Isolation and functional characterization of lipase from the thermophilic alkali-tolerant bacterium Thermosyntropha lipolytica

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ID: 119371
2012
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Abstract
As a result of sequencing the genome of the termophilic alkali-tolerant lipolytic bacterium Thermosyntropha lipolytica, the gene encoding a lipase secreted into the medium was identified. The recombinant enzyme was expressed in Escherichia coli. It was isolated, purified, and functionally characterized. The lipase exhibited hydrolytic activity toward para-nitrophenyl esters of various chain lengths, as well as triglycerides, including vegetable oils. The optimal reaction conditions were achieved at temperatures from 70 to 80°C and pH 8.0. This new thermostable lipase may be a promising biocatalyst for organic synthesis; it may find application in the food and detergent industry and biodiesel production.
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Authors V. M. Gumerov;A. V. Mardanov;P. M. Kolosov;N. V. Ravin;V. M. Gumerov;A. V. Mardanov;P. M. Kolosov;N. V. Ravin;
Journal applied biochemistry and microbiology
Year 2012
DOI
doi:10.1134/S0003683812040072
URL
https://link.springer.com/article/10.1134/S0003683812040072
Keywords
Microbiology biochemistry medical microbiology general

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