Tryptophan analysis in feed, food and pharmaceutical samples
Tryptophan is detectable as free amino acid, but is also bound in peptides or proteins. Free tryptophan can be detected in vegetable and physiological fluids, but also in feed and food samples. The bound tryptophan in peptides and proteins has to be liberated by alkaline hydrolysis. Acid hydrolysis is not advised, because tryptophan is acid labile. Ansynth Service B.V. is specialized in the analysis of free tryptophan and in the analysis of tryptophan bound in peptides and proteins after alkaline hydrolysis. If in the sequence of a peptide or protein valine, leucine or isoleucine are directly bound to tryptophan, then even after alkaline hydrolysis the dipeptides of tryptophan Val-Trp, Leu-Trp or Ile-Trp will remain. Ansynth Service B.V. can also estimate the dipeptide bound tryptophan by quantitative analysis of these dipeptides.