Plant proteins are a promising source for producing amphiphilic polypeptides with tailored techno-functional properties to be used in various food applications, such as fat replacers. This study investigated the effects of moderate enzymatic hydrolysis on amphiphilic polypeptide generation, by understanding the relationship of bioprocess - protein structure - functionality - amphiphilicity mechanism. Compared to non-specific protease alcalase, the specific protease trypsin catalyzed the production of polypeptides with higher surface hydrophobicity and relatively high molecular weight. Trypsin-produced polypeptides exhibited significantly higher water and oil holding capacities, foaming capacities, and emulsification than alcalase-produced counterparts. Furthermore, polypeptide sequences were obtained from proteomics and used to analyze amphiphilicity using Grand Average of Hydropathy (GRAVY) scores and hydropathy plots. Trypsin produced high number of amphiphilic polypeptides with balanced hydrophilic and hydrophobic regions. Molecular dynamics (MD) simulations of selected amphiphilic polypeptides in water-oleic acid systems suggested strong hydrophobic interactions with oleic acid and stable conformations in the interface.
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| http://dx.doi.org/10.1016/j.foodchem.2025.143602 | DOI Listing |
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