Conversion of waste cooking oil by rhodococcal lipase immobilized in gellan gum

Recently, the application of lipase enzyme as biocatalyst in the conversion of waste cooking oil (WCO) to free fatty acids and glycerol has been trending well. Therefore, the present study attempts to use WCO which is found in abundance in Malaysia as the substrate for halal microbial lipase conversion to glycerol which can be exploited in the food industry. The workability of free lipase for WCO conversion, however suffers severely due to potential denaturation of the enzyme and extended reaction time. Thus, this study embraced the immobilization method to encapsulate crude lipase extracted from Rhodococcus pyridinivorans strain UCC 0009 in gellan gum and calcium alginate, respectively and compared their ability for WCO conversion to free crude lipase. The gellan gum and calcium alginate-immobilized crude lipase evidently exhibited greater WCO conversion, demonstrating 2.18-fold and 1.61-fold enhanced lipase activity, respectively in comparison to free crude lipase. The repeated reuse of the gellan gum-immobilized crude lipase maintained reasonable lipase activity for 9 cycles, retaining an average 85 % WCO conversion for the first seven cycles and 67 % conversion in the subsequent batches. Thus, the immobilized halal lipase can be foreseen as a green substitute to chemical catalyst for WCO conversion which meets the worldwide demand for clean technologies.

Efficient media for high production of microbial lipase from Bacillus subtilis (BSK-L) using response surface methodology for enantiopure synthesis of drug molecules

Lipases are a multipurpose enzyme that holds a significant position in industrial applications due to its ability to catalyse a large number of reactions such as hydrolysis, esterification, interesterification, transesterification which makes it a potential candidate. It is also used for the separation of chiral drugs from the racemic mixture and this property of lipase is considered very important in pharmaceutical industries for the synthesis of enantiopure bioactive molecules. Assuming the tremendous importance of lipases, as stereoselective biocatalysts, in pharmaceuticals and various other commercial applications, industrial enzymologists have been forced to search for those microorganisms which are able to produce novel biocatalysts at reasonably high yield. In the present study microbial lipase was isolated from the water sample of pond at Katra, Jammu and Kashmir (India). This enzyme has shown wide specificity and higher enantioselectivity, which make it pharmaceutical important enzyme. To make it economical for industrial application, it was produced on cheap nutrient media using Response Surface Methodology and got maximum production. It was used for resolution of chiral drugs and the significant results obtained during the course of work shall have potential towards pharmaceutical industries.