InquilineKea Posted August 8, 2021 Report Share Posted August 8, 2021 (edited) " Wheat gluten is the plant-based protein with the lowest PDCAAS value at just 25% (Table 1). " from https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6723444/ ^hmm, this makes me want to eat more gluten! low protein digestibility means you feel full after eating them *AND* they don't stimulate mTOR as much same with peanut protein powder a la https://www.amazon.com/PB2-Performance-Peanut-Protein-Powder/dp/B07Y5H8K5D Quote Proline-rich stretches on protein sequences typically reduce the flexibility of the protein chain and are known for their high resistance against peptidase hydrolysis. Gluten proteins, for example, are characterized by high proline levels, which is one of the reasons for its limited digestibility. Tight protein folding or protein aggregation generally restrict access to the peptide chain, and, hence, slow down hydrolysis. Factors affecting protein solubility also influence protein digestibility. Martinez-Velasco and colleagues , while studying the digestibility of proteins in maize tortillas during storage, described a negative correlation between protein digestibility and the level of secondary beta-conformations (i.e., beta-sheet and beta-turn conformations) . The limited digestibility of these secondary structures was ascribed to their high hydrophobicity. Both beta-sheet and beta-turn structures were shown to play a crucial role in the formation of a viscoelastic wheat flour dough . At a higher structural level, crosslinking within and between single proteins drastically affects protein digestibility. Geiger and Harris  studied the digestibility of wool protein by pepsin. Wool protein is characterised by a dense network structure of peptide chains that are joined through disulfide crosslinks. The reduction of these disulfide bridges, followed by subsequent (partial) reoxidation, showed that the digestibility of those samples with low crosslinking degree was much higher than those proteins that were crosslinked to a greater extent. Upon breadmaking, disulifide bond formation plays a crucial role to dough viscoelasticity and gas retention capacity and final bread quality [37,38]. Quote The most well-described antinutritional factors found in plants (and (pseudo)cereals) that limit protein digestibility are protease inhibitors (e.g., trypsin and chymotrypsin inhibitors), tannins and phytates [8,39,40]. Haemagglutinins/lectins in legumes and cereals, glucosinolates in mustard and canola protein products, gossypol in cottonseed protein products, saponins in legumes, oats and tea, and uricogenic nucleic acid bases in yeast protein products are a few other examples [8,41]. Lectins, i.e., noncatalytic sugar-binding proteins, interfere with protein hydrolysis and are themselves known for their high resistance to proteolysis and stability over a wide pH range Edited August 8, 2021 by InquilineKea Quote Link to comment Share on other sites More sharing options...
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