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by claude@2026-07, 2026-07-04
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The paper evaluated how different downstream processing technologies affect the bulk properties and composition of clover grass protein prototypes, using membrane filtration followed by acid, heat, acid+heat precipitation, or ultra-/diafiltration with/without subsequent tryptic hydrolysis. Heat treatment produced CGPs with the highest protein content and greater whiteness, but reduced aqueous solubility, while the diafiltered concentrate showed excellent solubility across a broad pH range. Across prototypes, the proteins strongly reduced oil–water interfacial tension and showed viscoelastic, solid-like interfacial behavior, yet stabilized emulsions were physically unstable with larger droplets, and proteomics indicated CGPs were rich in RuBisCO with comparable overall protein composition despite state-dependent functional differences. The paper does not discuss endometriosis or adenomyosis; it was included in the corpus via a keyword match in the upstream search index.
Abstract
This study investigated the effects of different downstream processes for protein isolation on the bulk properties and composition of clover grass protein prototypes (CGPs). A clarified clover grass juice, obtained using membrane filtration (MF), underwent precipitation by acid (AP), heat (HP), or acid+heat (AHP), or underwent ultra- and diafiltration to produce a concentrate (DC) as well as subsequent tryptic hydrolysis of DC (DCH). HP had the highest protein content (p<0.05) and was whiter than other CGPs, although it showed lower aqueous solubility. In contrast, DC showed excellent solubility across a broad pH range. CGPs efficiently decreased oil-water interfacial tension (16-13 mN/m) and displayed viscoelastic and solid-like interfacial behavior. CGPs-stabilized emulsions displayed low physical stability with larger droplets despite high absolute ζ-potentials. CGPs were rich in RuBisCO (37-47%) but had varying levels of other proteins. Despite significant protein-level differences, overall protein composition of CGPs was comparable, highlighting that protein state governs bulk functionality more than subtle compositional changes. Graphical abstract Created with BioRender.com Highlights The effect of different processes on functional properties of CGPs was explored. Heat treatment increased protein purity and whiteness at the expense of solubility. CGPs efficiently reduced O/W interfacial tension but produced unstable emulsions. CGPs were found rich in RuBisCO (34-47%) using quantitative proteomics. Protein state had larger influence on functionality than protein-level composition.
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Abstract
This study investigated the effects of different downstream processes for protein isolation on the bulk properties and composition of clover grass protein prototypes (CGPs). A clarified clover grass juice, obtained using membrane filtration (MF), underwent precipitation by acid (AP), heat (HP), or acid+heat (AHP), or underwent ultra- and diafiltration to produce a concentrate (DC) as well as subsequent tryptic hydrolysis of DC (DCH). HP had the highest protein content (p<0.05) and was whiter than other CGPs, although it showed lower aqueous solubility. In contrast, DC showed excellent solubility across a broad pH range. CGPs efficiently decreased oil-water interfacial tension (16-13 mN/m) and displayed viscoelastic and solid-like interfacial behavior. CGPs-stabilized emulsions displayed low physical stability with larger droplets despite high absolute ζ-potentials. CGPs were rich in RuBisCO (37-47%) but had varying levels of other proteins. Despite significant protein-level differences, overall protein composition of CGPs was comparable, highlighting that protein state governs bulk functionality more than subtle compositional changes.
Graphical abstractCreated with BioRender.com
Highlights
The effect of different processes on functional properties of CGPs was explored.
Heat treatment increased protein purity and whiteness at the expense of solubility.
CGPs efficiently reduced O/W interfacial tension but produced unstable emulsions.
CGPs were found rich in RuBisCO (34-47%) using quantitative proteomics.
Protein state had larger influence on functionality than protein-level composition.
Competing Interest Statement
Peter Stephensen Lubeck reports a relationship with BiomassProtein ApS that includes board membership. Simon Gregersen Echers, Peter Stephensen Lubeck, Tuve Mattsson, Anders K Jorgensen, and Mette Lubeck have the patent #WO2025/133209: Method for Producing a food-grade protein product and/or feed protein product from plant material. Remaining authors report no competing interests.
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