Gastrointestinal and Colonic Metabolism of Different Types of Pea Proteins: Analysis of Structures and Metabolites

This study systematically evaluated the gastrointestinal fate of pea 7S, 11S globulin, and pea protein isolate (PPI) and their impact on gut using INFOGEST digestion, fecal fermentation, and multiomics approaches. During the gastrointestinal stage, pea proteins were largely digested, while pea 7S globulins and PPI exhibited partial resistance to gastric digestion. Intestinal digestion significantly enhanced Lys bioavailability, although Met remained as the first limiting amino acid across all pea proteins. During <i>in vitro</i> fermentation inoculated with microbiota from hyperuricemic individuals, pea proteins significantly reduced the production of trimethylamine <i>N</i>-oxide (TMAO) and guanosine relative to beef protein. Concurrently, pea protein supplementation promoted the generation of short-chain fatty acids and selectively enriched beneficial populations of gut microbiota such as <i>Phascolarctobacterium</i> and <i>Akkermansia</i>. Spearman correlation revealed that amino acid composition of pea proteins significantly affected microbial composition and gut-produced metabolites. Our results elucidate the structural-digestive-microbial interactions of pea proteins.