Enzyme-specific structural modifications regulate interfacial properties and emulsion stability of rice protein
Ju Yeon Ha1, Mi-Jung Choi2, Yeon-Ji Jo1
1Department of Marine Bio Food Science, Gangneung-Wonju National University, Gangneung 25457, Republic of Korea.
None:
In this study, rice protein hydrolysates (RPHs) were prepared using four proteases (Alcalase, Flavourzyme, Neutrase, and Protamex) and their structural and functional properties were systematically compared. Alcalase and Protamex generated diverse low-molecular-weight peptides that enhanced solubility and interfacial tension reduction, whereas Flavourzyme mainly released short peptides and free amino acids, increasing hydrophobicity with limited solubility. Emulsion characterization revealed that droplet size, distribution, and rheology were affected by both enzyme type and oil fraction (30-70%). At 70% oil, only Flavourzyme- and Protamex-stabilized emulsions were measurable, with Flavourzyme showing the highest viscosity and yield stress. High-pressure homogenization (HPH) further reduced droplet sizes to 343-517 nm and improved colloidal stability. Notably, Flavourzyme- and Neutrase-derived emulsions formed monomodal nanoemulsions with highly negative ζ-potential, whereas Alcalase and Protamex resulted in broader distributions and residual aggregates. These findings demonstrate that protease specificity and homogenization regime act synergistically to govern peptide structure, interfacial behavior, and emulsion stability.
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