Digestibility of cooked and raw egg protein in humans as assessed by stable isotope techniques.

Egg proteins contribute substantially to the daily nitrogen allowances in Western countries and are generally considered to be highly digestible. However, information is lacking on the true ileal digestibility of either raw or cooked egg protein. The recent availability of stable isotope-labeled egg protein allowed determination of the true ileal digestibility of egg protein by means of noninvasive tracer techniques. Five ileostomy patients were studied, once after ingestion of a test meal consisting of 25 g of cooked 13C- and 15N-labeled egg protein, and once after ingestion of the same test meal in raw form. Ileal effluents and breath samples were collected at regular intervals after consumption of the test meal and analyzed for 15N- and 13C-content, respectively. The true ileal digestibility of cooked and raw egg protein amounted to 90.9 +/- 0.8 and 51.3 +/- 9.8%, respectively. A significant negative correlation (r = -0.92, P < 0.001) was found between the 13C-recovery in breath and the recovery of exogenous N in the ileal effluents. In summary, using the 15N-dilution technique we demonstrated that the assimilation of cooked egg protein is efficient, albeit incomplete, and that the true ileal digestibility of egg protein is significantly enhanced by heat-pretreatment. A simple 13C-breath test technique furthermore proved to be a suitable alternative for the evaluation of the true ileal digestibility of egg protein.