Preparation of (S)-2-Phenylpropionic Acid by CaCl2/CMC Nanoparticles Immobilized Candida rugosa Lipase-Catalyzed Hydrolysis in Micro Aqueous Mixed Organic Solvent Systems

Candida rugosa lipase was immobilized in this study using CaCl2/CMC nanoparticles that yielded a lipase loading capacity of 127 mg/g, with better thermal stability and activity of 91.8%. The hydrolysis of racemic 2-phenylpropionic acid isopropyl ester by free and immobilized Candida rugosa lipase was investigated in the mixed organic-solvent composed of isooctane and methyl tert-butyl ether (9.5:0.5, V/V). The optimal conditions were 35 °C and pH 7.5 for free Candida rugosa lipase hydrolysis. We obtained (S)-2-phenylpropionic acid with 44.85% conversion, 95.75% enantiomeric excess and enantiomeric ratio of 112. The CaCl2/CMC nanoparticles immobilized Candida rugosa lipase possesses high enantioselectivity, with E = 237 at 40 °C and pH 7.5. It was efficiently reusable in four cycles and appropriately enhanced enantioselectivity within 120–240.

Investigating Enzyme Activity of Immobilized Candida rugosa Lipase

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.