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http://dx.doi.org/10.5352/JLS.2016.26.5.603

Characterization of Organic Solvent Stable Lipase from Pseudomonas sp. BCNU 106  

Choi, Hye Jung (Department of Biology and Chemistry, Changwon National University)
Hwang, Min Jung (Department of Biology and Chemistry, Changwon National University)
Kim, Dong Wan (Department of BioHealth Science, Changwon National University)
Joo, Woo Hong (Department of Biology and Chemistry, Changwon National University)
Publication Information
Journal of Life Science / v.26, no.5, 2016 , pp. 603-607 More about this Journal
Abstract
A crude extracellular lipase from solvent-tolerant bacterium Pseudomonas sp. BCNU 106 was highly stable in the broad pH range of 4-10 and at temperature of 37℃. Crude lipase of BCNU 106 exhibited enhanced stability in 25% organic solvents such as xylene (121.85%), hexane (120.35%), octane (120.41 %), toluene (118.14%), chloroform (103.66%) and dodecane (102.94%) and showed excellent stability comparable with the commercial immobilized enzyme. In addition, the stability of BCNU 106 lipase retained above 110% of its enzyme activity in the presence of Cu2+, Hg2+, Zn2+ and Mn2+, whereas Fe2+ strongly inhibited its stability. The detergents including tween 80, triton X-100 and SDS were positive signals for lipase stability. Because of its stability in multiple organic solvents, cations and surfactants, the Pseudomonas sp. BCNU 106 lipase could be considered as a potential biocatalyst in the industrial chemical processes without using immobilization.
Keywords
Lipolytic stability; organic solvent stable lipase; organic solvent-tolerant; Pseudomonas sp.;
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