Sd. Arntfield et A. Bernatsky, CHARACTERISTICS OF HEAT-INDUCED NETWORKS FOR MIXTURES OF OVALBUMIN AND LYSOZYME, Journal of agricultural and food chemistry, 41(12), 1993, pp. 2291-2295
Proteins with opposite charges were heated together to assess the impa
ct of this combination on the characteristics of the heat-induced prot
ein networks produced. The thermal properties and dynamic theological
characteristics of heat-induced networks were evaluated for ovalbumin,
lysozyme, and mixtures of the two at ratios ranging from that natural
ly found in egg white to 1:1. Ovalbumin formed stronger (high G' and G
''), more well cross-linked networks (lower tan delta value) than lyso
zyme. Network formation was unaffected by mixing ovalbumin and lysozym
e at pH 5.5, whereas at pH 7.0 and 8.5 network strength increased and
cross-linking in the network decreased as the relative proportion of l
ysozyme was increased. Mixed protein systems can produce stronger, les
s structured networks than pure proteins. Removal of lysozyme from egg
albumen can adversely affect its gel strength and hence reduce its co
ntribution to the textural properties of food products.