In vitro protein digestive properties and peptidomic characterization of five whole component plant protein beverages using a pepsin-pancreatin model

Abstract

Plant protein has received great attention for its potential nutrition and health benefits. In this study, the digestive properties and peptidomics of whole component plant protein beverages from soybean, chick pea, pea, oat, and quinoa were characterized using an in vitro pepsin-pancreatin digestion model. The study found that quinoa beverage had a higher in vitro protein digestibility (80.49 %), followed by pea, soybean, chick pea, and oat beverage (79.25–70.89 %). Additionally, quinoa and soybean beverage showed comparably higher in vitro digestible indispensable amino acid score (DIAAS) of 81–97, while chick pea and pea beverage had lower in vitro DIAAS of 58–79 due to low concentration of sulfur-containing AA (SAA). Meanwhile, peptides with molecular weight (MW) below 1 kDa occupied more than 93 % of the digested fraction in quinoa beverage, which might result in its higher DPPH scavenging activity, ABTS scavenging activity and ACE inhibitory activity with the IC50 value of 2.80, 0.20 and 0.90 mg/mL, respectively. Peptidomics characterization combined with rapid screening by PeptideRanker and BIOPEP database further suggested that cereals, especially oat and quinoa, released potentially bioactive peptides with a higher percentage (30.89 % and 22.81 %, respectively) compared to legumes like soybean and chick pea (13.30–18.52 %). Additionally, the identified active peptides were more likely to be derived from globular proteins. The methods and data here provided a reference for a better understanding of the digestive properties and nutritional recommendations of whole component plant protein product.