AI Article Synopsis
- This study examines the effects of different processing methods on yellow lupin protein isolates (YLPI), highlighting changes in structure and properties due to defatting.
- The defatting process alters the physical and functional characteristics of YLPI, reducing α-helix content and increasing disulfide bonds, which enhances emulsifying stability.
- Both hot and cold defatting lead to decreased turbidity and changes in protein particle size and viscosity, indicating structural changes in the protein isolates.
Article Abstract
This study investigates the structure, physico-chemical and functional properties of yellow lupin isolate protein (YLPI) obtained by different processes (conventional wet and purely aqueous fractionation) from un-defatted (YLPIU), and hot (YLPIHD) and cold (YLPICD) defatted flour. The defatting process modified the physical, structural and functional characteristics of lupin protein isolates. Indeed, a decrease of α-helix, free sulfhydryl groups amount and an increase of disulfide bond levels were observed for defatted samples, improving their emulsifying stability. The defatting process exposes the hydrophobic groups present within the YLPI, which increases total sulfhydryl content and protein surface hydrophobicity. Hot and cold defatting induced a decrease in turbidity, water-holding capacity, oil adsorption capacity, tapped and poured bulk densities. In addition, the defatting process changed the particle size of protein isolates that induced changes in their viscosity. Tryptophan spectra and protein surface hydrophobicity indicated that YLPICD and YLPIHD underwent structural conformational change during the defatting process.
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| http://dx.doi.org/10.1016/j.foodchem.2023.137871 | DOI Listing |
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