Purification and characterization of a thermophilic xylanase from the brown-rot fungus Gloeophyllum trabeum

Anne-Christine Ritschkoff (Corresponding Author), Johanna Buchert, Liisa Viikari

Research output: Contribution to journalArticleScientificpeer-review

25 Citations (Scopus)

Abstract

A xylanase produced by the brown-rot fungus, Gloeophyllum trabeum, was purified to electrophoretic homogeneity by ion-exchange chromatography and gel filtration. The enzyme had an isoelectric point of 5.0 and molecular mass of 39–42 kDa, respectively. The xylanase appeared to prefer the most substituted glucurono-xylan (DMSO-xylan) as substrate and exhibited a pH optimum of 4.0 and a temperature optimum of 80°C after 30 min incubation. Approximately 22% of the activity remained after 2 h incubation at 70°C and the half-life of xylanase at 60°C was 24 h. The xylanase also showed β-glucanase activity with barley β-glucan as substrate as side activity. The xylanase of G. trabeum was very tolerant to inhibitors. Among the various inhibitors studied, only 10 mM AlCl3 was found to inhibit the xylanase activity.
Original languageEnglish
Pages (from-to)67-74
Number of pages8
JournalJournal of Biotechnology
Volume32
Issue number1
DOIs
Publication statusPublished - 1994
MoE publication typeA1 Journal article-refereed

Fingerprint

Xylans
Fungi
Purification
Glucans
Ion Exchange Chromatography
Isoelectric Point
Molecular mass
Substrates
Hordeum
Chromatography
Dimethyl Sulfoxide
Gel Chromatography
Half-Life
Ion exchange
Gels
Enzymes
Temperature
aluminum chloride

Cite this

@article{4fe3a3c105044923bc50cff5dc6d8879,
title = "Purification and characterization of a thermophilic xylanase from the brown-rot fungus Gloeophyllum trabeum",
abstract = "A xylanase produced by the brown-rot fungus, Gloeophyllum trabeum, was purified to electrophoretic homogeneity by ion-exchange chromatography and gel filtration. The enzyme had an isoelectric point of 5.0 and molecular mass of 39–42 kDa, respectively. The xylanase appeared to prefer the most substituted glucurono-xylan (DMSO-xylan) as substrate and exhibited a pH optimum of 4.0 and a temperature optimum of 80°C after 30 min incubation. Approximately 22{\%} of the activity remained after 2 h incubation at 70°C and the half-life of xylanase at 60°C was 24 h. The xylanase also showed β-glucanase activity with barley β-glucan as substrate as side activity. The xylanase of G. trabeum was very tolerant to inhibitors. Among the various inhibitors studied, only 10 mM AlCl3 was found to inhibit the xylanase activity.",
author = "Anne-Christine Ritschkoff and Johanna Buchert and Liisa Viikari",
note = "Project code: PUU202502",
year = "1994",
doi = "10.1016/0168-1656(94)90121-X",
language = "English",
volume = "32",
pages = "67--74",
journal = "Journal of Biotechnology",
issn = "0168-1656",
publisher = "Elsevier",
number = "1",

}

Purification and characterization of a thermophilic xylanase from the brown-rot fungus Gloeophyllum trabeum. / Ritschkoff, Anne-Christine (Corresponding Author); Buchert, Johanna; Viikari, Liisa.

In: Journal of Biotechnology, Vol. 32, No. 1, 1994, p. 67-74.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Purification and characterization of a thermophilic xylanase from the brown-rot fungus Gloeophyllum trabeum

AU - Ritschkoff, Anne-Christine

AU - Buchert, Johanna

AU - Viikari, Liisa

N1 - Project code: PUU202502

PY - 1994

Y1 - 1994

N2 - A xylanase produced by the brown-rot fungus, Gloeophyllum trabeum, was purified to electrophoretic homogeneity by ion-exchange chromatography and gel filtration. The enzyme had an isoelectric point of 5.0 and molecular mass of 39–42 kDa, respectively. The xylanase appeared to prefer the most substituted glucurono-xylan (DMSO-xylan) as substrate and exhibited a pH optimum of 4.0 and a temperature optimum of 80°C after 30 min incubation. Approximately 22% of the activity remained after 2 h incubation at 70°C and the half-life of xylanase at 60°C was 24 h. The xylanase also showed β-glucanase activity with barley β-glucan as substrate as side activity. The xylanase of G. trabeum was very tolerant to inhibitors. Among the various inhibitors studied, only 10 mM AlCl3 was found to inhibit the xylanase activity.

AB - A xylanase produced by the brown-rot fungus, Gloeophyllum trabeum, was purified to electrophoretic homogeneity by ion-exchange chromatography and gel filtration. The enzyme had an isoelectric point of 5.0 and molecular mass of 39–42 kDa, respectively. The xylanase appeared to prefer the most substituted glucurono-xylan (DMSO-xylan) as substrate and exhibited a pH optimum of 4.0 and a temperature optimum of 80°C after 30 min incubation. Approximately 22% of the activity remained after 2 h incubation at 70°C and the half-life of xylanase at 60°C was 24 h. The xylanase also showed β-glucanase activity with barley β-glucan as substrate as side activity. The xylanase of G. trabeum was very tolerant to inhibitors. Among the various inhibitors studied, only 10 mM AlCl3 was found to inhibit the xylanase activity.

U2 - 10.1016/0168-1656(94)90121-X

DO - 10.1016/0168-1656(94)90121-X

M3 - Article

VL - 32

SP - 67

EP - 74

JO - Journal of Biotechnology

JF - Journal of Biotechnology

SN - 0168-1656

IS - 1

ER -