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J Agric Food Chem ; 69(36): 10630-10637, 2021 Sep 15.
Article in English | MEDLINE | ID: mdl-34473491

ABSTRACT

In this study, ß-glucan interaction with lentil and yellow pea proteins and the effect on in vitro protein digestibility were investigated. Proteins were mixed with ß-glucan at mass ratios of 1:0.5, 1:1, and 1:2. The interaction between ß-glucan and the proteins was demonstrated by the decrease in transmittance and surface charge and the increase in particle size of the complexes. Bright-field microscopy showed the formation of aggregates between the biopolymers, although increased molecular size was not observed by discontinuous native polyacrylamide gel electrophoresis. Fluorescence microscopy indicated that ß-glucan formed aggregates with lentil proteins, while the interaction with yellow pea proteins appeared as distinct phases of protein within the ß-glucan network. The in vitro protein digestibility of lentil and pea protein decreased by 27.3 and 34.5%, respectively, in the presence of a ß-glucan mass ratio of 1:2. The findings confirm the possibility to modulate protein digestibility by changing the physical characteristics of a food matrix.


Subject(s)
Lens Plant , Pea Proteins , beta-Glucans , Allergens , Pisum sativum
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