Proteolytic enzymes like casease are essential biological catalysts, valued for their ability to break down complex proteins such as casein into smaller, more digestible molecules. Among these, casease a serine protease holds major industrial importance, particularly in the food, pharmaceutical, and environmental sectors, owing to its role in protein hydrolysis and nutrient release. In this study, we isolated, produced, and characterized casease from two bacterial species, Bacillus subtilis and Serratia marcescens, both known for efficient extracellular enzyme secretion. Enzyme activity was confirmed by the formation of clear zones on skim milk agar signifying successful casein degradation. Comparative profiling revealed distinct production dynamics. Bacillus subtilis generated casease early, peaking at 24 hours, while Serratia marcescens showed delayed but more intense activity, reaching its maximum at 48 hours. Characterization studies indicated that Serratia marcescens had higher overall proteolytic activity. The response of enzymes to chemical inhibitors like hydrogen peroxide and hydrochloric acid suggested structural and functional differences between the two. Both enzymes al
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