorganisms. This putative gene was cloned and over-expressed in Escherichia coli, and the encoded protein was purified to give a nitrilase with a molecular mass of about 37 kDa. The molecular weight of the holoenzyme was about 455 kDa, suggesting that nitrilase bll6402 self-aggregated to the active form with native structure being 12 subunits of identical size. This nitrilase was most active toward mandelonitrile with Vmax and Km for mandelonitrile being 44.7 U/mg and 0.26 mM, respectively. The kcat and overall catalytic efficiency kcat/Km were 27.0 s−1 and 1.04 × 105 M−1 s−1, indicating that nitrilase bll6402 is very active for the hydrolysis of mandelonitrile to mandelic acid. Nitrilase bll6402 also effectively hydrolyzed several mandelonitrile derivatives.

Keywords
Nitrilase; Mandelonitrile; Rational genome mining; Bradyrhizobium japonicum
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Discovery of a mandelonitrile hydrolase from Bradyrhizobium japonicum USDA110 by rational genome mining
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Biotechnology - Volume 129, Issue 4, 10 May 2007, Pages 645–650
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