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Abstract

The suitability of chicken intestine, a poultry processing by-product, as a source of aminopeptidases has been evaluated. To investigate the heterogeneity of the aminopeptidases in the tissue, tissue fractions separated by differential centrifugation and ion exchange chromatography were screened for aminopeptidase activity using twelve different amino acid naphthylamide substrates. The sedimentable fractions obtained by differential centrifugation, although differing in substrate profile, were largely enriched (72-90%) in aminopeptidase activities. However, the enzymes hydrolysing pro-β-naphthylamide largely belonged to the soluble fraction (> 40%). On the basis of their interaction with the ion exchange resins, DEAE and CM Sepharose, six regions of aminopeptidase activity differing in their elution profiles and substrate specificities were identified. Data reveal the presence of a number of aminopeptidases with multiple specificities in chicken intestine which could be used for industrial applications.