Myofibrillar proteins of vertebrate skeletal muscles are insoluble in solutions of ionic strength that approximate physiological conditions. We established a method to solubilize more than 80% of chicken breast muscle myofibrillar proteins in water for the use of meat as a source of food protein. SDS-polyacrylamide gel electrophoretic patterns of water-soluble myofibrillar proteins demonstrated that all identified myofibrillar proteins except connectin/titin were soluble in water. A part of α-actinin was released from myofibrils by repeated washing with 2.5 mmol/L NaCl and 5 mmol/L L-histidine solution, and subsequent destruction of connectin/titin in washed myofibrils by ultrasonication resulted in solubilization of a large fraction of chicken breast muscle myofibrillar proteins in water. Myofibrillar proteins of chicken leg, pork loin, beef shoulder loin, and lamb were also solubilized in water using this procedure.
All Science Journal Classification (ASJC) codes
- Agricultural and Biological Sciences(all)