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A strategy for regulating conformational of mulberry leaf protein based on cold plasma modification: Implications for
Jingkai Zhang1, Danrong Zhao1, Yi Liu1
1College of Food Science and Engineering, Shandong Agricultural University, Key Laboratory of Food Nutrition and Human Health in Universities of Shandong, Tai'an 271018, PR China.
Abstract:
Cold plasma (CP) was used as a non-thermal strategy to improve the solubility and foaming properties of mulberry leaf protein (MLP). MLP was treated for different times and evaluated for solubility, foaming capacity, foam stability, and structural changes. A 120 s CP treatment gave the best results, increasing solubility, foaming capacity, and foam stability by 3.50-fold, 3.27-fold, and 4.14-fold, respectively. CP cleaved disulfide (SS) bonds, increased exposed sulfhydryl groups, and raised surface hydrophobicity. It also reduced particle size and altered secondary structure, with lower α-helix and β-sheet contents and higher random coil. These changes partially unfolded MLP, enhancing molecular flexibility, water interaction, and interfacial adsorption, which strengthened foam formation and stability. Overall, CP effectively tailors the interfacial functionality of plant proteins and offers a promising route to valorize MLP for foam-based and aerated food products.

