Purification and Properties of Three Types of Xylanases Induced by Methyl β-Xyloside from<i>Streptomyces</i>sp.

Marui, Masaki; Nakanishi, Kotoyoshi; Yasui, Toshihiro

doi:10.1080/00021369.1985.10867283

Cited by 3 publications

(1 citation statement)

References 22 publications

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“…The Mr (21500) and pl (8.9) values of the xylanase characterized here are within the ranges previously reported for microbial xylanases. However, its high specific activity and amino acid composition distinguish it from other Dxylanases with similar Mr and/or pl values [20,[23][24][25][27][28][29][30][31][32]. Interestingly, the present endoxylanase is different from either of the two low-Mr endoxylanases (29000, 17700) purified from T. koningii IMI 73022 [22], both of which had lower pl (7.24, 7.3) and higher Km (1.4 mg/ml, 4.2 mg/ml) values and were devoid of carbohydrate.…”

Section: Discussionmentioning

confidence: 99%

Purification and characterization of an endoxylanase from Trichoderma koningii G-39

Huang

Hseu

Wey

1991

Biochemical Journal

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Trichoderma koningii G-39 produced xylanases in submerged culture using oat spelt xylan or crystalline cellulose, Avicel, as the sole carbon source. A low-Mr xylanase was purified from the culture filtrate by ion-exchange chromatography on SP-Trisacryl-M and gel filtration on Fractogel TSK HW-50F. It was homogeneous on SDS/PAGE and isoelectric focusing. A typical procedure provided about 11-fold purification with 4.5% protein yield and 50% activity recovery. The purified enzyme has an Mr value of about 21,500 and a pI of 8.9. Its specific activity was 6100 units/mg of protein, with optimal activity towards 0.5% xylan at about pH 5.5 and 60 degrees C. The purified enzyme had no activity against CM-cellulose with a degree of substitution of 0.63. It also showed no beta-xylosidase activity. The Km and Vmax. values, as determined with the soluble fraction of oat spelt xylan as substrate, were 0.70 mg/ml and 1.85 x 10(6) mumol/min per mg of enzyme respectively. Hg2+ (1 mM) and SDS (10 mM) completely inhibited xylanase activity, whereas Ca2+ showed no significant effect on the enzyme activity at 1 mM, but gave 80% inhibition at 10 mM. The enzyme contained about 4.4% carbohydrate and showed an immunological relationship to a cellobiohydrolase from the same fungal strain.

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Section: Discussionmentioning

confidence: 99%

Purification and characterization of an endoxylanase from Trichoderma koningii G-39

Huang

Hseu

Wey

1991

Biochemical Journal

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Trichoderma Xylanases, Their Properties and Application

Wong

Saddler

1992

Critical Reviews in Biotechnology

188

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Xylanolytic Enzymes from Fungi and Bacteria

Sunna

Antranikian

1997

Critical Reviews in Biotechnology

495

227

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The development of new analytical techniques and the commercial availability of new substrates have led to the purification and characterization of a large number of xylan-degrading enzymes. Furthermore, the introduction of recombinant DNA technology has resulted in the selection of xylanolytic enzymes that are more suitable for industrial applications. For a successful integration of xylanases in industrial processes, a detailed understanding of the mechanism of enzyme action is, however, required. This review gives an overview of various xylanolytic enzyme systems from bacteria and fungi that have been described recently in more detail.

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Purification and Properties of Three Types of Xylanases Induced by Methyl β-Xyloside fromStreptomycessp.

Cited by 3 publications

References 22 publications

Purification and characterization of an endoxylanase from Trichoderma koningii G-39

Purification and characterization of an endoxylanase from Trichoderma koningii G-39

Trichoderma Xylanases, Their Properties and Application

Xylanolytic Enzymes from Fungi and Bacteria

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