Gelation of Crude Myofibrillar Protein Isolated From Beef Heart Under Antioxidative Conditions

Oxidation inhibition during washing, as it affects gelling properties and binding strength of beef heart myofibrillar protein, was investigated. Crude myofibrils isolated by repeated washing in the presence of propyl gallate, ascorbate and tripolyphosphate had a lower TBA value and formed stronger gels (puncture and compression strengths) in the pH range 5.8–7.0 and in 0.6M NaCl than the control myofibrils. Inhibition of oxidation increased tensile stress of myofibrillar gels and enhanced bind strength in restructured meat. Functionality of myofibrillar protein could be protected by antioxidants used in the washing process.