Abstract
In this study, the gel properties of myofibrillar proteins (MPs) from four meat sources (fish, beef, sheep, and pork) were compared. Oscillatory rheology measurements including temperature sweep, frequency sweep, and strain sweep were conducted to characterise the small and large deformation rheological properties of the MPs. In addition, sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and scanning electron microscopy (SEM) were used to evaluate differences in the molecular weight distribution as well as the microstructures in gel among different MPs. Frequency sweep measurements showed that all MP gels were weak gels. MPs extracted from pork exhibited the highest gel strength and most compact gel structure, whereas those from fish exhibited the lowest gel strength and loosest gel structure. In addition, the MP extracted from pork (PSM) had the highest content of myosin heavy chain (MHC) and actin. In conclusion, the MPs extracted from fish source and mammalian sources varied significantly in terms of rheological properties and microstructural characteristics. These results provided useful information for developing mixed gel products with different gel strengths.
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