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

Anne-Christine Ritschkoff; Johanna Buchert; Liisa Viikari

doi:10.1016/0168-1656(94)90121-X

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

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

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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 language	English
Pages (from-to)	67-74
Number of pages	8
Journal	Journal of Biotechnology
Volume	32
Issue number	1
DOIs	https://doi.org/10.1016/0168-1656(94)90121-X
Publication status	Published - 1994
MoE publication type	A1 Journal article-refereed

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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.",

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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

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JO - Journal of Biotechnology

JF - Journal of Biotechnology

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

Abstract

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