Abstract
This study was focused on partial purification and characterization of lipase from Streptomyces acrimyciniNGP 1, isolated from marine sediment of south Indian coastal region. In purification steps, 4.53 fold purification was achieved after 85% ammonium sulphate precipitation with 0.97 percent recovery. In further purification steps, 1.33 fold purification was achieved by Sephadex G-100 chromatography with 1.61 percent of recovery. The specific activity of purified enzyme was 1525 U/mg. Zymogram of crude enzyme on native-PAGE presented bands with lipase activity of molecular weight and Isoelectric point were 50 kDa and 7.4 respectively. These features render this lipase of interest as a biocatalyst for applications such as biodiesel production and detergent formulations.
Highlights
Lipases are serine hydrolases characterized as triacylglycerol acylhydrolases (E.C. 3.1.1.3) and ought to be separated from esterases (E.C. 3.1.1.1) by the idea of their substrate
Lipases extracted from animal pancreas are rarely pure enough to be used in the food industry (Sharma and Kanwar, 2014). Because of their capacity to utilize fat as the main carbon source, microorganisms delivering lipases have been separated from nourishment waste, where they are answerable for the enhance change of dairy items, for example, cheddar, or from slick situations (Li et al, 2014)
Screening and Identification The actinomycetes growth occured on the starch casein Agar (SCA) plate was subjected for Lipase screening in the Rhodomine B agar medium and it produced maximum enzyme of about 40 U/ml
Summary
Lipases are serine hydrolases characterized as triacylglycerol acylhydrolases (E.C. 3.1.1.3) and ought to be separated from esterases (E.C. 3.1.1.1) by the idea of their substrate. A criteria used to recognize these two kinds of catalysts, i.e., actuation by the nearness of an interface, called "interfacial initiation," was discovered unacceptable for the arrangement of such proteins as a few lipases didn't show such marvel. Lipases extracted from animal pancreas are rarely pure enough to be used in the food industry (Sharma and Kanwar, 2014). Because of their capacity to utilize fat as the main carbon source, microorganisms delivering lipases have been separated from nourishment waste, where they are answerable for the enhance change of dairy items, for example, cheddar, or from slick situations (sewage, waste dump locales, and oil plant emanating) (Li et al, 2014). Partial purification and characterization of the partially purified enzyme were investigated and these parameters are necessary to use the enzyme efficiently in an industrial application
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