In vitro gastro-small intestinal digestion of conventional and mildly processed pea protein ingredients. (1st September 2022)

• Record Type: Journal Article
• Authors: Rivera del Rio, Andrea; Möller, Anna C.; Boom, Remko M.; Janssen, Anja E.M.
• Is Part Of: Food chemistry. Volume 387(2022)
• Publication Date: 2022-09-01
• Subjects: DH degree of hydrolysis -- GE gastric emptying -- NSPF non-soluble protein fraction -- PPI pea protein isolate -- PRF protein-rich fraction -- SPF soluble protein fraction -- TIU trypsin inhibitory units; Protein digestion -- Semi-dynamic in vitro digestion -- Mild fractionation -- Plant protein -- Pea protein isolate -- Heat treatment; Food -- Analysis -- Periodicals; Food -- Composition -- Periodicals; 664
• DOI: 10.1016/j.foodchem.2022.132894
• Languages: English
• ISSNs: 0308-8146

Abstract

Highlights: The digestibility of pea proteins depends on their processing history. The digestibility of native pea proteins can be improved by heat treatment. Mild and conventional pea protein fractions have comparable digestibilities. Longer residence time in the gastric phase enhances digestion by pancreatic enzymes. Abstract: We report on the effect of processing, particularly heating, on the digestion dynamics of pea proteins using the standardised semi-dynamic in vitro digestion method. Fractions with native proteins were obtained by mild aqueous fractionation of pea flour. A commercial pea protein isolate was chosen as a benchmark. Heating dispersions of pea flour and mild protein fractions reduced the trypsin inhibitory activity to levels similar to that of the protein isolate. Protein-rich and non-soluble protein fractions were up to 18% better hydrolysed after being thermally denatured, particularly for proteins emptied later in the gastric phase. The degree of hydrolysis throughout the digestion was similar for these heated fractions and the conventional isolate. Further heating of the protein isolate reduced its digestibility as much as 9%. Protein solubility enhances the digestibility of native proteins, while heating aggregates the proteins, which ultimately reduces the achieved extent of hydrolysis from gastro-small intestinal enzymes.