The effect of active caspase-3 on degradation of chicken myofibrillar proteins and structure of myofibrils

Food Chem. 2011 Sep 1;128(1):22-7. doi: 10.1016/j.foodchem.2011.02.062. Epub 2011 Feb 18.

Abstract

The objective of this study was to investigate the potential contribution of caspase-3 to meat postmortem tenderisation by examining the role of caspase-3 in the degradation of myofibrillar proteins and disruption of myofibril structure in vitro. Myofibrillar protein prepared from chicken muscle was incubated with EDTA or EDTA plus caspase-3 at 25°C for 16h and used for detecting muscle protein degradation and ultrastructure of myofibril. Results revealed that caspase-3 reproduced the degradation patterns of titin, nebulin and α-actinin during postmortem storage of meat, but caused little proteolysis of desmin and no appearance of 28-30kDa peptides. Meanwhile, caspase-3 also induced the weakening in the I band adjacent to Z-lines, which occurred during meat postmortem ageing. Therefore, caspase-3 could account only for a part of the myofibrillar protein degradation observed in naturally aged meat and is likely involved in postmortem tenderisation of meat together with other endogenous proteases.

Keywords: Caspase-3; Chicken muscle; Myofibrillar proteins; Tenderisation; Ultrastructure.