Abstract:
Lipases are a class of enzymes that are widely used in various industrial applications due to their ability to hydrolyze ester bonds in lipids. They have attracted significant attention as a biocatalyst in various industries, including food, detergent, leather, and pharmaceuticals. Therefore, the discovery of novel lipases with improved properties is of great interest for industrial biotechnology. Lipase-producing bacterial isolates were obtained from Azad Jammu and Kashmir hot springs and identified as Bacillus toyonensis (TEHKF) and Bacillus thuringiensis (TCHO) based on 16SrRNA sequencing. The lipase enzyme was purified by sequential methods of ammonium sulfate precipitation and Sephadex G-75 gel filtration chromatography, resulting in a 58.6-fold purification with a final yield of 40.63%. SDS-PAGE analysis revealed a molecular weight of 41 kDa for the purified enzyme. The purified lipase exhibited maximal lipolytic activity at a temperature range of 40-90°C, with an optimal temperature of 70°C and an incubation time of 30 minutes for olive oil hydrolysis. Furthermore, lipase activity was stimulated by 100mM tris HCL buffer at pH 7.8 but strongly inhibited by 100mM acetate buffer. These findings suggest that lipases from these bacterial strains have potential industrial applications, and the purification method could be used for other enzymes with similar properties. Moreover, the purification and characterization of the lipases with improved properties and optimal conditions for activity provide a promising potential for industrial applications.
Page(s):
197-197
DOI:
DOI not available
Published:
Journal: Abstract Book on Second International Conference on Recent Approaches in Plant Sciences (RAPS-23) 4-5 May 2023 , Volume: 0, Issue: 0, Year: 2023
Keywords:
Lipase
,
purification
,
Molecular weight
,
SDSPAGE
,
lipolytic activity