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

被引:16
作者
Boachie, Ruth T. [1 ,2 ]
Commandeur, Mieke M. B. [1 ,2 ]
Abioye, Raliat O. [3 ]
Capuano, Edoardo [2 ]
Oliviero, Teresa [2 ]
Fogliano, Vincenzo [2 ]
Udenigwe, Chibuike C. [1 ,3 ]
机构
[1] Univ Ottawa, Fac Hlth Sci, Sch Nutr Sci, Ottawa, ON K1H 8M5, Canada
[2] Wageningen Univ & Res, Food Qual & Design Grp, POB 8129, NL-6700 EV Wageningen, Netherlands
[3] Univ Ottawa, Fac Sci, Dept Chem & Biomol Sci, Ottawa, ON K1N 6N5, Canada
基金
加拿大自然科学与工程研究理事会;
关键词
yellow pea protein; lentil protein; beta-glucan; protein-fiber interaction; protein digestibility; simulated gastrointestinal digestion; fluorescence microscopy; FUNCTIONAL-PROPERTIES; FOOD; PH; EXTRACTION; COMPLEXES; ULTRASOUND; LEGUMIN;
D O I
10.1021/acs.jafc.1c03022
中图分类号
S [农业科学];
学科分类号
09 ;
摘要
In this study, beta-glucan interaction with lentil and yellow pea proteins and the effect on in vitro protein digestibility were investigated. Proteins were mixed with beta-glucan at mass ratios of 1:0.5, 1:1, and 1:2. The interaction between beta-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 beta-glucan formed aggregates with lentil proteins, while the interaction with yellow pea proteins appeared as distinct phases of protein within the beta-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 beta-glucan mass ratio of 1:2. The findings confirm the possibility to modulate protein digestibility by changing the physical characteristics of a food matrix.
引用
收藏
页码:10630 / 10637
页数:8
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