Effect of carnosine, anserine and other endogenous skeletal peptides on the activity of porcine muscle alanyl and arginyl aminopeptidases

The effect of endogenous dipeptides (carnosine and anserine) and peptidic f ractions from meat extracts on aminopeptidase activity, alanyl and arginyl aminopeptidases purified from porcine skeletal muscle, was studied Carnosin e inhibited the activity of porcine arginyl aminopeptidase (RAP), the inhib ition being stronger with the purified form of the enzyme than in the muscl e extract. The RAP inhibition was competitive. One of the peptidic fraction s isolated from meat extracts inhibited RAP activity but the degree of inhi bition depended on the extent of purification. The major aminopeptidase pre sent in muscle, alanyl aminopeptidase (AAP), was neither inhibited by natur al dipeptides nor any of the peptidic fractions. The study of meat inhibito ry peptides provides a better understanding of the action of proteolytic en zymes during meat processing.