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1000
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Abstract/Summary
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Candida rugosa lipase is a food-grade enzyme that is extensively utilized in the dairy processing industry for milk fat hydrolysis. The enzyme is mainly employed to modify the fatty acid chain length that results in the enhancement of flavors. The hydrolytic activities of C. rugosa lipase (fungal source) in its free and immobilized forms were investigated at different pH and temperature settings. The main objective of this study was to understand how different support materials (Celite-545, Sephadex G-25, and chitosan) and immobilization techniques alter lipase activity and stability. Our results indicated that hydrolytic activity increased significantly with immobilization on Celite-545. In general, immobilization resulted in considerable improvements in the stability of the enzyme with variations in pH and temperature. Immobilization on Celite-545 led to the highest catalytic efficiency. Remarkable improvements in the recovery and reusability of the immobilized lipases were noted. Comparatively, the acetone immobilization procedure resulted in higher activities than alcohol immobilization. In conclusion, the activity of C. rugosa lipase was enhanced most significantly when immobilized on Celite-545 using acetone as an adsorption solvent.
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