Functionality of muscle constituents in the processing of comminuted meat products.
Emulsification through the creation of a fat dispersion and formation of an interfacial protein membrane at the fat-water interface is not the sole aspect responsible for comminuted meat "emulsion" stability. In addition, water binding which occurs initially during myofibrillar protein extraction from tissue disruption, and later during entrapment within the heat-induced protein gel matrix, must be included. The criteria that affect formation of the gel matrix adds another aspect, in that conditions for optimum protein-protein interaction also influence ultimate water and fat stabilization. Rheological considerations are in their infancy and will require future study, particularly during the transformation of a "flowing" batter into a "nonflowing" solid product. This review has been aimed at emphasizing that the myofibrillar protein component is the predominant constituent involved in an interactive role with water, fat, and itself, in forming the ultimate stabilized comminuted meat matrix.
D000185:Actinin; D000205:Actomyosin; D000818:Animals; D002417:Cattle; D055598:Chemical Phenomena; D002621:Chemistry; D004655:Emulsions; D005511:Food Handling; D006863:Hydrogen-Ion Concentration; D008055:Lipids; D046911:Macromolecular Substances; D008460:Meat / Q000592:standards; D008461:Meat Products / Q000592:standards; D009124:Muscle Proteins; D009132:Muscles; D009210:Myofibrils; D015879:Myosin Subfragments; D009218:Myosins; D013499:Surface Properties; D013552:Swine; D013696:Temperature; D014783:Viscosity; D014867:Water
D004655:Emulsions; D008055:Lipids; D046911:Macromolecular Substances; D009124:Muscle Proteins; D015879:Myosin Subfragments; D014867:Water; D000185:Actinin; D000205:Actomyosin; D009218:Myosins