Metabolic fates of U-14C-labelled monosaccharides and an enzyme-treated cell-wall substrate in the fowl.

A major benefit of supplementing non-ruminant feedstuffs with exogenous enzymes is presumed to be the degradation of plant cell-wall polysaccharides to metabolizable monosaccharide residues. In the present study, metabolic fates of (U-14C-labelled, 10 mM) glucose, galactose, mannose, xylose and arabinose were compared in the fowl, by measuring recoveries of 14C radioactivity in exhaled carbon dioxide excreta and body tissues after administration either by wing vein (iv) or into the crop (ic). A further comparison was made with a tube-fed, enzyme-treated, U-14C-labelled cell-wall substrate, Festuca arundinacea, and a final experiment tested possible competition for absorption between different cell-wall residues. Delays between iv and ic treatments in recovery of 14C in CO2, which were assumed to reflect intestinal absorption, indicated that xylose was absorbed more slowly than glucose and galactose, but faster than mannose and arabinose. Total recoveries of 14C in CO2 and excreta over the whole test period indicated that metabolizabilities were highest with glucose, galactose and mannose, and lowest with arabinose. After testing, 14C recovery in caecal contents was highest with ic arabinose, and recoveries in body tissues, with all sugar treatments, were in the order liver greater than breast and leg muscle greater than abdominal fat greater than plasma. Results with the Festuca substrate showed similar patterns of recovery in body tissues and confirmed an increase in metabolizability with addition of enzyme. The timing of the 14CO2 response with Festuca and a wet enzyme pretreatment was broadly similar to a 'predicted Festuca' response, based on the composition of the substrate and the measured responses with individual (ic) monosaccharides. There was no evidence of any competition for absorption or metabolism among cell-wall residues. It was concluded that glucose release from cellulose is potentially the most important product of cell-wall degradation to contribute to enzyme enhancement of metabolizable energy.