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- W2372732014 abstract "A protease-producing clone(CAPRO2) was screened from metagenomic library of deep sea sediments using selective medium,and the characteristics of protease was studied.The results showed that the optimal temperature and pH for CAPRO2 protease activity were 65℃ and 9.0,respectively.The enzyme had excellent thermal stability.It was stable at temperature below 40℃,and retained about 60% of residual activity after 6 hours incubation at 50℃ and 30 minutes incubation at 60℃.The presence of Ca2+,Mg2+,Sr2+ and Co2+ increased the activity obviously,and Ca2+ enhanced the thermal stability distinctly.Three ions,Ca2+,Sr2+ and Co2+,increased the activity of the enzyme significantly at concentration of 3.0 mmol/dm3,and the activity-increasing effect was weak when the concentrations of these 3 ions were higher than 3.0 mmol/dm3.The ions Hg2+,Fe3+ and Cu2+ inhibited the enzyme activity notably.The CAPRO2 protease showed higher activity at pH 7.5 ~ 9.5,retaining 80% and 60% of residual activity at pH 7.5 and 9.5,respectively.The residual activity decreased rapidly at pH higher than 9.5 and reduced to about 15% at pH 10.0.It indicates that the enzyme belongs to alkaline protease.The serine protease inhibitors,PMSF,E-64 and AEBSF,showed no inhibition to the CAPRO2 enzyme activity,which indicates that the enzyme was not serine protease.On the other hand,EDTA inhibited the enzyme activity strongly,indicating that the enzyme belongs to metalloproteinase." @default.
- W2372732014 created "2016-06-24" @default.
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- W2372732014 date "2011-01-01" @default.
- W2372732014 modified "2023-09-26" @default.
- W2372732014 title "Screening and characterization of a protease-producing clone CAPRO2 from metagenomic library of deep sea sediments" @default.
- W2372732014 hasPublicationYear "2011" @default.
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