Abstract
High pH employed during the guanidination process (conversion of lysine residues to homoarginine) and its possible effects on racemization of amino acid residues to D-forms and on amino acid digestibility are concerns often raised with the use of guanidinated proteins to estimate endogenous amino acid losses in monogastric animals. The objective of the present study was to investigate the influence of guanidination on apparent ileal amino acid digestibility of casein, soybean meal, cottonseed meal, and canola meal for broiler chickens. Apparent ileal digestibility of amino acids in guanidinated and unreacted proteins, with few exceptions, were found to be remarkably similar. These results suggest that the guanidination process has no influence on the susceptibility of proteins to proteolysis and that racemization is not a practical problem when the proteins are guanidinated at low temperatures.
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