Abstract
The effect and mechanism of myofibrillar protein (MP) gelation influenced by konjac glucomannan (KG) addition were studied. The KG addition significantly improved gel strength and water holding capability (WHC) of MP-KG composite gel, but it had additive limitation at 1.0%. The SEM showed that KG (<1.0%) reduced the appearance of moisture channels and promoted the formation of an integral MP gel network. Raman spectroscopy showed that KG addition (<1.0%) promoted the protein unfolding and the interaction of hydrophobic groups during thermal processing. However, the KG (>1.0%) would form continuous viscous hydrogel and interpenetrate with the MP solution, which hindered the interaction of hydrophobic groups during thermal process, and the MP formed a loose and degraded final structure. Hence, MP gels produced with the addition of KG underwent a transformation from a loose structure to a compact structure to an unaggregated structure, which was influenced by moisture stability and phase separation behavior.
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