Purification and Characterization of Cold-adapted Neutral Protease from Enterococcus faecalis RQ15

doi:10.7506/spkx1002-6630-201111049

Abstract

Abstract: The protease from Enterococcus faecalis RQ15 was characterized after purification with DEAE Sepharose Fast Flow and SuperdexTM 75. The molecular weight of the protease was determination by SDS-PAGE to be 32.4 kD. The optimal reaction temperature and pH of protease were 35-40 ℃ and 7.5, respectively. The protease was characterized to be a cold-adapted enzyme. It had more activity at 20-40 ℃ and a wide range of pH tolerance.The activity of the protease could be activated by Zn2+ but inhibited by Ag+, Hg2+ and EDTA-Na2 significantly. The Km and Vmax of the purified protease were 1.31 × 10-4 mol/L and 6.92×10-6 mol/(L ·s), respectively.

Key words: Enterococcus faecalis, cold-adapted acid protease, purification

CLC Number:

Q939.117

ZHU Wei-wei，LI Yang，ZHU Wan-qin，WANG Yan-hua，JI Bao-ying，SUN Cui-huan. Purification and Characterization of Cold-adapted Neutral Protease from Enterococcus faecalis RQ15[J]. FOOD SCIENCE, 2011, 32(11): 239-242.

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Purification and Characterization of Cold-adapted Neutral Protease from Enterococcus faecalis RQ15

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