Purification, Crystallization, and Properties of Bovine Milk Catalase

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 produc...

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Bibliographic Details
Published in:Journal of dairy science 1983-01, Vol.66 (5), p.967-973
Main Authors: Ito, Osamu, Akuzawa, Ryozo
Format: Article
Language:English
Subjects:
catalase
cattle
milk
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Summary: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%.
ISSN:0022-0302
1525-3198
DOI:10.3168/jds.S0022-0302(83)81888-8