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Titolo:
Isolation and characterisation of a major cellobiohydrolase (S-8) and a major endoglucanase (S-11) subunit from the cellulosome of Clostridium thermocellum
Autore:
Bhat, S; Owen, E; Bhat, MK;
Indirizzi:
Food Res Inst, Food Mat Sci Div, Norwich NR4 7UA, Norfolk, England Food Res Inst Norwich Norfolk England NR4 7UA h NR4 7UA, Norfolk, England Univ Reading, Dept Agr, Reading RG6 6AT, Berks, England Univ Reading Reading Berks England RG6 6AT eading RG6 6AT, Berks, England
Titolo Testata:
ANAEROBE
fascicolo: 3, volume: 7, anno: 2001,
pagine: 171 - 179
SICI:
1075-9964(200106)7:3<171:IACOAM>2.0.ZU;2-Q
Fonte:
ISI
Lingua:
ENG
Soggetto:
ACID-SEQUENCE SIMILARITIES; TRICHODERMA-REESEI; PENICILLIUM-PINOPHILUM; GLYCOSYL HYDROLASES; 3-DIMENSIONAL STRUCTURE; CRYSTAL-STRUCTURE; ESCHERICHIA-COLI; CELLULASE; CLASSIFICATION; PURIFICATION;
Keywords:
Clostridium thermocellum; CBH (S-8); endoglucanase (S-11); thermostability; substrate specificity and mode of action;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
40
Recensione:
Indirizzi per estratti:
Indirizzo: Bhat, MK Food Res Inst, Food Mat Sci Div, Norwich Res Pk, Norwich NR4 7UA,Norfolk,England Food Res Inst Norwich Res Pk Norwich Norfolk England NR4 7UA land
Citazione:
S. Bhat et al., "Isolation and characterisation of a major cellobiohydrolase (S-8) and a major endoglucanase (S-11) subunit from the cellulosome of Clostridium thermocellum", ANAEROBE, 7(3), 2001, pp. 171-179

Abstract

The cellulosome of Clostridium thermocellum was dissociated under mild conditions, and mg quantities of pure cellobiohydrolose (CBH)(dagger) (S-g) and endoglucanase (S-11) were isolated in active form. The CBH (79kDa) and endoglucanase (61 kDa) were optimally active between pH 4.5-6.0 at temperatures of 60 and 70 degreesC, respectively. Between pH 6.0-8.4, the CBH was stable at 60 degreesC for 5 h, whereas the endoglucanase was stable at 70 degreesC for 48 h. Both enzymes were active on natural and derivatised Glc(n), H3PO4-swollen cellulose, Avicel, laminarin, lichenan and barley glucan, while only endoglucanase was active on carboxymethyl (CM)-cellulose and CM-pachyman. Cellobiose inhibited the CBH competitively with a Ki of 0.28 mM. CBHcleaved preferentially either the second (between putative sub-sites -2 and -1 or +1 and +2) or the fourth glycosidic bond (between putative sub-sites -1 and +1) of MeUmbGlc(n) from the non-reducing end, while the endoglucanase required a MeUmbGlC(n) with at least three glycosidic bonds and was specific for internal linkages (between putative sub-sites -1 and +1). (C) 2001 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 11/07/20 alle ore 03:55:34