Variation of in vitro digestibility of pea protein powder dispersions from commercially available sources
Luis Jiménez‐Munoz, M. Torp Nielsen, Laura Román, Milena Corredig
Food Chemistry
Abstract
With raising consumer demand for plant-derived proteins, there has been an increased interest in the utilization of pea ingredients in food formulations. It was hypothesized that differences in processing history and composition affect their colloidal properties and their breakdown during in vitro simulated gastrointestinal digestion. The gastrointestinal fate of three different commercial pea protein ingredients, two protein isolates and one less refined concentrate was compared. The concentrate dispersion showed greater solubility, different protein composition and smaller particle size than the reconstituted pea protein isolates. When heat-treated, the release of free amino groups decreased for the isolates, but increased for the concentrate dispersions. LC-TQMS of free amino acids in the intestinal digestates indicated a significantly higher release of methionine (limiting amino acid in pea protein) in the concentrates than in the isolates. This work highlights the influence of processing and composition on techno-functional and digestion properties of pea ingredients.
Extracted Claims
5 claims extracted from this paper into the knowledge graph
in vitro simulated gastrointestinal digestion affects digestion properties of pea ingredients
“It was hypothesized that differences in processing history and composition affect their colloidal properties and their breakdown during in vitro simulated gastrointestinal digestion.”
heat treatment increases release of free amino groups in concentrate dispersions
“When heat-treated, the release of free amino groups decreased for the isolates, but increased for the concentrate dispersions.”
LC-TQMS analysis indicates higher release of methionine in concentrates
“LC-TQMS of free amino acids in the intestinal digestates indicated a significantly higher release of methionine (limiting amino acid in pea protein) in the concentrates than in the isolates.”