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Journal of Dairy Science Vol. 77 No. 10 2880-2889
© 1994 by American Dairy Science Association ®
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Purification and Characterization of a General Aminopeptidase (St-PepN) from Streptococcus salivarius ssp. thermophilus CNRZ 302

Francoise Rul 1, Veronique Monnet 1, and Jean-Claude Gripon 1

1 Unité d'Enzymologie, Station de Recherches Laitières, lnstitut National de la Recherche Agronomique, 78352 Jouy-en-Josas, Cedex, France

A general aminopeptidase (St-PepN) was purified from an intracellular extract of Streptococcus salivarius ssp. thermophilus CNRZ 302 by ion-exchange chromatography and hydrophobic interaction chromatography. Gel electrophoresis of the purified enzyme in denaturing or nondenaturating conditions showed a single protein band. The enzyme is a monomer with a molecular mass of 97 kDa. Its activity is maximal at pH 7 and 36°C and is completely abolished by CuCl2 and ZnCl2. The enzyme is strongly inhibited by metalchelating reagents, such as EDTA and o-phenanthroline, which suggests that St-PepN is a metalloenzyme. The enzyme showed activity toward p-nitroanilide derivatives or dipeptides and tripeptides and showed a preference for hydrophobic or basic amino acids at the N-terminal position, Longer peptide chains, such as the B-chain of insulin, glucagon, or peptides generated by the hydrolysis of caseins, were degraded, too. The sequence of the first 21 residues of the mature enzyme was determined and showed high homology with that of the aminopeptidase PepN isolated from Lactococcus lactis ssp. cremoris Wg2. The properties of the enzyme are compared with those of corresponding enzymes of other species of lactic acid bacteria.

Key Words: aminopeptidase • Streptococcus salivarius ssp. thermophilus • lactic acid bacteria

Submitted on November 22, 1993
Accepted on May 2, 1994




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