Binding of hemicellulases on isolated polysaccharide substrates

Maija Tenkanen (Corresponding Author), Johanna Buchert, Liisa Viikari

Research output: Contribution to journalArticleScientificpeer-review

45 Citations (Scopus)

Abstract

Binding of five fungal xylanases produced by Trichoderma reesei, Aspergillus oryzae, and Aspergillus fumigatus and two mannanases of Bacillus subtilis and T. reesei on insoluble xylan, mannan, and cellulose was studied at different pH values and ionic strengths.
For comparison, the binding of cellobiohydrolase I (CBH I) and endoglucanase (EG I) of T. reesei on the same substrates was examined. Ionic interactions appeared to play an important role in the binding of xylan, as most of the enzymes were totally bound on xylan when the pH was below their isoelectric point but remained mainly unbound at pH values above the isoelectric point.
The binding on xylan was also clearly sensitive to ionic strength. The xylanases were also incompletely bound on mannan and cellulose, and the two mannanases tested were partially bound on mannan. The two cellulolytic enzymes of T. reesei used in this work are both known to contain a cellulose binding domain and were efficiently bound on cellulose. Interestingly, T. reesei mannanase was also found to bind readily on cellulose.
Thus, it most probably contains, instead of a mannan binding domain, a specific cellulose binding domain.
Original languageEnglish
Pages (from-to)499-505
JournalEnzyme and Microbial Technology
Volume17
Issue number6
DOIs
Publication statusPublished - 1995
MoE publication typeA1 Journal article-refereed

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Polysaccharides
Cellulose
Mannans
Xylans
Substrates
Aspergillus
Isoelectric Point
Ionic strength
Osmolar Concentration
Enzymes
Cellulose 1,4-beta-Cellobiosidase
Aspergillus oryzae
Cellulases
Trichoderma
Aspergillus fumigatus
Cellulase
Bacilli
Bacillus subtilis
hemicellulase

Cite this

Tenkanen, Maija ; Buchert, Johanna ; Viikari, Liisa. / Binding of hemicellulases on isolated polysaccharide substrates. In: Enzyme and Microbial Technology. 1995 ; Vol. 17, No. 6. pp. 499-505.
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abstract = "Binding of five fungal xylanases produced by Trichoderma reesei, Aspergillus oryzae, and Aspergillus fumigatus and two mannanases of Bacillus subtilis and T. reesei on insoluble xylan, mannan, and cellulose was studied at different pH values and ionic strengths. For comparison, the binding of cellobiohydrolase I (CBH I) and endoglucanase (EG I) of T. reesei on the same substrates was examined. Ionic interactions appeared to play an important role in the binding of xylan, as most of the enzymes were totally bound on xylan when the pH was below their isoelectric point but remained mainly unbound at pH values above the isoelectric point. The binding on xylan was also clearly sensitive to ionic strength. The xylanases were also incompletely bound on mannan and cellulose, and the two mannanases tested were partially bound on mannan. The two cellulolytic enzymes of T. reesei used in this work are both known to contain a cellulose binding domain and were efficiently bound on cellulose. Interestingly, T. reesei mannanase was also found to bind readily on cellulose. Thus, it most probably contains, instead of a mannan binding domain, a specific cellulose binding domain.",
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Binding of hemicellulases on isolated polysaccharide substrates. / Tenkanen, Maija (Corresponding Author); Buchert, Johanna; Viikari, Liisa.

In: Enzyme and Microbial Technology, Vol. 17, No. 6, 1995, p. 499-505.

Research output: Contribution to journalArticleScientificpeer-review

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T1 - Binding of hemicellulases on isolated polysaccharide substrates

AU - Tenkanen, Maija

AU - Buchert, Johanna

AU - Viikari, Liisa

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AB - Binding of five fungal xylanases produced by Trichoderma reesei, Aspergillus oryzae, and Aspergillus fumigatus and two mannanases of Bacillus subtilis and T. reesei on insoluble xylan, mannan, and cellulose was studied at different pH values and ionic strengths. For comparison, the binding of cellobiohydrolase I (CBH I) and endoglucanase (EG I) of T. reesei on the same substrates was examined. Ionic interactions appeared to play an important role in the binding of xylan, as most of the enzymes were totally bound on xylan when the pH was below their isoelectric point but remained mainly unbound at pH values above the isoelectric point. The binding on xylan was also clearly sensitive to ionic strength. The xylanases were also incompletely bound on mannan and cellulose, and the two mannanases tested were partially bound on mannan. The two cellulolytic enzymes of T. reesei used in this work are both known to contain a cellulose binding domain and were efficiently bound on cellulose. Interestingly, T. reesei mannanase was also found to bind readily on cellulose. Thus, it most probably contains, instead of a mannan binding domain, a specific cellulose binding domain.

U2 - 10.1016/0141-0229(94)00050-2

DO - 10.1016/0141-0229(94)00050-2

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