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Purification and characterization of alkylcatechol 2,3-dioxygenase from butylphenol degradation pathway of Pseudomonas putida MT4

Paper ID Volume ID Publish Year Pages File Format Full-Text
22482 43291 2007 6 PDF Available
Title
Purification and characterization of alkylcatechol 2,3-dioxygenase from butylphenol degradation pathway of Pseudomonas putida MT4
Abstract

Alkylcatechol 2,3-dioxygenase was purified from the cell extract of recombinant Escherichia coli JM109 harboring the alkylcatechol 2,3-dioxygenase gene (bupB) cloned from the butylphenol-degrading bacterium Pseudomonas putida MT4. The purified enzyme (BupB) showed relative meta-cleavage activities for the following catechols: catechol (100%), 4-methylcatechol (572%), 4-n-butylcatechol (185%), 4-n-hexylcatechol (53%), 4-n-heptylcatechol (45%), 4-n-nonylcatechol (10%), 4-tert-butylcatechol (0%), and 3-methylcatechol (33%). The kinetic parameters, namely, Km and Vmax, for catechol, 4-methylcatechol, and 4-n-butylcatechol, were 23.4, 8.4, and 6.5 μM and 25.8, 76.9, and 18.0 U mg−1, respectively. These results suggest that BupB has broad substrate specificity for 4-n-alkylcatechols.

Keywords
alkylcatechol 2,3-dioxygenase; butylphenol; molar extinction coefficient; kinetic parameters; Pseudomonas putidaA23O; alkylcatechol 2,3-dioxygenase; aa; amino acid; AC; alkylcatechol; AP; alkylphenol; BC; butylcatechol; C23O; catechol 2,3-dioxygenase; MC;
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Purification and characterization of alkylcatechol 2,3-dioxygenase from butylphenol degradation pathway of Pseudomonas putida MT4
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Bioscience and Bioengineering - Volume 104, Issue 4, October 2007, Pages 309–314
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