Purification and Properties of a Ribonuclease from a Species of the Genus Monascus

Abstract

Ribonuclease was purified to homogeneity from Monascus sp. No. 3403 by column chromatography on DEAE-cellulose, DEAE-Toyopearl 650S, 5'-AMP Sepharose 4B, and Sephadex G-75. The molecular weight of the purified enzyme was estimated to be 30, 000by gel filtration and 26, 000 by Sodium dodmlecyl sulfate poly-acrylamide gel electrophoresis. The enzyme contained 5.0% car-bohydrate. Homopolyadenylic acid was a good substrate for the enzyme. The optimum pH of the enzyme was 4.2 and its optimum temperature was 55°C.