Detection of protease activity in peeI,stem and leaf of Musa paradisiaca extracts by agar plate technique and physicochemical property of meat

Protease is group of enzymes that can catalyze the hydrolization of peptide bonds of protein and break it down into polypeptide and amino acids. Protease can be detected through its proteolytic activity by using skim milk agar. it also can cause physicochemical changes to meat which can be used to determine it proteolytic activity. There were three parts of M. paradisiaca used in this study which are peel. stem and leaf. The parts of M. paradisiaca were extracted by using distilled water which then tested on skim milk agar plate to detect the proteolytic activity of each sample by using disc paper technique. The clear zone was observed around the disc after the plates were incubated for 12 and 24 hours. The proteolytic activity was also determined by treating the beef with the sample extracted to test its physicochemical property based on water holding capacity and pH. One way ANOVA and Duncan test was chosen to test whether there is significant difference between clear zone changes in skim milk agar plate for 12 hours and 24
hours. There were significant differences (p<0.05) in total proteolytic activity in skim milk agar plate method which showed proteolytic activity of leaf of M. paradisiaca is most active and obtained most significant differences compared to others extracted protease for 12 hours while peel of M. paradisiaca is most active and obtained most significant differences compared to others extracted protease for 24 hours. For the test towards
meat quality assessment, meat sample treated with protease from extracted stem of M. paradisiaca extract obtained lower WHC percentage which is 3.00% and pH 5.42 thus making the meat to become less available for water holding and increase protein denaturation. Extracted protease from stem of M. paradisiaca has higher potential for meat tenderization thus, increasing the meat tenderness.