Lipase production bacterial isolate was isolated from soil of service station and identified as PS3 by 16SrRNA with accession number |LN999829.1|. Lipase enzyme was purified by sequential methods of ammonium sulfate precipitation and Sephadex G-100 gel column chromatography. The molecular weight of purified enzyme was 31.40 kDa on SDS-PAGE. This purification procedure resulted in 2.90-fold purification of lipase with a 24.10% final yield. The purified lipase presented maximal hydrolytic activity at a temperature of 55 C, and pH of 7.0. Lipase activity was stimulated by Triton X-100 and SDS with Mg and Ca metals employ a positive effect and outlast its stable in organic solvent i.e. methanol and ethanol.

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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6296573PMC
http://dx.doi.org/10.1016/j.jgeb.2017.06.007DOI Listing

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