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Updated: Feb 5, 2026

Defining Substrate Specificities for Lipase and Phospholipase Candidates
Published on: November 23, 2016
Screening, purification and characterization of lipase from Burkholderia pyrrocinia B1213
Jinlong Li1,2, Weijia Shen1,2, Guangsen Fan1,3
11Beijing Advanced Innovation Center for Food Nutrition and Human Health, Beijing Technology and Business University, Fucheng Road, Haidian District, Beijing, 100048 People's Republic of China.
Abstract:
A lipase producing strain B1213 isolated from soil was identified as Burkholderia pyrrocinia based on 16S rRNA gene and recA sequeence analysis, making this the first report on the presence of a lipase from B. pyrrocinia. 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. Mg2+, Al3+, Mn2+, and Fe3+ enhanced lipase activity at both 1 mM and 5 mM concentrations. p-NPP, a long-chain acyl group 4-NP ester, appeared to be a good substrate candidate.
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