Processing–Microstructure–Properties Relationship of Meat Myofibrillar Proteins as Defined by High Hydrostatic Pressure

High hydrostatic pressure (HHP) modulates noncovalent interactions of myofibrillar proteins (MP) at low temperature and influences microstructure-quality-function coupling for tailored meat quality and product development. Nevertheless, multiscale structural responses to pressure gradients remain incompletely defined. This review summarizes recent evidence on HHP-induced MP conformational transitions, aggregation-reorganization behaviors, and functional outcomes and discusses their qualitative/quantitative relationship with improvements in meat quality attributes. Comparative analyses across meats highlight differences in domain flexibility, hydrophobic exposure, and cross-linking propensity, underscoring the need for a cross-species structure-quality-function predictive model. At the processing level, combining HHP with fermentation, curing, and aging processes can accelerate diffusion and throughput, reduce salt inputs, and optimize the texture and flavor. Future work should prioritize cross-species, multiparameter predictive models, in situ time-resolved characterization, and carbon-footprint assessment frameworks. In summary, HHP provides a controllable molecular-level pathway to develop low-salt, clean-label, high-quality meat products while supporting mechanistic innovation and industrial application in nonthermal processing.