Purification and Study Enzymatic Properties of Acid Protease from Fermentation of Crayfish Shell with Monascus
Crayfish shell waste discharge causes environmental pollution and waste of resources.Monascus can convert and utilize shrimp shell proteins.In this paper,crayfish shells were used as the only nitrogen source,and Monascus fuliginosus BQ2 liquid fermentation induced the production of extracellular acid pro-tease.The acid protease was purified by ammonium sulfate and DEAE-Sepharose CL 6B anion exchange column.The enzyme activity was 29.10U/mL,purification ratio was 11.42,and molecular weight was 65 KDa.Its enzymatic properties were investigated.The results showed that the optimal pH value for the en-zyme activity was 4.0 and the optimal reaction temperature was 40℃.Pepstatin A strongly inhibited the enzyme activity and the enzyme belongs to the aspartic proteases.Cu2+and Ca2+inhibited the activity of the protease.Mg+,Zn 2+and Fe3+promoted the activity of the protease.
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