Abstract
A lipase from Candida rugosa was covalently immobilized on the cellulose acetate (CA)-coated Fe2O3 nanoparticles for the biocatalysis applications. The characterization of the Fe2O3-CA particles before and after immobilization of lipase was studied. The biocatalyst was assayed for the glycerolysis of olive oil in solvent system. The effect of reaction time, temperature, molar ratio of glycerol to oil and amount of lipase on the glycerolysis reaction was investigated. Results showed that the high yield of monoglycerides (49.7 wt%) and diglycerides (17.4 wt%) was achieved at 40 °C temperature and 0.02 g of lipase with relatively low glycerol to oil molar ratio (2:1) within 4 h of reaction time. Kinetics of immobilized lipase followed Lineweaver–Burk model with lower K m and V max values when compared to the free lipase. The immobilized lipase showed higher activity, thermal stability and reusability compared to the free lipase.
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Singh, A.K., Mukhopadhyay, M. Enzymatic Synthesis of Mono- and Diglyceride Using Lipase From Candida rugosa Immobilized Onto Cellulose Acetate-Coated Fe2O3 Nanoparticles. Arab J Sci Eng 41, 2553–2561 (2016). https://doi.org/10.1007/s13369-016-2036-3
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DOI: https://doi.org/10.1007/s13369-016-2036-3