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

Applied Biochemistry and Microbiology volume 48, pages 338–343 (2012)Cite this article

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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 and Affiliations

  1. Centre “Bioengineering”, Russian Academy of Sciences, Moscow, 117312, Russia

    V. M. Gumerov, A. V. Mardanov, P. M. Kolosov & N. V. Ravin

Authors
  1. V. M. Gumerov
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  2. A. V. Mardanov
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  3. P. M. Kolosov
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  4. N. V. Ravin
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Correspondence to N. V. Ravin.

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Original Russian Text © V.M. Gumerov, A.V. Mardanov, P.M. Kolosov, N.V. Ravin, 2012, published in Prikladnaya Biokhimiya i Mikrobiologiya, 2012, Vol. 48, No. 4, pp. 376–382.

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Gumerov, V.M., Mardanov, A.V., Kolosov, P.M. et al. Isolation and functional characterization of lipase from the thermophilic alkali-tolerant bacterium Thermosyntropha lipolytica . Appl Biochem Microbiol 48, 338–343 (2012). https://doi.org/10.1134/S0003683812040072

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  • DOI: https://doi.org/10.1134/S0003683812040072

Keywords

  • Lipase
  • Apply Biochemistry
  • Lipase Activity
  • Recombinant Lipase
  • Thermostable Lipase