Salt extraction and subsequent micellization of pea protein: effects on composition, structure, and functionality

TY - CONF

T1 - Salt extraction and subsequent micellization of pea protein

T2 - 3rd Food Chemistry conference

AU - Zhang, Yi

AU - Corredig, Milena

PY - 2023

Y1 - 2023

N2 - Pea proteins are increasingly gaining popularity as alternatives to animal-derived protein sources. The quality of pea protein ingredients is greatly affected by the extraction history. However, a detailed understanding of the interrelation between process parameters and structure is not yet available. This research aimed to investigate differences caused by micellization after salt extraction. Particularly, the composition, conformational and functional properties of pea proteins were compared between extracts obtained at high salt concentration and then diluted, and those extracted with lower but the same concentration of salt as the diluted. It was expected that the composition and structure of protein populations remaining soluble would be comparable when tested at the same ionic composition. The protein composition was studied using SDS-PAGE and size exclusion chromatography with multi-angle static light scattering and refractive index (SEC-MALS-RI) detection. The presence of ions and phytate were also measured. The structure of samples was characterized at various length scales using FTIR, fluorescence, and SAXS. To better understand potential differences in structure/function relationships between samples, drop tensiometry was applied to evaluate the interfacial behavior. The diluted samples had a similar protein profile to non-diluted samples that were extracted with the same salt concentration. In contrast, the protein composition changed after dilution with increased soluble aggregates and decreased legumin in the diluted samples. The proportion and aggregation state of vicilin was not influenced by the micellization process. Significant differences in protein structure between the diluted and non-diluted samples were observed. The diluted samples had a more flexible conformational structure, contributing to their different interfacial behaviors at the W/O interface. The structural response as an effect of micellization provides novel insights into the potential of controlled modification of conformational structure of pea protein products for better functional applications in food industry.

AB - Pea proteins are increasingly gaining popularity as alternatives to animal-derived protein sources. The quality of pea protein ingredients is greatly affected by the extraction history. However, a detailed understanding of the interrelation between process parameters and structure is not yet available. This research aimed to investigate differences caused by micellization after salt extraction. Particularly, the composition, conformational and functional properties of pea proteins were compared between extracts obtained at high salt concentration and then diluted, and those extracted with lower but the same concentration of salt as the diluted. It was expected that the composition and structure of protein populations remaining soluble would be comparable when tested at the same ionic composition. The protein composition was studied using SDS-PAGE and size exclusion chromatography with multi-angle static light scattering and refractive index (SEC-MALS-RI) detection. The presence of ions and phytate were also measured. The structure of samples was characterized at various length scales using FTIR, fluorescence, and SAXS. To better understand potential differences in structure/function relationships between samples, drop tensiometry was applied to evaluate the interfacial behavior. The diluted samples had a similar protein profile to non-diluted samples that were extracted with the same salt concentration. In contrast, the protein composition changed after dilution with increased soluble aggregates and decreased legumin in the diluted samples. The proportion and aggregation state of vicilin was not influenced by the micellization process. Significant differences in protein structure between the diluted and non-diluted samples were observed. The diluted samples had a more flexible conformational structure, contributing to their different interfacial behaviors at the W/O interface. The structural response as an effect of micellization provides novel insights into the potential of controlled modification of conformational structure of pea protein products for better functional applications in food industry.

M3 - Poster

Y2 - 10 October 2023 through 12 October 2023

ER -