Open AccessPurification and characterization of an extracellular proline iminopeptidase from Arthrobacter nicotianae 9458
Author(s) -
Smacchi Emanuele,
Gobbetti Marco,
Lanciotti Rosalba,
Fox Patrick F.
Publication year - 1999
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1999.tb13777.x
Subject(s) - proline , extracellular , chemistry , biochemistry , enzyme , proteolysis , pmsf , enzyme assay , chromatography , amino acid
An extracellular proline iminopeptidase, with a molecular mass of about 53 kDa, was purified from Arthrobacter nicotianae 9458 and characterized. The enzyme had temperature and pH optima of 37°C and 8.0, respectively, was completely inactivated by heating for 1 min at 80°C and showed highest activity on Pro‐pNA. The proline iminopeptidase was characterized by activity at low temperature, NaCl concentrations up to 7,5% and by high sensitivity to pH values 6.0, serine enzyme inhibitor PMSF and divalent cations, Fe 2+ , Sn 2+ , Cu 2+ , Zn 2+ , Hg 2+ , Co 2+ and Ni 2+ . The extracellular proline iminopeptidase from A. nicotianae 9458 was able to hydrolyze proline‐containing peptides at the pH, temperature and NaCl concentration typical of the surface of smear‐ripened cheeses and may contribute to proteolysis of these cheeses during ripening.