The influence of the albumin fraction on the bioavailability and postprandial utilization of pea protein given selectively to humans.

Pulse seed proteins such as those found in peas (Pisum sativum) contain fractions of very dissimilar composition and properties, which may therefore be differently utilized by the human body. To analyze the nutritional value of the soluble protein fractions of pea seed, human volunteers ingested a mixed meal of 30 g of raw purified pea protein either as [15N]-globulins (G, n = 9) or as a mix of [15N]-globulins and [15N]-albumins (GA, n = 7) in their natural proportions (22:8). Dietary and endogenous nitrogen fluxes at the terminal ileum were assessed using a tube perfusion technique with an isotopic dilution method. Systemic dietary amino acid availability and the retention of dietary amino acids were determined using 15N enrichment in plasma amino acids and deamination products in blood and urine for 8 h postprandially. The results showed that the pea albumin fraction had the following effects: 1) significantly lowered the real ileal digestibility of pea protein (94 +/- 2.5% for G vs. 89.9 +/- 4% for GA), probably because of a direct effect of trypsin inhibitors; 2) did not promote acute intestinal losses of endogenous nitrogen; and 3) did not significantly improve the postprandial biological value of pea protein (76.5 +/- 3.9% for G vs. 78.7 +/- 3.6% for GA), despite the fact that it corrected the globulin deficiency in sulfur amino acids. We conclude that both G and GA are of good nutritional value for humans and show that cysteine-rich albumins have a far more modest effect on the efficiency of postprandial dietary protein utilization than would be expected from the amino acid scores.