Abstract
Catalase of bovine milk was crystallized following n-butanol extraction, ammonium sulfate fractionation, ethanol-chloroform fractionation, diethyl-aminoethyl-Sephacel column chromatography, and Sephacryl S-300 gel filtration. About 120mg crystalline catalase was produced from 1200kg milk. The product was approximately 23,000 times as pure as milk.The crystalline catalase appeared homogeneous on disc-electrophoretic analysis. Its molecular weight was approximately 225,000 by Sephadex G-200 gel filtration. Optimum pH and temperature of the crystalline catalase were pH 8.0 and 20°C. The enzyme had a thermostable range below 40° C. Its absorption spectrum showed two bands, one at 275nm (protein) and the other from 360 to 450nm (Soret band, heme group). About 8% sodium chloride concentration reduced catalase activity by more than 6%.
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