PRODUCTION, UTILIZATION AND PARTIAL PURIFICATION OF PROTEINASE FROM BACTERIA ISOLATE ASSOCIATED WITH THE DEGRADATION OF COWPEA SEED COAT (VIGNA UNGUICULATA)

ABSTRACT Cowpea is a popular legume crop cultivated in tropical and subtropical regions, providing a significant protein source for human consumption that is commonly grown in Nigeria. The seed coat can be degraded by microorganisms to produce proteinase. The aim of this work is to produce, optimize and partially purify proteinase from bacteria isolate using cowpea seed coat The production, utilization, and partial purification of proteinase from cowpea seed coat was investigated to explore its potential applications in various industrial and biochemical processes. Cowpea seed coats, a readily available agricultural byproduct, were collected, cleaned, and processed to extract the enzyme. The proteinase was efficiently extracted using a phosphate buffer and its activity was measured through standard proteolytic assays. The result showed the highest crude proteinase activity (33.63±0.26 Ng/ml) at 30°C temperature for Bacillus pumibilis and the lowest activity at 70°C. The highest proteinase activity observed at pH 5.0 for Bacillus pumibilis and the lack of detectable activity at pH 2.0 across all three isolates can be explained by examining the relationship between pH, enzyme structure, and catalytic activity. Bacillus pumibilis produced the highest proteinase activity (162.24±0.44 Ng/ml) when cowpea seed coat was used as the carbon source. After partial purification, the highest Proteinase activity was (36.85±0.31)Ng/ml from Bacillus subtilis. The varied pH had significant effect (p