A lipase producing strain B1213 isolated from soil was identified as based on 16S rRNA gene and recA sequeence analysis, making this the first report on the presence of a lipase from . Under an aqueous two-phase purification strategy, which included (ATPE)-ion-exchange chromatography (IEC)-gel and filtration chromatography (GFC), the specific activity of the 35-kDa lipase was determined to be 875.7 U/mg protein. The optimum pH and temperature of this lipase was pH 8.0 and 50 °C, respectively. The lipase retained > 85% activity in isopropanol and acetone at 30 °C for 10 min but the activity was reduced to 10.6% in n-hexane. Mg, Al, Mn, and Fe enhanced lipase activity at both 1 mM and 5 mM concentrations. -NPP, a long-chain acyl group 4-NP ester, appeared to be a good substrate candidate.
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| http://dx.doi.org/10.1007/s13205-018-1414-9 | DOI Listing |
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