β-Glucan Interaction with Lentil (Lens culinaris) and Yellow Pea (Pisum sativum) Proteins Suppresses Their In Vitro Digestibility

豌豆 葡聚糖 萝卜 豌豆 豌豆蛋白 体外 多糖 化学 生物化学 电泳 食品科学 生物 植物
作者
Ruth T. Boachie,Mieke M.B. Commandeur,Raliat O. Abioye,Edoardo Capuano,Teresa Oliviero,Vincenzo Fogliano,Chibuike C. Udenigwe
出处
期刊:Journal of Agricultural and Food Chemistry [American Chemical Society]
卷期号:69 (36): 10630-10637 被引量:12
标识
DOI:10.1021/acs.jafc.1c03022
摘要

In this study, β-glucan interaction with lentil and yellow pea proteins and the effect on in vitro protein digestibility were investigated. Proteins were mixed with β-glucan at mass ratios of 1:0.5, 1:1, and 1:2. The interaction between β-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 β-glucan formed aggregates with lentil proteins, while the interaction with yellow pea proteins appeared as distinct phases of protein within the β-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 β-glucan mass ratio of 1:2. The findings confirm the possibility to modulate protein digestibility by changing the physical characteristics of a food matrix.
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