Heat-induced Gelation Properties of Chicken Breast Muscle Salt Soluble Proteins when Mixed with β-Lactoglobulin or an α -Lactalbumin Enriched Protein Fraction

摘要

The heat-induced gelation properties of mixed protein systems containing chicken breast muscle salt-soluble proteins (SSP) and β-lactoglobulin (β-lg) or SSP and an α-lactalbu- min-enriched fraction (α-la) in 0.6 M NaCl, pH 6.5, were investigated using dynamic rheology. At 70 deg. C, SSP had greater storage modulus (') values than mixtures conain- ing SSP /α-lg. However, at 90 deg. C, mixtures containing 80: 20 and 60: 40 SSP: β-lg had higher G' values than SSP alone, indicating that denaturation of β-lg directly or indirectly facilitates the formation of a more rigid gel structure.