ISOLATION AND CHARACTERIZATION OF PROTEASE FROM WISTERIA SINENSIS AND CHLORIS BARBATA

Enzymes, as biocatalysts, have extensive industrial applications. Protease enzymes, in particular, are widely used in industries such as leather, detergents, food, pharmaceuticals, and diagnostics. Alkaline proteases, which require a neutral to alkaline pH for activity, are notably sourced from plants. Objective: This study aimed to isolate and partially purify protease enzymes from the leaves of Wisteria sinensis and Chloris barbata, and to characterize their enzymatic properties, particularly their caseinolytic activity in alkaline conditions. Methods: Proteases were isolated and partially purified from the leaves of Wisteria sinensis and Chloris barbata. Enzyme kinetics were assessed to determine the optimal caseinolytic activity of the proteases. The study focused on evaluating the enzymes' stability at specific pH levels and temperatures. Statistical analysis was conducted to compare the enzymatic activities and to validate the findings. Results: The isolated proteases from both Wisteria sinensis and Chloris barbata demonstrated optimal caseinolytic activity in alkaline pH. The enzymes exhibited significant stability across specific pH levels and temperatures, confirming their alkaline nature. These findings highlight the potential industrial applications of these proteases. Conclusion: The study provides valuable insights into the isolation and characterization of proteases from Wisteria sinensis and Chloris barbata. The identified alkaline proteases show promise as industrial biocatalysts due to their stability and significant protease activity. Further research is warranted to purify these enzymes fully and explore their specific industrial applications, emphasizing the biotechnological potential of diverse plant sources.