Purification and properties of pendimethalin nitroreductase from Bacillus circulans

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• 作者：V. S. More ; P. N. Tallur ; H. Z. Ninnekar…
• 关键词：pendimethalin ; pendimethalin nitroreductase ; Bacillus circulans
• 刊名：Applied Biochemistry and Microbiology
• 出版年：2015
• 出版时间：May 2015
• 年：2015
• 卷：51
• 期：3
• 页码：329-335
• 全文大小：284 KB
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• 作者单位：V. S. More (1)
  P. N. Tallur (2)
  H. Z. Ninnekar (3)
  F. N. Niyonzima (4)
  S. S. More (5)
  
  1. Department of Biochemistry, MSRCASC, Mattikere, MSRIT Post, Bangalore, 560054, India
  2. Department of Chemistry, Government Arts and Science College, Karwar, 581301, India
  3. Department of Biochemistry, Karnataka University, Dharwad, 58003, India
  4. Department of Biology-Chemistry, CE, University of Rwanda, Kigali, 5039, Rwanda
  5. Department of Biochemistry, CPGS, Jain University, Bangalore, 560011, India
  
• 刊物类别：Biomedical and Life Sciences
• 刊物主题：Life Sciences
  Biochemistry
  Microbiology
  Medical Microbiology
  Russian Library of Science
  
• 出版者：MAIK Nauka/Interperiodica distributed exclusively by Springer Science+Business Media LLC.
• ISSN：1608-3024

文摘

A pendimethalin nitroreductase was purified from Bacillus circulans to 52-fold increase with a recovery of 21.1% and had a specific activity of 4.16 U/mg. The molecular weight was 27 kDa. The optimum pH and temperature were 7.5 and 35°C, respectively. Fe2+, Ca2+, Mg2+ and Mn2+ did not cause any effect on the enzyme activity, whereas Ag+, Hg2+ significantly inhibited it. The pendimethalin nitroreductase from B. circulans required NADPH as cofactor. It was not affected by GSH, DTT, L-Cys and β-mercaptoethanol but inhibited by p-hydroxymercuribenzoate, N-ethylmaleimide, and iodoacetamide. EDTA, 1,10-phenanthroline and α,α-dipyridyl had a moderate effect on the enzyme activity. The nitroreductase reduced all the tested nitroaromatic compounds but was more active towards pendimethalin and trifluralin. The K_M and V_max for the enzyme reaction using pendimethalin as a substrate were 4.35 μM and 620 μmoles mg? min?, respectively. The broad substrate specificity towards dinitroaniline herbicides suggested the enzyme to be used as a potent reducing agent of these toxic compounds. This is the first report for the purification and characterization of pendimethalin nitroreductase from any bacterial or fungal species.