Immobilization of Lipase on Agarose Beads for Enzymatic Hydrolsis/Transesterification of Castor Oil.

Lipase was immobilized onto agarose beads and used for enzyme-catalyzed hydrolysis/transesterification of castor oil at room temperature without surfactants and salts. The immobilization yield was evaluated by reacting p-nitrophenyl butyrate and immobilized lipase. The reaction was performed in a 25 mL phosphate buffer medium (pH 7.0) and incubated for 2 hours. The absorbance of the formed p-nitrophenol was measured at 346 nm. The highest immobilization rate was obtained using 5.0 mg lipase with 2.5 mL glyoxal agarose beads. The reaction was performed in 25.0 mL sodium bicarbonate buffer pH 10 for 12 h. The hydrolysis/transesterification of castor oil was performed in phosphate buffer (pH 7) – ethanol medium. The main products were ricinoleic acid and ethyl ricinoleate. The highest hydrolysis/transesterification yield was 87% using 1.0 g castor oil and 2.5 mL of lipase immobilized agarose beads in the phosphate buffer (pH 7): ethanol (1: 9, V: V) at 72 hours. The reaction products were analyzed using a Fourier Transform Infrared spectrometer (FTIR) and Reversed-Phase High-Performance Liquid Chromatography (RP-HPLC). [ABSTRACT FROM AUTHOR]

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