High pressure treatment and the effects on meat proteins

When understanding the mechanisms of HPinduced changes, HP can be used in targeted and unique biomolecule architecture. Thereby, HP offers opportunities to modify structure and interactions within or between biopolymers. This review introduces the principle of HP and its characteristic followed by a description of the pressure effects on meat proteins. Overall, meat protein systems and meat proteins as such are rather pressurelabile of nature. It is shown that HP results in significant changes in the sarcomere and is capable of modifying meat proteins by pressureinduced changes of the molecular structure. Pressurization (200-800 MPa) of meat affects the structure and functionality of myofibrillar proteins resulting in a considerably decreased solubility due to formation of insoluble aggregates. The underlying mechanisms of these pressureinduced molecular changes consist of two overall steps: 1) rupture of the noncovalent, intermolecular interactions resulting in protein denaturation and 2) formation of new intraand/or intermolecular noncovalent bonds resulting in aggregation. How these findings may be useful for future research in medical and pharmaceutical applications is speculated upon.