Multiple forms of Rhizopus oligosporus protease
1970
Extracellular proteases of Rhizopus oligosporus have been purified and separated into five active fractions (A-E) by ammonium sulfate fractionation, gel filtration, or diethylaminoethyl cellulose chromatography. All fractions showed single bands on acrylamide gel electrophoresis. Preliminary characterization studies showed that the enzymes respond similarly to inhibitors and have the same pH stabilities. However, consistent differences in pH optima, temperature optima, and ratio of casein digestion to milk-clotting activity were found between two groups consisting of Fractions A, B, C and Fractions D, E. Crystalline enzymes were obtained from Fractions A and B.
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