Abstract
Purified wheat germ lipase has a specific activity of 12 ± 1 units, and the addition of urea decreases the activity of the enzyme. Partial specific volume of the enzyme in presence of 8 M urea is 0.723 and 0.717 mL/g for isomolal and isopotential measurements, respectively, and the preferential interaction parameter (ξ3) value is 0.05 g/g. Ultraviolet and fluorescence emission measurements indicated the exposure of aromatic amino acid residues from the interior of the protein, and thermal denaturation temperature (Tm) measurements indicated a decreased stability of the enzyme by 12 °C from a control value of 56 °C. The addition of specific cosolvents was found to increase the thermal stability of the enzyme to different extents (patent pending). The concentration of the cosolvent (10−40%) used has a direct effect on the retention of activity of the enzyme after being exposed to elevated temperatures in the presence of these cosolvents. Keywords: Wheat germ lipase; thermal stabilization; hydration; denatur...
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