Abstract
Aqueous stem bark extract of Nothopegia beddomei was assayed for serine and aspartic protease inhibitors by using trypsin and pepsin as the target enzymes, respectively. Crude bark extract was dialyzed and subjected to inhibition assays. The thermal stabilities of serine and aspartic protease inhibitors were studied by incubating the extract at 4 oC, room temperature and 37 oC for a period of one month and subjecting to higher temperatures (55 oC, 75 oC and 95 oC) for 15 minutes. The crude bark extract of N. beddomei exhibited serine and aspartic protease inhibitory activities. However, the serine protease inhibitory activity was significantly higher. The approximate molecular mass of both serine and aspartic protease inhibitors were more than 8 kDa. Both types of inhibitors were identified as mixtures of thermally stable and labile compounds due to their variations in inhibitory activities with time at different temperatures. Attempts made to purify the protease inhibitors using ion exchange chromatography and ammonium sulphate precipitation were unsuccessful. In conclusion, the results indicate both serine and aspartic protease inhibition activities in N. beddomei bark extract are governed by mixtures of protenaceous and non-protenaceous molecules.
Highlights
Proteases are one of the most important groups of enzymes which involve in plethora of physiological and biochemical processes in all organisms
The optimized bark extract concentration, volume and pre incubation time for serine protease inhibitory assay procedure were 2.5%, 30 μl and 15 min heating of bark extract at higher temperatures was resulted a significant decrease in trypsin and pepsin inhibitory activities
N. beddomei can be considered as one of the important species belonging to the Family Anacardiaceae containing potent serine and aspartic protease inhibitors
Summary
Proteases are one of the most important groups of enzymes which involve in plethora of physiological and biochemical processes in all organisms. The key roles governed by proteases in living organisms are regulation of protein catabolism, regulation of protein – protein interactions, processing of cellular information and in generation, transduction and amplification of molecular signals. The function of proteases in living organisms is highly consequential. Regulation of protease activity is crucial in order to maintain the cellular homeostasis. PIs prevent the association of proteases with their substrates. These inhibitors process either reversible inhibition or irreversible inhibition. PIs are either proteins or non-protein compounds such as phenolics, alkaloids and terpenes and are classified based on type of protease they inhibit and the mode of inhibition (Mahajan and Badgujar, 2010)
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