Hydrolysis of alanine oligopeptides by porcine muscle alanyl aminopeptidase

Alanyl aminopeptidase from porcine skeletal muscle was purified and its act ivity against alanine oligopeptides studied using capillary electrophoresis . The purpose was to determine the effect of the chain length of alanine ol igopeptides on aminopeptidase activity. The enzyme showed high specificity against penta- and tetraalanine and absence of activity against dialanine. In this way, dipeptides and free amino acids would be generated in meat pro cessing. Thus, the presence of a specific amino acid on the N-terminal end of a peptide is determinant for the enzyme activity and the length of that peptide also affects the hydrolysis rate.