Aims: To study the properties and show the potential application of a glycine aminopeptidase from Actinomucor elegans. Methods and Results: The enzyme was estimated to have molecular mass of 320 kDa by gel filtration and the subunit size of 56.5 kDa by SDS-PAGE. It hydrolysed glycine from substrate more efficiently than other amino acids. The optimal temperature for this enzyme was 40degreesC and at pH 8.0 it showed its highest activity. The K-m and K-cat of the enzyme for glycine-beta-naphthylamine was 0.24 mm and 100.8 s(-1), respectively. Zinc, copper, cadmium and o-phenanthrolin suppressed almost all enzyme activities at the concentration of 1.0 mm. In the process of hydrolysing proteins, it could improve the protease activity considerably. Conclusions: It was a hexamer metalloenzyme which was specific for the substrates with glycinse residue at the N-terminal and some metal cations were needed to maintain its activity. Significance and Impact of the Study: This study demonstrates the properties of a novel aminopeptidase and shows its potential application in the process of the food industry.