Abstract:

The proteases from mucor is of relatively high hydrolysis efficiency to soy protein and of good debittering effect to the hydrolysates of protein. In order to effectively explore such proteases, one protease was purified from the fermented wheat bran by Actinomucor elegans AS3. 2778 using ion exchange chromatography, hydrophobic chromatography, and gel chromatography, and its hydrolysis properties to soybean protein were investigated. The results show that the purified protease is a single-chain polypeptide with a relative molecular mass of 32000, which has relatively higher hydrolysis activity to soy protein at 55 ℃ and pH8.0 - 10. 0 than such commercial proteases as papain, Alcalase and Protamex. It is thus concluded that, as compared with the above-mentioned commercial proteases, the purified protease is of more extensive peptide-bond selectivity, stronger affinity to soybean protein isolate （SPI）, and more cleavage points on SPI.

Key words: Actinomucor elegans, protease, purification, hydrolysis