Degradation of myofibrillar, sarcoplasmic and connective tissue proteins by plant proteolytic enzymes and their impact on camel meat tenderness
Inside round muscles (Adductor) from camels treated with bromelain or ficin or papain at 50 or 100 ppm were subsequently stored at 4 °C for 4 days to study the impact on quality attributes, protein degradation and textural changes. Results revealed that papain (100 ppm) treated camel meat showed higher drip loss and lower water holding capacity compared to other treatments. Total protein, sarcoplasmic protein solubility, trichloroacetic acid (TCA)-soluble peptides and soluble collagen were higher in papain and bromelain treated samples at 100 ppm compared to other treatments. Electrophoretic profile of whole camel meat, isolated sarcoplasmic and myofibrillar proteins depicted a noticeable degradation of various proteins in enzyme treated samples, with papain and bromelain (100 ppm) displaying pronounced effect. Meat treated with papain at 100 ppm displayed lower hardness and shear force (P < 0.05). Thus, enzymes treatment at 100 ppm displayed good potential to tenderize camel meat with the papain being more effective among all.
KeywordsEnzymes Quality Tenderization Camel meat Proteolysis SDS-PAGE
Authors are thankful to United Arab Emirates University for the funding this research through a research grant (UAE-NRF No. 31F024 and UPAR 31F078).
Compliance with ethical standards
Conflict of interest
The authors declare no conflict of interest.
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