Optimization of biosynthesis parameters, partial purification and characterization of extracellular lipase from soil derived Streptomyces sp. Loyola Lipase-1

In this study, we have attempted to isolate and characterize the extracellular lipase from Streptomyces sp. Actinomycetes strains were isolated from the soil collected from the Vedanthangal bird sanctuary. Further, the isolated strains were subjected to lipase enzyme activity. Lipase activity was determined for isolated pure colonies by using peptone tween agar (PTA); enzyme activity were quantified by using olive oil hydrolysis method. After quantification, best strains for lipase activity was selected for media optimization, characterization and for free fatty acid analysis. Among the five strains, Loyola lipase-1 strain showed maximum inducible extracellular lipase activity (523.33 U/mL). The morphological and 16S rRNA gene sequence studies clearly revealed the organism belong to Streptomyces sp. and was named as Streptomyces sp. Loyola lipase-1 strain (JN863118). The maximum enzyme yield was ensured by optimizing production medium. Partially purified enzyme was characterized. The specific activity of the partially purified enzyme was 172.04 U/mg with 2.03 fold purification factor. Moreover, optimal lipolytic activity was standardized at pH 7.0 and 40 degrees C. Finally, the partially purified enzyme was further characterized using SDS-PAGE analysis. This study, revealed the increased lipolytic potential of Loyola lipase-1 strain. This can be successfully utilised in industrial applications.