Abstract
The analysis of a peptic bovine hemoglobin hydrolysate, produced at pilot plant scale, was carried out using two techniques: SE-HPLC and RP-HPLC. Analysis of amino acid composition, second-order derivative spectrometry and FAB mass spectrometry of isolated peptides allowed us to determine the exact positions of these peptides in the sequence of bovine hemoglobin. This, consequently, gave rise to a peptidic map of the hydrolysate. It also revealed, at the same time, some biologically active peptides in the hydrolysate. This information should find use in the potential future application of enzymatic bovine hemoglobin hydrolysate.
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