The screening was carried out to find strains in Monascus fungus that would produce a high activity of acid proteinase. Monascus sp. No. 3404 was found to have the highest activity of the enzyme, which was formed by addition of defatted soybean meal to the medium.The enzyme was purified to homogeneity from the culture broth of this organism grown on defatted soybean meal. The molecular weight of the purified enzyme was determined to be 43000 by gel filtration method and 46000 by SDS-polyacryl amide gel electrophoresis method. The optimum pH was 3.2 and the optimum temperature was 50°C. The enzyme was active on human hemoglobin, milk casein and bovine serum albumin, and Km values for them were calculated to be 0.80, 1.45 and 1.80mg/ml, respectively. The enzyme was markedly inhibited by pepstatin A and chymostatin, and Ki values for them were calculated to be 28nM and 0.13mM, respectively.
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Yasuda et al. (1991) studied this question.