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Variation in seed protein digestion of different pea (Pisum sativumL.) genotypes by cecectomized broiler chickens: 2. Relation betweenin vivoprotein digestibility and pea seed characteristics, and identification of resistant pea polypeptides

Elsevier B.V.
Publication Date
DOI: 10.1016/j.livsci.2007.04.005
  • Broiler Chickens
  • Pisum Sativum
  • Pea Seed Characteristics
  • Trypsin Inhibitor
  • Protein Digestibility
  • Resistant Pea Proteins
  • Biology


Abstract Eight pea genotypes characterized for their major protein fractions were used to investigate the effect of seed protein composition variability on protein digestibility in poultry. These genotypes of various pea types, were also variable in other seed components. They showed variations in their carbohydrate (insoluble fibre compounds, soluble fibre, soluble carbohydrates) and trypsin inhibitor (TI) contents. To exclude the effect of tannins and of particle size, the seeds were dehulled and micro-ground. They were incorporated as the only protein source in isoproteinaceous diets with similar metabolisable energy content and fed to cecectomized chickens. The average amino acid digestibility (apparent and true) and endogenous amino acid excretion were related with pea diet characteristics (protein composition, carbohydrate composition and TI activity). This allowed to precise which of the diet characteristics affect protein digestibility and endogenous excretion. Average apparent digestibility of amino acids was negatively correlated with insoluble fibre components ( R = − 0.71 to − 0.72; p < 0.05) and TI activity ( R = − 0.93; p < 0.001). Average endogenous losses of amino acids were positively correlated with soluble carbohydrate content ( R = 0.77; p < 0.05) and TI activity ( R = 0.84; p < 0.01). Average true digestibility of amino acids was positively correlated with the PA2 albumin level ( R = 0.71; p < 0.05), and negatively with the legumin level ( R = − 0.72; p < 0.05). Resistant peptides extracted from chicken excreta were analysed through electrophoresis and identified by immunodetection. Intensity of detected resistant peptides showed variation among genotypes. However, for the 8 pea genotypes, the pea proteins, which persisted at the end of the digestive tract, were mainly albumin PA1b and lectin. Other minor peptides were also detected: vicilin, albumin PA2 and legumin peptides which migrated at the same level as β-subunits.

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