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Titolo:
ANALYSIS OF A CELLODEXTRINASE CLONED FROM RUMINOCOCCUS-FLAVEFACIENS FD-1
Autore:
BROWN GD; JORGENSEN T; MORRIS EJ; THOMSON JA;
Indirizzi:
UNIV CAPE TOWN,DEPT MICROBIOL RONDEBOSCH 7700 SOUTH AFRICA UNIV CAPE TOWN,DEPT MICROBIOL RONDEBOSCH 7700 SOUTH AFRICA
Titolo Testata:
FEMS microbiology letters
fascicolo: 1, volume: 111, anno: 1993,
pagine: 57 - 61
SICI:
0378-1097(1993)111:1<57:AOACCF>2.0.ZU;2-H
Fonte:
ISI
Lingua:
ENG
Soggetto:
BACTEROIDES-SUCCINOGENES; ESCHERICHIA-COLI; MOLECULAR-CLONING; EXPRESSION; GENE; PURIFICATION; ENZYMES;
Keywords:
RUMINOCOCCUS-FLAVEFACIENS; CELLULASE; CELLODEXTRINASE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
22
Recensione:
Indirizzi per estratti:
Citazione:
G.D. Brown et al., "ANALYSIS OF A CELLODEXTRINASE CLONED FROM RUMINOCOCCUS-FLAVEFACIENS FD-1", FEMS microbiology letters, 111(1), 1993, pp. 57-61

Abstract

A cellulase gene from Ruminococcus flavefaciens FD-1 had previously been cloned in Escherichia coli. The product of this gene, CelA, was purified from E. coli and characterised. This 39 kDa cellulase is antigenically related. and of similar mass. to a protein in R. flavefaciens. The enzyme has cellodextrinase activity with predominantly exo-type action. CelA activity was optimal at pH 6.5 and 41-degrees-C, and was inhibited in the presence of divalent metal cations. The K(m) and V(max) were determined as 0.68 mM and 1.89 mumol min-1 mg-1 of CelA, respectively. Cellobiose was the major end product of cellodextrin hydrolysis, and our results suggest that cellobiose is a competitive inhibitor of CelA.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 27/11/20 alle ore 13:46:32