Purification and characterization of an antimicrobial chitinase extracellularly produced by Monascus purpureus CCRC31499 in a shrimp and crab shell powder medium

Monascus purpureus CCRC31499 produced an antimicrobial chitinase when it was grown in a medium containing shrimp and crab shell powder (SOSP) of marine wastes. An extracellular antimicrobial chitinase was purified from the culture supernatant to homology. The chitinase had a molecular weight of similar to81000 and a pl of 5.4. The optimal pH, optimum temperature, and pH stability of the chitinase were pH 7, 40 degreesC, and pH 6-8, respectively. The activity of the chitinase was activated by Fe2+ and strongly inhibited by Hg2+. The unique characteristics of the purified chitinase include high molecular weight, nearly neutral optimum pH, protease activity, and antimicrobial activity with bacteria and fungal phytopathogens. This is also the first report of isolation of a chitinase from a Monascus species.