Abstract
An alkaline protease from Acetes chinensis was purified and characterized in this study. The steps of purification include ammonium sulfate precipitation, ion-exchange chromatography with Q-sepharose Fast Flow, gel filtration chromatography with S300 and the second ion-exchange chromatography with Q-sepharose Fast Flow. The protease was isolated and purified, which was present and active on protein substrates (azocasein and casein). The specific protease activity was 17.15 folds and the recovery was 4.67. The molecular weight of the protease was estimated at 23.2 kD by SDS-PAGE. With azocasein as the susbstrate, the optimal temperature was 55°C and the optimal pH value was 5.5. Ion Ca2+ could enhance the proteolytic activity of the protease, while Cu2+, EDTA and PMSF could inhibit its activity.
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Xu, J., Liu, X., Li, Z. et al. Purification and characterization of an alkaline protease from Acetes chinensis . J Ocean Univ. China 4, 257–261 (2005). https://doi.org/10.1007/s11802-005-0044-0
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DOI: https://doi.org/10.1007/s11802-005-0044-0