Background: Eucommia ulmoides Oliv. seed meal (ESM) as a potential edible protein source as this by-product is usually underutilized or discarded. This study aimed to isolate antioxidant ESM protein hydrolysates (ESMHs) fractions and investigate their physicochemical properties to explore their potential applications.
Results: Three fractions (F1, F2, F3) were isolated via gel chromatography, showing a positive correlation between the antioxidant capabilities and their antioxidant amino acids composition. Fluorescence spectra revealed a red shift of 3-6 nm in the maximum emission wavelength (λmax) for the fractions compared to ESMHs, indicating increased exposure of aromatic amino acids on the side chains of F1, F2, and F3 isolates. The surface hydrophobicity (H0) index for these isolates followed the order: F2 > F3 > F1, aligning with their endogenous fluorescence spectra data. These findings further verified that more hydrophobic amino acid residues were exposed as a result of the structural unfolding of proteins. Thermal stability analysis demonstrated that the isolated fractions with higher H0 required less energy for denaturation. A distinct taste difference was observed between isolated fractions and ESMHs, tyrosine, phenylalanine, histidine and arginine were closely associated with the taste generation. Additionally, the low molecular weight and high glutamic acid content of the isolated fractions would contribute to their umami taste.
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The Journal of the Science of Food and Agriculture publishes peer-reviewed original research, reviews, mini-reviews, perspectives and spotlights in these areas, with particular emphasis on interdisciplinary studies at the agriculture/ food interface.
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