Effects of enzyme inhibitors on trypsin activity
Proteases can be classified by their sensitivity to various inhibitors. To confirm the nature of the purified protease, activities were measured in the presence of different enzyme inhibitors (Table 2). Trypsin from Z. ophiocephalus was strongly inhibited by the well-known trypsin inhibitor investigated, namely, SBTI (1 mg/ml) and by PMSF and benzamidine, serine proteaseinhibitors. On the other hand, the metalloprotease inhibitor (EDTA,5 mM) inhibited the enzyme by 59%. The relatively high activity of the trypsin in the presence of EDTA is very useful for application as detergent additive because chelating agents are components of most detergents. Chelating agents function as water softeners and also assist in the removal of stain. These agents specifically chelate metal ions making them unavailable in the detergent solution.
In addition, Pepstatin A, an aspartic protease inhibitor and DTNB, specific for thiol proteases, did not show any inhibitory effects against the purified trypsin. The inhibition results indicate that the purified enzyme is a serine-protease based on inhibition by PMSF and authentic trypsin based on its catalytic specificity for BAPNA and inhibition by SBTI.
Effects of enzyme inhibitors on trypsin activityProteases can be classified by their sensitivity to various inhibitors. To confirm the nature of the purified protease, activities were measured in the presence of different enzyme inhibitors (Table 2). Trypsin from Z. ophiocephalus was strongly inhibited by the well-known trypsin inhibitor investigated, namely, SBTI (1 mg/ml) and by PMSF and benzamidine, serine proteaseinhibitors. On the other hand, the metalloprotease inhibitor (EDTA,5 mM) inhibited the enzyme by 59%. The relatively high activity of the trypsin in the presence of EDTA is very useful for application as detergent additive because chelating agents are components of most detergents. Chelating agents function as water softeners and also assist in the removal of stain. These agents specifically chelate metal ions making them unavailable in the detergent solution.In addition, Pepstatin A, an aspartic protease inhibitor and DTNB, specific for thiol proteases, did not show any inhibitory effects against the purified trypsin. The inhibition results indicate that the purified enzyme is a serine-protease based on inhibition by PMSF and authentic trypsin based on its catalytic specificity for BAPNA and inhibition by SBTI.
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