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Insight into dairy casein implications that enhance egg white proteins' thermodynamic and microrheological functions
Mohamed Salama1, Mostafa Gouda2, Mahmoud Abou-Elsoud3
1Hubei Hongshan Laboratory, College of Food Science and Technology, Huazhong Agricultural University, Wuhan 430070, China; Dairy Department, Food Industries and Nutrition Research Institute, National Research Centre, Dokki 12622, Cairo, Egypt.
Abstract:
One of the critical challenges in egg white proteins (EWP) industry is its high aggregation ability during its heat pasteurization preprocess. Thus, the current study has explained the casein (CN) mechanism to improve EWP thermal stability. In the methods, EWP-CN intermolecular forces, covalent bonds, secondary structure thermal behaviors, and micro-rheology were investigated. The results showed that EWP-CN sulfhydryl bonds and hydrophobicity were enhanced significantly (p < 0.05) after dynamic heat treatment. Whereas, EWP-CN complex (2,1, v/v) demonstrated the lowest turbidity (61.6 %) and highest stability coefficient (78.2 %) at 90 °C for 20 min compared to EWP. Besides, CN (10 mg/mL) has decreased the EWP aggregated particles up to 1.8 times compared to the control. That was in harmony with viscosity, storage modulus, and thermogram patterns, indicating high heat resistance. In conclusion, this study establishes a new concept to enhance the sensitive raw protein's responses by their conjugations with potential active stabilizers.
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