Abstract
This study explored the use of pig blood fibrinogen hydrolysates, enzymatically hydrolyzed with trypsin and flavorzyme, to enhance myofibrillar protein gels, addressing issues like poor gel strength and water loss in meat products. By incorporating varying concentrations of fibrinogen hydrolysates into myofibrillar proteins, heat-induced gels were prepared. The composite gels showed improved textural properties, rheological characteristics and water-holding capacity. Scanning electron microscopy and atomic force microscopy analyses revealed a uniform, dense surface and an orderly internal structure in the composite gels. The study also noted decreased α-helix and random coil and increased β-sheet and β-turn contents, indicating a more ordered secondary structure. Hydrophobic interactions and disulfide bonds were identified as key factors in enhancing gelation, and a model was proposed to explain these molecular effects. This research demonstrates a potential of fibrinogen hydrolysates to improve quality and structure of myofibrillar protein gels designed for high-quality meat products.
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