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Titolo:
Purification and characterization of an extracellular proline iminopeptidase from Arthrobacter nicotianae 9458
Autore:
Smacchi, E; Gobbetti, M; Lanciotti, R; Fox, PF;
Indirizzi:
Univ Perugia, Fac Agr, Ist Ind Agr Microbiol, I-06126 Perugia, Italy Univ Perugia Perugia Italy I-06126 Agr Microbiol, I-06126 Perugia, Italy Univ Bari, Fac Agr, Ist Prod & Preparaz Alimentari, I-71100 Foggia, Italy Univ Bari Foggia Italy I-71100 reparaz Alimentari, I-71100 Foggia, Italy Natl Univ Ireland Univ Coll Cork, Dept Food Chem, Cork, Ireland Natl Univ Ireland Univ Coll Cork Cork Ireland Food Chem, Cork, Ireland
Titolo Testata:
FEMS MICROBIOLOGY LETTERS
fascicolo: 1, volume: 178, anno: 1999,
pagine: 191 - 197
SICI:
0378-1097(19990901)178:1<191:PACOAE>2.0.ZU;2-S
Fonte:
ISI
Lingua:
ENG
Soggetto:
LACTOBACILLUS-HELVETICUS; BREVIBACTERIUM-LINENS; CHEESE; BACTERIA; MICROFLORA; PEPTIDASE; PROTEINS; FLORA;
Keywords:
peptidase; proline iminopeptidase; smear surface-ripened cheese; Arthrobacter;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
27
Recensione:
Indirizzi per estratti:
Indirizzo: Gobbetti, M Univ Perugia, Fac Agr, Ist Ind Agr Microbiol, I-06126 Perugia,Italy Univ Perugia Perugia Italy I-06126 l, I-06126 Perugia, Italy
Citazione:
E. Smacchi et al., "Purification and characterization of an extracellular proline iminopeptidase from Arthrobacter nicotianae 9458", FEMS MICROB, 178(1), 1999, pp. 191-197

Abstract

An extracellular proline iminopeptidase, with a molecular mass of about 53kDa, was purified from Arthrobacter nicotianae 9458 and characterized. Theenzyme had temperature and pH optima of 37 degrees C and 8.0, respectively, was completely inactivated by healing for 1 min at 80 degrees C and showed highest activity on Pro-pNA. The proline iminopeptidase was characterizedby activity at low temperature, NaCl concentrations up to 7.5% and by highsensitivity 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 NaCl concentration typical of the surface of smear-ripened cheeses and may contribute to proteolysis of these cheeses during ripening. (C) 1999 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 15/07/20 alle ore 12:23:09