Abstract

The effect of egg white protein (EWP) and β-cyclodextrin (β-CD) mixture was analysed on the myofibrillar proteins (MP) of Culter alburnus during a frozen storage at −18 °C for 60 days. Different proportions of EWP:β-CD mixture (0%, 2%, 4% and 6%) were added into MP to analyse their effect against oxidative changes. During the study, sulphydryl contents and Ca-ATPase activity (0.297 to 0.136 mmol g−1) decreased. Moreover, protein denaturation also prompted the surface hydrophobicity (11.47 to 32.06 μg) and carbonyls (26.36 to 49 mg.28 nmol mg−1) of control MP. A significant decline was observed in emulsifying properties. Besides, EWP:β-CD showed remarkable stability against oxidative changes, by significantly reducing the carbonyls (26.26 to 37.69 nmol mg−1) and surface hydrophobicity (11.51 to 20.31 μg) and also the decline of Ca-ATPase activity (0.29 to 0.19 mmol g−1). It can be concluded that EWP:β-CD (6%) is an efficient approach against oxidative changes in MP from Culter alburnus.