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Titolo:
Subcellular distribution of glycanases and related components in Ruminococcus albus SY3 and their role in cell adhesion to cellulose
Autore:
Miron, J; Jacobovitch, J; Bayer, EA; Lamed, R; Morrison, M; Ben-Ghedalia, D;
Indirizzi:
Agr Res Org, Volcani Ctr, Metab Unit, IL-50250 Bet Dagan, Israel Agr Res Org Bet Dagan Israel IL-50250 b Unit, IL-50250 Bet Dagan, Israel Weizmann Inst Sci, Dept Biol Chem, IL-76100 Rehovot, Israel Weizmann Inst Sci Rehovot Israel IL-76100 Chem, IL-76100 Rehovot, Israel Tel Aviv Univ, Ctr Biotechnol, IL-69978 Tel Aviv, Israel Tel Aviv Univ Tel Aviv Israel IL-69978 echnol, IL-69978 Tel Aviv, Israel Ohio State Univ, Dept Anim Sci, Columbus, OH 43210 USA Ohio State Univ Columbus OH USA 43210 pt Anim Sci, Columbus, OH 43210 USA
Titolo Testata:
JOURNAL OF APPLIED MICROBIOLOGY
fascicolo: 4, volume: 91, anno: 2001,
pagine: 677 - 685
SICI:
1364-5072(200110)91:4<677:SDOGAR>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
FIBROBACTER-INTESTINALIS DR7; SURFACE-STRUCTURES; RUMEN BACTERIA; PROTEINS; WALL; ADHERENCE; MUTANT;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
26
Recensione:
Indirizzi per estratti:
Indirizzo: Miron, J Agr Res Org, Volcani Ctr, Metab Unit, POB 6, IL-50250 Bet Dagan, Israel Agr Res Org POB 6 Bet Dagan Israel IL-50250 50 Bet Dagan, Israel
Citazione:
J. Miron et al., "Subcellular distribution of glycanases and related components in Ruminococcus albus SY3 and their role in cell adhesion to cellulose", J APPL MICR, 91(4), 2001, pp. 677-685

Abstract

Aims: To compare the subcellular distribution of glycanase-related components between wildtype Ruminococcus albus SY3 and an adhesion-defective mutant, to identify their possible contribution to the adhesion process, and to determine their association with cellulosome-like complexes. Methods and Results: Cell fractionation revealed that most of the cellulases and xylanases were associated with capsular and cell-wall fractions. SDS-PAGE and gel filtration indicated that most of the bacterial enzyme activity was not integrated into cellulosome-like complexes. The adhesion-defective mutant produced significantly less (5- to 10-fold) overall glycanase activity, and the 'true cellulase activity' appeared to be entirely confined to the cell membrane fractions. Antibodies specific for the cellulosomal scaffoldin of Clostridium thermocellum recognized a single 240 kDa band in R. albus SY3. Conclusions: The adhesion-defective mutant appeared to be blocked in exocellular transport of enzymes involved in true cellulase activity. A potential cellulosomal scaffoldin candidate was identified in R. albus SY3. Significance and Impact of the Study: Several glycanase-related proteins and more than one mechanism appear to be involved in the adhesion of R. albus SY3 tocellulose.

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Documento generato il 02/04/20 alle ore 05:59:05