Physicochemical and sensory properties of carabeef treated with Bacillus subtilis (Ehrenberg) Cohn protease as meat tenderizer
2015
Bureros, KJ.C.
Proteases occur in all organisms, from prokaryotes to eukaryotes to viruses. These enzymes are involved in a multitude of physiological reactions from simple digestion of food proteins to highly regulated processes. This study investigated the use of Bacillus subtilis protease as a meat tenderizer. The physiochemical properties, proximate composition, and sensory characteristic of carabeef treated with the bacterial enzyme and a commercial meat tenderizer containing papain were determined. Only B. subtilis protease showed significant enzyme activity (80-190 U/g), while the commercial meat tenderizer had no activity (0 U/g). Results from the shear force device revealed that 0.35% B. subtilis protease was the optimal concentration required to induce significant tenderization in carabeef (282 g/cm sup 2) and found to reduce carabeef toughness by 80%. Proximate analysis revealed that the roasted carabeef samples had less moisture content and more crude protein. However, carabeef treated with B. subtilis protease had significantly greater crude protein (37%) than the negative control (34%) and carabeef treated with commercial meat tenderizer (31%). Sensory evaluation showed that carabeef treated with 0.35% B. subtilis protease is more tender than untreated and those treated with commercial meat tenderizer. Hence, B. subtilis protease can be commercially used as a meat tenderizer in place of available commercial tenderizers containing plan proteases without causing over tenderization.
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