Abstract
Response surface methodology was adopted to model and optimize the effects of microbial transglutaminase (TG) and calcium alginate (CA) systems of various ratios on the gelation characteristics of porcine myofibrillar protein (MP) at various salt levels. The CA system consisting of sodium alginate (SA), calcium carbonate (CC) and glucono--lactone (GdL) showed no remarkable changes in the salt-soluble fraction, and only minor effects on electrostatic interactions were observed. Increasing CA concentration caused acid-induced hydrophobic interactions in MPs, resulting in increased MP gel strength. The TG system, containing TG and sodium caseinate (SC), induced cold-set MP gelation by formation of covalent bonding. The main advantage of the combined system was a higher cooking yield when the MP gel was heated. These results indicated that 0.7% TG combined with 0.8% CA system can form a viscoelastic MP gel, regardless of salt levels.
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