Abstract
The aim of this work was to evaluate the impact of incorporating different legume flours (faba bean, lentil or split pea flours) on the pasta protein network and its repercussion on in vitro protein digestibility, in comparison with reference dairy proteins. Kinetics and yields of protein hydrolysis in legume enriched pasta and, for the first time, the peptidomes generated by the pasta at the end of the in vitro gastric and intestinal phases of digestion are presented. Three isoproteic (21%) legume enriched pasta with balanced essential amino acids, were made from wheat semolina and 62% to 79% of legume flours (faba bean or F-pasta; lentil or L-pasta and split pea or P-pasta). Pasta were prepared following the conventional pastification steps (hydration, mixing, extrusion, drying, cooking). Amino acid composition and protein network structure of the pasta were determined along with their culinary and rheological properties and residual trypsin inhibitor activity (3–5% of the activity initially present in raw legume flour). F- and L-pasta had contrasted firmness and proportion of covalently linked proteins. F-pasta had a generally weaker protein network and matrix structure, however far from the weakly linked soluble milk proteins (SMP) and casein proteins, which in addition contained no antitrypsin inhibitors and more theoretical cleavage sites for digestive enzymes. The differences in protein network reticulation between the different pasta and between pasta and dairy proteins were in agreement in each kinetic phase with the yield of the in vitro protein hydrolysis, which reached 84% for SMP, and 66% for casein at the end of intestinal phase, versus 50% for L- and P-pasta and 58% for F-pasta. The peptidome of legume enriched pasta is described for the first time and compared with the peptidome of dairy proteins for each phase of digestion. The gastric and intestinal phases were important stages of peptide differentiation between legumes and wheat. However, peptidome analysis revealed no difference in wheat-derived peptides in the three pasta diets regardless of the digestion phase, indicating that there was a low covalent interaction between wheat gluten and legume proteins.
Highlights
Diversifying protein sources in food intake, increasing the consumption of vegetable proteins could reduce the risks to health and to the environment associated with the production and the excessive consumption of animal proteins in Western countries [1,2]
In comparison to pasta diets, casein and soluble milk proteins (SMP) diets were richer in most amino acids except for cysteine, which was equivalent in the casein diet, and phenylalanine, which was present in lower amounts in SMP
Much higher lysine concentration were found in milk protein diets, especially in SMP diet, whereas tyrosine was more concentrated in the casein diet
Summary
Diversifying protein sources in food intake, increasing the consumption of vegetable proteins could reduce the risks to health and to the environment associated with the production and the excessive consumption of animal proteins in Western countries [1,2]. Wheat proteins are mainly composed of glutenins soluble in acid or alkali solutions, and gliadins, which are soluble in hydro-alcoholic solutions. These proteins form inter- and intra-molecular disulfide bonds during food processing, leading to the formation of a three dimensional gluten network [8]. Enzyme-inhibitors and lectins, all involved in seed defense mechanisms, are present in legumes and are anti-nutritional factors in the human diet. Depending on their sedimentation coefficient, legume proteins are classified as legumin (globulin 11S), vicilin and convicilin (globulin 7S) and albumin (2S)
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