During chlorination, the enzyme get deactivated due to *
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Enzyme stability is greatly influenced by the presence of water (Klibanov, 1989; Zaks and Russel, 1988). For example, the stability of α-amylase dissolved in water is very poor especially in low concentration without buffer. Many researchers focus on the methods that can promote the stability of enzymes. Among various possible methods of enzyme stability enhancement, immobilization (Brodelius, 1978; Sadhukhan et al, 1990; Sadhukhan et al, 1993), addition of various compounds (Asther and Meunier, 1990; Kalibanov, 1983; Violet and Meunier, 1989; Ward and Moo-Young, 1988; Windish and Mhatre, 1965) and chemical modification (Fretheim et al, 1979; Tsuji, 1990) are frequently mentioned.
The enzyme α-amylase (1,4-α-D-glucanohydrolase, EC 3.2.1.1), widely used in the starch-to-fructose process, randomly hydrolyzes α-1,4 glucosidic linkages in polysaccharides into three or more α-1,4 linked D-glucose units to produce maltose or large oligo-saccharides (Boyce, 1986; Norman, 1981).
Supercritical fluids generally have similar density to liquids and similar viscosity to gases (Randolph, 1985). Thus, they are often recognized for their solvent power like liquids and diffusion capability in solids as gases. Among the supercritical fluids, supercritical carbon dioxide (abbreviated as SC-CO2 hereafter) is the most frequently mentioned for its mild condition. That is, the critical pressure and temperature of 1070 psi and 31.3°C, repectively, make it suitable for various applications in food industry. Therefore, SC-CO2 has attracted a great deal of attention for its use in the extraction of natural food substances (Taniguchi et al, 1985 and 1987). In this report, a novel application of SC-CO2 to enhance the stability of α-amylase is explored.
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