Two major xylanases of Trichoderma reesei

Maija Tenkanen, Jurgen Puls, Kaisa Poutanen

Research output: Contribution to journalArticleScientificpeer-review

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Abstract

The two main xylanases produced by Trichoderma reesei were purified to electrophoretic homogeneity by ion-exchange and gel chromatography. The enzymes had isoelectric points of 9.0 and 5.5 and their molecular masses were 20 and 19 kDa, respectively. The purified xylanases were most probably distinct gene products, as they were also serologically dissimilar and had different proteolytic cleavage patterns. The pI 9.0 xylanase tolerated higher pH values and temperatures than the pI 5.5 xylanase. Both enzymes clearly preferred polymeric substrates to xylo-oligosaccharides. The substrate preference for polymeric xylans decreased with decreasing substitution (decreasing solubility). The apparent Km values for different xylans varied from 3.0 to 6.8 mg ml-1 for the pI 9.0 xylanase and from 14.8 to 22.3 mg ml-1 for the pI 5.5 xylanase. The pI 9.0 xylanase also showed transxylosidase activity with xylotetraose and xyloheptaose as substrates.
Original languageEnglish
Pages (from-to)566 - 574
JournalEnzyme and Microbial Technology
Volume14
Issue number7
DOIs
Publication statusPublished - 1992
MoE publication typeA1 Journal article-refereed

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Xylans
Trichoderma
Ion Exchange Chromatography
Isoelectric Point
Substrates
Enzymes
Oligosaccharides
Solubility
Gel Chromatography
Molecular mass
Chromatography
Temperature
Ion exchange
Substitution reactions
Gels
Genes

Cite this

Tenkanen, Maija ; Puls, Jurgen ; Poutanen, Kaisa. / Two major xylanases of Trichoderma reesei. In: Enzyme and Microbial Technology. 1992 ; Vol. 14, No. 7. pp. 566 - 574.
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Two major xylanases of Trichoderma reesei. / Tenkanen, Maija; Puls, Jurgen; Poutanen, Kaisa.

In: Enzyme and Microbial Technology, Vol. 14, No. 7, 1992, p. 566 - 574.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Two major xylanases of Trichoderma reesei

AU - Tenkanen, Maija

AU - Puls, Jurgen

AU - Poutanen, Kaisa

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Y1 - 1992

N2 - The two main xylanases produced by Trichoderma reesei were purified to electrophoretic homogeneity by ion-exchange and gel chromatography. The enzymes had isoelectric points of 9.0 and 5.5 and their molecular masses were 20 and 19 kDa, respectively. The purified xylanases were most probably distinct gene products, as they were also serologically dissimilar and had different proteolytic cleavage patterns. The pI 9.0 xylanase tolerated higher pH values and temperatures than the pI 5.5 xylanase. Both enzymes clearly preferred polymeric substrates to xylo-oligosaccharides. The substrate preference for polymeric xylans decreased with decreasing substitution (decreasing solubility). The apparent Km values for different xylans varied from 3.0 to 6.8 mg ml-1 for the pI 9.0 xylanase and from 14.8 to 22.3 mg ml-1 for the pI 5.5 xylanase. The pI 9.0 xylanase also showed transxylosidase activity with xylotetraose and xyloheptaose as substrates.

AB - The two main xylanases produced by Trichoderma reesei were purified to electrophoretic homogeneity by ion-exchange and gel chromatography. The enzymes had isoelectric points of 9.0 and 5.5 and their molecular masses were 20 and 19 kDa, respectively. The purified xylanases were most probably distinct gene products, as they were also serologically dissimilar and had different proteolytic cleavage patterns. The pI 9.0 xylanase tolerated higher pH values and temperatures than the pI 5.5 xylanase. Both enzymes clearly preferred polymeric substrates to xylo-oligosaccharides. The substrate preference for polymeric xylans decreased with decreasing substitution (decreasing solubility). The apparent Km values for different xylans varied from 3.0 to 6.8 mg ml-1 for the pI 9.0 xylanase and from 14.8 to 22.3 mg ml-1 for the pI 5.5 xylanase. The pI 9.0 xylanase also showed transxylosidase activity with xylotetraose and xyloheptaose as substrates.

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DO - 10.1016/0141-0229(92)90128-B

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