Cloning, Expression and Characterization of a Monooxygenase P450BM3 from Bacillus megaterium ALA2

Ting Wang; Liang Liang Wang; Xun Li

doi:10.4028/www.scientific.net/AMR.518-523.5533

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HomeAdvanced Materials ResearchAdvanced Materials Research Vols. 518-523Cloning, Expression and Characterization of a...

Cloning, Expression and Characterization of a Monooxygenase P450BM3 from Bacillus megaterium ALA2

Abstract:

Cytochrome P450 monooxygenases are enzymes which are capable of oxidising saturated and unsaturated substrates. P450BM3 from Bacillus megaterium is one of this family. For the ﬁrst time, the cyp gene for coding P450BM3 from B. megaterium ALA2 has been cloned and expressed in Escherichia coli. The recombinant enzyme is 120 kDa, containing 1049 aa. The highest activity of purified enzyme is 14.8 U/mg towards palmitic acid by monitoring the NADPH oxidation. The optimal pH and temperature were 9.0 and 40°C. The enzyme has higher activity towards linoleic acid, and 2-Methyl-7-octadecene can also be catalyzed which is a precursor of displar.

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Advanced Materials Research (Volumes 518-523)

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5533-5538

DOI:

https://doi.org/10.4028/www.scientific.net/AMR.518-523.5533

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Online since:

May 2012

Authors:

Ting Wang, Liang Liang Wang, Xun Li

Keywords:

Bacillus Megaterium ALA2, Escherichia coli, Expression, P450BM3

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