Gene

Biology

Storage protein

Animal science

Proteolysis

Vimentin

Telecommunications

Longissimus

Biochemistry

Skeletal muscle

Computer science

Food science

Tenderness

Immunology

Myofibril

Anatomy

Muscle protein

Degradation (telecommunications)

Desmin

Enzyme

Myocardial infarction

Internal medicine

Troponin T

Food storage

Medicine

Chemistry

Immunohistochemistry

Protein degradation

Muscle fibre

Meat Science

This study investigated the effect of superchilled storage (−4 °C) on protein degradation and structural changes of beef steaks from M. longissimus lumborum compared with traditional chilling (2 °C) and frozen storage (−18 °C). Traditional chilling induced significantly greater degradation of troponin T and desmin, and more rapid loss of calpain activity, compared to superchilled or frozen storage treatments. The proteolysis of key myofibrillar proteins resulted in a sharp decline of WBSF values during traditional chilled storage. For frozen beef samples, no major changes were observed with respect to protein degradation or muscle structure during storage. However, superchilled samples exhibited wider gaps between muscle fibers at 12 weeks storage, associated with muscle fiber shrinkage.

Protein degradation and structure changes of beef muscle during superchilled storage