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Abstract Mild heating (20 °C, 40 °C, 60 °C, and 80 °C) for 1 h assisted pH12 shifting on the structural, physicochemical and functional properties of egg white protein (EWP) were investigated. The results of… Click to show full abstract
Abstract Mild heating (20 °C, 40 °C, 60 °C, and 80 °C) for 1 h assisted pH12 shifting on the structural, physicochemical and functional properties of egg white protein (EWP) were investigated. The results of intrinsic fluorescence, surface hydrophobicity, and free sulfhydryl groups indicated that the tertiary structure depolymerized, the hydrophobic groups exposed and the protein subunits dissociated. Fourier transform infrared spectrophotometer and circular dichroism showed that the content of α-helix decreased, and the content of β-turn increased in the secondary structure of EWP. Moreover, the size and zeta potential of EWP12-80 significantly decreased to 119.17 nm (P
Journal Title: Lwt - Food Science and Technology
Year Published: 2021
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