Detection of protease activity in carica papaya, artocarpus heterophyllus and Manilkara zapota 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 down it into polypetide and amino acids. Protease can be detected by it proteolytic activity which can be detected by using skim milk agar and gelatin agar. It also can cause physicochemical changes to meat which can be used to determine it proteolytic activity. There were three types of fruits peels used in this study which are Carica papaya, Artocarpus heterophyllus and Manilkara zapota. The peels was extracted by using 2 types of solution which is sodium acetate buffer and distilled water which then tested on skim milk agar plate and gelatin agar plate to detect the proteolytic activity of each sample. The clear zone was observed after the plates were incubated for 12 and 24 hours. The clear zone formed on the plates indicates the proteolytic activity. The determination of proteolytic activity was also determined by treating the with beef with the peels extract to test its physicochemical property based on water holding capacity and pH test. Gelatin agar plate showed higher proteolytic activity compared to milk agar plate during 12 and 24 hours incubation. The extraction using sodium acetate buffer solution showed slightly higher proteolytic activity compared to distilled water extraction. Extraction of both solutions shows that C.papaya has the highest proteolytic activity followed by M.zapota and then A.heterophyllus. Extract with sodium acetate buffer has slightly lower in pH value. It was observed that C. papaya has the highest proteolytic activity, followed by M.zapota then A. heterophyllus extract.