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High pressure (HP) has the prospect to engineer protein conformation, but the fundamentals of physicochemical HP-effects on biomolecules need to be addressed before HP can be fully exploited.

When understanding the mechanisms of HP-induced 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 pressure-labile of nature. It is shown that HP results in significant changes in the sarcomere and is capable of modifying meat proteins by pressure-induced 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 pressure-induced molecular changes consist of two overall steps: 1) rupture of the noncovalent, intermolecular interactions resulting in protein denaturation and 2) formation of new intra- and/or intermolecular non-covalent bonds resulting in aggregation.  How these findings may be useful for future research in medical and pharmaceutical applications is speculated upon.