Bromelain Enzyme Analysis

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Bromelain is cystein protease or an enzyme mixture coming from pineapple. Although bromelain is found in every part of the pineapple, it's most plentiful in the stem. This enzyme has low but significant activity at 0°C, which dramatically increases at 50-70°C. The activity is sustained without a marked decrease up to 80°C. Bromelain is quite effective at dividing proteins such as the collagen in steak. Bromelain first degrades 40% of the collagen in the sarcolemma followed by degradation of myosin in the myofibrillar component. Bromelain separates all the important peptide bonds that link the proteins in collagen and the muscle tissue begins losing firmness. However, bromelain efficiently softens the steak for chewing, but leaves it firm enough to enjoy its taste. The enzymes are neutralized by heat of about 70°C, so bromelain stop …show more content…
Papain is mixture of enzymes obtained from the green papaya (pawpaw) fruit. Papain is a highly aggressive, indiscriminate enzyme causing significant degradation to both myofibrillar and collagen proteins. The optimal temperature range for papain is 65-80°C. Papain cuts the protein chains in the fibrils and also in the connective tissue, disrupting the structural integrity of the muscle fibre, and tenderizing the meat. Besides, ficin is also an enzyme used to tenderize the meat but it exhibits less activity against all types of proteins when compared to papain and bromelain. Ficin is a vegetable-based enzyme derived from figs. This thiol protease, although capable of minimal degradation of collagen and elastin, will preferentially degrade myofibrillar protein. Ficin is able to degrade elastin at temperatures as low as 20°C whereas it has little activity against collagen and myofibrillar proteins below 40°C. Optimal activity occurs between 60-70°C. The optimal pH for activity is near 7 for collagen and myofibrillar proteins and approximately 5.0-5.5 for elastin

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