Purification and characterization of a xylanase from Bipolaris sorokiniana

Sari Peltonen; Reijo Karjalainen; Marja-Leena Niku-Paavola

doi:10.1016/S0953-7562(09)80339-0

Purification and characterization of a xylanase from Bipolaris sorokiniana

Sari Peltonen
, Reijo Karjalainen
, Marja-Leena Niku-Paavola

VTT Technical Research Centre of Finland

University of Helsinki

Research output: Contribution to journal › Article › Scientific › peer-review

12 Citations (Scopus)

Abstract

Bipolaris sorokiniana, a cereal fungal pathogen, showed xylanase activity when grown on minimal salt medium containing 2% of cell wall prepared from barley leaves as the sole carbon source. The most abundant of the xylanases, 1,4-β-D-xylan xylanohydrolase (EC 3.2.1.8), was purified to homogeneity by S-Sepharose chromatography, and its properties were determined. The induction of xylanase was highest on the 12th day after inoculation in shake flask culture. The purified xylanase had a molecular weight of 30 kDa and an isoelectric point of 9·5. The pH and temperature optima of the B. sorokiniana xylanase activity were 5·5 and 70°C respectively. The enzyme was stable over the pH range 5–10 but the stability towards temperature fell sharply above 55°.

Original language	English
Pages (from-to)	67-73
Journal	Mycological Research
Volume	98
Issue number	1
DOIs	https://doi.org/10.1016/S0953-7562(09)80339-0
Publication status	Published - 1994
MoE publication type	A1 Journal article-refereed

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title = "Purification and characterization of a xylanase from Bipolaris sorokiniana",

abstract = "Bipolaris sorokiniana, a cereal fungal pathogen, showed xylanase activity when grown on minimal salt medium containing 2\% of cell wall prepared from barley leaves as the sole carbon source. The most abundant of the xylanases, 1,4-β-D-xylan xylanohydrolase (EC 3.2.1.8), was purified to homogeneity by S-Sepharose chromatography, and its properties were determined. The induction of xylanase was highest on the 12th day after inoculation in shake flask culture. The purified xylanase had a molecular weight of 30 kDa and an isoelectric point of 9·5. The pH and temperature optima of the B. sorokiniana xylanase activity were 5·5 and 70°C respectively. The enzyme was stable over the pH range 5{\textendash}10 but the stability towards temperature fell sharply above 55°.",

author = "Sari Peltonen and Reijo Karjalainen and Marja-Leena Niku-Paavola",

note = "Project code: BIO2024",

year = "1994",

doi = "10.1016/S0953-7562(09)80339-0",

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T1 - Purification and characterization of a xylanase from Bipolaris sorokiniana

AU - Peltonen, Sari

AU - Karjalainen, Reijo

AU - Niku-Paavola, Marja-Leena

N1 - Project code: BIO2024

PY - 1994

Y1 - 1994

N2 - Bipolaris sorokiniana, a cereal fungal pathogen, showed xylanase activity when grown on minimal salt medium containing 2% of cell wall prepared from barley leaves as the sole carbon source. The most abundant of the xylanases, 1,4-β-D-xylan xylanohydrolase (EC 3.2.1.8), was purified to homogeneity by S-Sepharose chromatography, and its properties were determined. The induction of xylanase was highest on the 12th day after inoculation in shake flask culture. The purified xylanase had a molecular weight of 30 kDa and an isoelectric point of 9·5. The pH and temperature optima of the B. sorokiniana xylanase activity were 5·5 and 70°C respectively. The enzyme was stable over the pH range 5–10 but the stability towards temperature fell sharply above 55°.

AB - Bipolaris sorokiniana, a cereal fungal pathogen, showed xylanase activity when grown on minimal salt medium containing 2% of cell wall prepared from barley leaves as the sole carbon source. The most abundant of the xylanases, 1,4-β-D-xylan xylanohydrolase (EC 3.2.1.8), was purified to homogeneity by S-Sepharose chromatography, and its properties were determined. The induction of xylanase was highest on the 12th day after inoculation in shake flask culture. The purified xylanase had a molecular weight of 30 kDa and an isoelectric point of 9·5. The pH and temperature optima of the B. sorokiniana xylanase activity were 5·5 and 70°C respectively. The enzyme was stable over the pH range 5–10 but the stability towards temperature fell sharply above 55°.

U2 - 10.1016/S0953-7562(09)80339-0

DO - 10.1016/S0953-7562(09)80339-0

M3 - Article

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VL - 98

SP - 67

EP - 73

JO - Mycological Research

JF - Mycological Research

IS - 1

ER -

Purification and characterization of a xylanase from Bipolaris sorokiniana

Abstract

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