Abstract
ABSTRACTCo‐gels of egg white (EW) and oat globulin (native and deamidated) were prepared by heating mixtures of the two proteins at different ratios. Rheological properties of the co‐gels were assessed by small amplitude oscillatory tests. Storage (G′) and loss (G″) moduli of the co‐gels increased with increases in EW content in the mixtures. At comparable EW/non‐EW ratios, EW formed much stronger co‐gels with deamidated oat globulin (DOG) than with native globulin (OG) or several other non‐EW proteins. Microscopic examination of mixed gels revealed structural differences between EW/OG and EW/DOG co‐gels. The former exhibited a two gel system with OG distributed discontinuously throughout the supporting EW matrix. DOG and EW formed a homogenous gel network, demonstrating compatibility between the two proteins.
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