Background: During the initial steps of green biorefining aimed at protein recovery, endogenous proteins and enzymes, along with, e.g., phytochemical constituents, are decompartmentalized into a green juice. This creates a highly dynamic environment prone to a plethora of reactions including oxidative protein
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Background: During the initial steps of green biorefining aimed at protein recovery, endogenous proteins and enzymes, along with, e.g., phytochemical constituents, are decompartmentalized into a green juice. This creates a highly dynamic environment prone to a plethora of reactions including oxidative protein modification and deterioration. Obtaining a fundamental understanding of the enzymes capable of exerting antioxidant activity
ex vivo could help mitigate these reactions for improved product quality.
Methods: In this study, we investigated perennial ryegrass (
Lolium perenne var. Abosan 1), one of the most widely used turf and forage grasses, as a model system. Using size exclusion chromatography, we fractionated the green juice to investigate
in vitro antioxidant properties and coupled this with quantitative bottom-up proteomics, GO-term analysis, and fraction-based enrichment.
Results: Our findings revealed that several enzymes, such as superoxide dismutase and peroxiredoxin proteoforms, already known for their involvement in
in vivo oxidative protection, are enriched in fractions displaying increased
in vitro antioxidant activity, indicating retained activity
ex vivo. Moreover, this study provides the most detailed characterization of the
L. perenne proteome today and delivers new insights into protein-level partitioning during wet fractionation.
Conclusions: Ultimately, this work contributes to a better understanding of the first steps of green biorefining and provides the basis for process optimization.
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