抄録
Monascus purpureus CCRC31499 produced a protease when it was grown in a medium containing shrimp and crab shell powder (SCSP) of marine wastes. An extracellular protease was purified from the culture supernatant to homology. The protease had a molecular weight of 40,000 and a pI of 7.9. The optimal pH, optimum temperature, and pH stability of the protease were pH 9, 50°C, and pH 7-12, respectively. In addition to protease activity, CCRC 31499 also exhibited activity of enhancing vegetable growth in culture supernatant. This is also the first report of isolation of a protease from Monascus species.
