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PLoS One. 2014 Jul 1;9(7):e101343. doi: 10.1371/journal.pone.0101343. eCollection 2014.

Purification and characterization of a cold-adapted lipase from Oceanobacillus strain PT-11.

Author information

1
Key laboratory of Leather Chemistry and engineering, College of Light Industry, Textile and Food Engineering, Sichuan University, Chengdu, China; Department of Pharmaceutical and Biological Engineering, College of Chemical Engineering, Sichuan University, Chengdu, Sichuan, China.
2
Department of Pharmaceutical and Biological Engineering, College of Chemical Engineering, Sichuan University, Chengdu, Sichuan, China.
3
Key laboratory of Leather Chemistry and engineering, College of Light Industry, Textile and Food Engineering, Sichuan University, Chengdu, China.

Abstract

We isolated a moderately halophilic lipase-producing bacterium from the saline soil. Based on the morphological, physiological, chemotaxonomic and phylogenetic analysis, the isolate PT-11 was postulated to be a novel species identified as Oceanobacillus rekensis PT-11. The lipase was purified 2.50-fold by Q-Sepharose FF and SP-Sepharose FF chromatography and its molecular mass was estimated to be 23.5 kDa by SDS-PAGE. It was highly active over the broad temperature ranging from 10 to 35°C and showed up to 80% of the maximum activity at 10°C indicating the lipase to be a typical cold-adapted enzyme. The enzyme activity was slightly enhanced by Na+, Li+ and K+. Incubation with detergents, such as Tween-20 and Tween-80, slightly inhibited the enzyme activity; while Triton X-100decreased the enzyme activity. The enzyme was fairly stable in the presence of long-chain alcohols but was highly denatured in hydrophilic solvents such as acetone or short-chain alcohols (C1-C3).

PMID:
24984141
PMCID:
PMC4077839
DOI:
10.1371/journal.pone.0101343
[Indexed for MEDLINE]
Free PMC Article
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