Filamentous myosin in low-ionic strength meat protein processing media: Assembly mechanism, impact on protein functionality, and inhibition strategies

Abstract

BackgroundSalt-soluble myofibrillar proteins (MPs) form the major protein component of meat and have several advantages over plant-derived proteins, including high digestibility and the presence of all the essential amino acids. However, MPs are not widely used because the presence of myosin filaments limits their functionality in low ionic strength media. Hence, an approach for effectively inhibiting or disrupting the formation of myosin filaments is a challenging issue in the development of novel meat protein based products. Scope and approachTo develop a strategy for inhibiting or destroying the formation of myosin filaments, an understanding of the process of myosin self-association is needed at the molecular level. Hence, the present review systematically elaborates the assembly mechanism of myosin filaments and its relation to the functionality of MPs. Additionally, the review focuses on the description of several chemical and physical strategies, with an emphasis on advantages, disadvantages, and recent progress. Key findings and conclusionsThe assembly of myosin into filaments has been shown to be mediated by sequentially distributed charges in the myosin tail. Moreover, the dissociation of myosin filaments, leading to improved functional properties of the MPs, has been demonstrated by amino acid treatment, glycation, high-intensity ultrasonication (HIU), and high-pressure homogenization (HPH) in low ionic strength media. Nevertheless, these strategies still face a number of limitations and, hence, further research is needed in order to achieve large-scale industrial production. In addition, the enhanced development of novel meat protein based products requires a consideration of the thermal stability of MPs throughout the entire process from product sterilization through to preservation and consumption.