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Merck
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  • [Isolation and functional characterization of lipase from the thermophilic alkali-tolerant bacterium Thermosyntropha lipolytica].

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

Prikladnaia biokhimiia i mikrobiologiia (2012-10-06)
V M Gumerov, A V Mardanov, P M Kolosov, N V Ravin
摘要

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 degrees C and pH 8.0. Enzyme saved more than 80% of its activity in the presence of 10% methanol. 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.