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Titolo:
PARTIAL-PURIFICATION AND CHARACTERIZATION OF A PROTEINASE FROM BREVIBACTERIUM-LINENS
Autore:
CLANCY M; OSULLIVAN M;
Indirizzi:
NATL UNIV IRELAND UNIV COLL DUBLIN,DEPT FOOD SCI DUBLIN 4 IRELAND
Titolo Testata:
Irish journal of agricultural and food research
fascicolo: 2, volume: 32, anno: 1993,
pagine: 185 - 194
SICI:
0791-6833(1993)32:2<185:PACOAP>2.0.ZU;2-E
Fonte:
ISI
Lingua:
ENG
Keywords:
BREVIBACTERIUM-LINENS; PROTEINASE; SURFACE-RIPENED CHEESE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
NO
Recensione:
Indirizzi per estratti:
Citazione:
M. Clancy e M. Osullivan, "PARTIAL-PURIFICATION AND CHARACTERIZATION OF A PROTEINASE FROM BREVIBACTERIUM-LINENS", Irish journal of agricultural and food research, 32(2), 1993, pp. 185-194

Abstract

A thermostable extracellular proteinase from the culture filtrate of a strain of Brevibacterium linens, isolated from a bacterial surface-ripened cheese, was partially purified and characterised. The enzyme had a molecular weight of 18.5 kDa as determined by gel filtration. The optimum pH and temperature on azocasein were 7.5 and 67.5-degrees-C, respectively, and the enzyme remained stable over a pH range of 2 to 12. It was inactivated by n-ethylmalemide and had a decimal reduction time of 72 min at 70-degrees-C. The kinetics of inactivation were biphasic, yielding energies of inactivation of 405.8 and 120.3 kJ/mol for the temperature ranges of 62.5 to 70-degrees-C and 70 to 80-degrees-C, respectively. The enzyme hydrolysed both alpha-S1 and beta-caseins to products which included peptides of relatively high molecular weight.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 07/08/20 alle ore 21:16:18