Author/Authors :
Zhao، نويسنده , , Guo-Yan and Zhou، نويسنده , , Ming-Yang and Zhao، نويسنده , , Huilin and Chen، نويسنده , , Xiu-Lan and Xie، نويسنده , , Binbin and Zhang، نويسنده , , Xi-Ying and He، نويسنده , , Hai-Lun and Zhou، نويسنده , , Bai-Cheng and Zhang، نويسنده , , Yu-Zhong، نويسنده ,
Abstract :
The enzymes currently used to increase meat tenderness are all mesophilic or thermophilic proteases. This study provides insight into the tenderization effect and the mechanism of a cold-adapted collagenolytic enzyme MCP-01 on beef meat at low temperatures. MCP-01 (10 U of caseinolytic activity) reduced the meat shear force by 23% and increased the relative myofibrillar fragmentation index of the meat by 91.7% at 4 °C, and it also kept the fresh colour and moisture of the meat. Compared to the commercially used tenderizers papain and bromelain, MCP-01 showed a unique tenderization mechanism. MCP-01 had a strong selectivity for degrading collagen at 4 °C, showed a distinct digestion pattern on the myofibrillar proteins, and had a different disruption pattern on the muscle fibres under scanning electron micrograph. These results suggest that the cold-adapted collagenolytic protease MCP-01 may be promising for use as a meat tenderizer at low and moderate temperatures.
Keywords :
Cold-adapted collagenolytic protease , Mcp-01 , Collagen , myofibrillar proteins , Meat tenderization