Titre du document / Document title

Purification and characterization of an extracellular proline iminopeptidase from Arthrobacter nicotianae 9458

Auteur(s) / Author(s)

SMACCHI E. ⁽¹⁾ ; GOBBETTI M. ⁽²⁾ ; LANCIOTTI R. ⁽²⁾ ; FOX P. F. ⁽³⁾ ;

Affiliation(s) du ou des auteurs / Author(s) Affiliation(s)

⁽¹⁾ Istituto di Industrie Agrarie (Microbiologia), Facoltà di Agraria, Università degli Studi di Perugia, S. Costanzo, 06126 Perugia, ITALIE
⁽²⁾ Stituto di Produzioni e Preparazioni Alimentari, Facoltà di Agraria, Università degli Studi di Bari, Via Napoli 25, 71100 Foggia, ITALIE
⁽³⁾ Department of Food Chemistry, University College Cork, Cork, IRLANDE

Résumé / Abstract

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 I min at 80°C and showed highest activity on Pro-pNA. The proline iminopeptidase was characterized by activity at low temperature, NaCI concentrations up to 7.5% and by high sensitivity to pH values 6.0, serine enzyme inhibitor PMSF and divalent cations, Fe²⁺, Sn²⁺, Cu²⁺, Zn²⁺, Hg²⁺, Co²⁺ and Ni²⁺, The extracellular proline iminopeptidase from A. nicotianae 9458 was able to hydrolyze proline-containing peptides at the pH, temperature and NaCI concentration typical of the surface of smear-ripened cheeses and may contribute to proteolysis of these cheeses during ripening.

Revue / Journal Title

FEMS microbiology letters   ISSN 0378-1097   CODEN FMLED7 

Source / Source

1999, vol. 178, n^o1, pp. 191-197 (27 ref.)

Langue / Language

Anglais

Editeur / Publisher

Blackwell, Oxford, ROYAUME-UNI  (1977) (Revue)

Mots-clés anglais / English Keywords

Prolyl aminopeptidase ; Extracellular ; Purification ; Characterization ; Physicochemical properties ; Enzymatic activity ; Aminopeptidases ; Peptidases ; Hydrolases ; Enzyme ; Arthrobacter ; Actinomycetes ; Bacteria ; Cheese ripening ;

Mots-clés français / French Keywords

Prolyl aminopeptidase ; Extracellulaire ; Purification ; Caractérisation ; Propriété physicochimique ; Activité enzymatique ; Arthrobacter nicotianae ; Aminopeptidases ; Peptidases ; Hydrolases ; Enzyme ; Arthrobacter ; Actinomycetes ; Bactérie ; Affinage fromage ;

Mots-clés espagnols / Spanish Keywords

Prolyl aminopeptidase ; Extracelular ; Purificación ; Caracterización ; Propiedad fisicoquímica ; Actividad enzimática ; Aminopeptidases ; Peptidases ; Hydrolases ; Enzima ; Arthrobacter ; Actinomycetes ; Bacteria ; Curación queso ;

Localisation / Location

INIST-CNRS, Cote INIST : 17567 A, 35400008590318.0270