2004Huadong Li-Gong Daxue xuebaoRequires access

Study on the Kinetics of Immobilized Lipase

Zhiguo Li, Ou Ling, Qingxun Song, Wei Dong-zhi

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Abstract

Lipase (EC3.1.1.3) from Candida sp. was immobilized on chitosan by physical adsorption. In this article, different factors that influenced the immobilization were investigated, and the optimum conditions were ascertained. Comparative studies of pH, temperature and thermal stability between free lipase and immobilized lipase were conducted. As a result, the optimum pH(7.0) of the immobilized lipase was lower than that of the soluble lipase (8.0). The optimum reaction temperature shifted from 40(°C) for the free lipase to 50(°C) for the immobilized lipase. The patterns of thermal stability indicated that the immobilization process tends to stabilize the enzyme. Compared with the half-life(0.32 h) of the soluble free (lipase) at 50(°C), the half-life(0.96 h) of the immobilized lipase increased three times. The activity of immobilized lipase changed slightly after 3 months storage at 4(°C).

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What this paper is about

Lipase (EC3.1.1.3) from Candida sp. was immobilized on chitosan by physical adsorption. In this article, different factors that influenced the immobilization were investigated, and the optimum conditions were ascertained. Comparative studies of pH, temperature and thermal stability between free lipase and immobilized lipase were conducted. As a result, the optimum pH(7.0) of the immobilized lipase was lower than that of the soluble lipase (8.0). The optimum reaction temperature shifted from 40(°C) for the free lipase to 50(°C) for the immobilized lipase. The patterns of thermal stability indicated that the immobilization process tends to stabilize the enzyme. Compared with the half-life(0.32 h) of the soluble free (lipase) at 50(°C), the half-life(0.96 h) of the immobilized lipase increased three times. The activity of immobilized lipase changed slightly after 3 months storage at 4(°C).

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Available abstract

Lipase (EC3.1.1.3) from Candida sp. was immobilized on chitosan by physical adsorption. In this article, different factors that influenced the immobilization were investigated, and the optimum conditions were ascertained. Comparative studies of pH, temperature and thermal stability between free lipase and immobilized lipase were conducted. As a result, the optimum pH(7.0) of the immobilized lipase was lower than that of the soluble lipase (8.0). The optimum reaction temperature shifted from 40(°C) for the free lipase to 50(°C) for the immobilized lipase. The patterns of thermal stability indicated that the immobilization process tends to stabilize the enzyme. Compared with the half-life(0.32 h) of the soluble free (lipase) at 50(°C), the half-life(0.96 h) of the immobilized lipase increased three times. The activity of immobilized lipase changed slightly after 3 months storage at 4(°C).

Key concepts: Lipase, Immobilized enzyme, Chemistry, Chromatography, Adsorption, Thermal stability, Triacylglycerol lipase, Chitosan

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