Screening, purification and characterization of lipase from Burkholderia pyrrocinia B1213
- 42 Downloads
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.
KeywordsB. pyrrocinia Lipase Screening Purification Characterization
This work was supported by the National Natural Science Foundation of China (Grant Numbers: 31501487, 31671798). We are grateful to Professor Madhav P. Yadav for his helpful promoting in the language quality of this article.
Compliance with ethical standards
Conflict of interest
On behalf of all authors, the corresponding author states that there is no conflict of interest.
- Thakur S (2012) Lipases, its sources, properties and applications: a review. Int J Sci Eng Res 3(7):1–29Google Scholar
- Velu N, Divakar K, Nandhinidevi G, Gautam P (2012) Lipase from Aeromonas caviae AU04: isolation, purification and protein aggregation. Biocatal Agric Biotechnol 1(1):45–50Google Scholar
- Verma N, Thakur S, Bhatt AK (2012) Microbial lipases: industrial applications and properties (a review). Int Res J Biol Sci 1(8):88–92Google Scholar