Some properties of a fungal β-D-glucanase preparation

David J Manners; J Roger Stark; Glynn Wilson; James Y Brodie

Some properties of a fungal β-D-glucanase preparation

David J Manners, J Roger Stark, Glynn Wilson, James Y Brodie

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Abstract

A commercial enzyme preparation, of fungal origin, contained a mixture of ß-D-glucanases which were fractionated by ion-exchange chromatography to give a mixture of an endo-(1?4)- and an exo-(1?3)-ß-D-glucanase. These two enzymes were then separated by molecular-sieve chromatography on Sephadex G-150. The purified exo-(1?3)-ß-D-glucanase has a relatively high specificity for (1?3)-ß-D-glucosidic linkages, and has no action on lichenin. © 1976.

Original language	English
Pages (from-to)	383-388
Number of pages	6
Journal	Carbohydrate Research
Volume	49
Issue number	C
Publication status	Published - Jul 1976

Cite this

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abstract = "A commercial enzyme preparation, of fungal origin, contained a mixture of {\ss}-D-glucanases which were fractionated by ion-exchange chromatography to give a mixture of an endo-(1?4)- and an exo-(1?3)-{\ss}-D-glucanase. These two enzymes were then separated by molecular-sieve chromatography on Sephadex G-150. The purified exo-(1?3)-{\ss}-D-glucanase has a relatively high specificity for (1?3)-{\ss}-D-glucosidic linkages, and has no action on lichenin. {\textcopyright} 1976.",

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AU - Wilson, Glynn

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N2 - A commercial enzyme preparation, of fungal origin, contained a mixture of ß-D-glucanases which were fractionated by ion-exchange chromatography to give a mixture of an endo-(1?4)- and an exo-(1?3)-ß-D-glucanase. These two enzymes were then separated by molecular-sieve chromatography on Sephadex G-150. The purified exo-(1?3)-ß-D-glucanase has a relatively high specificity for (1?3)-ß-D-glucosidic linkages, and has no action on lichenin. © 1976.

AB - A commercial enzyme preparation, of fungal origin, contained a mixture of ß-D-glucanases which were fractionated by ion-exchange chromatography to give a mixture of an endo-(1?4)- and an exo-(1?3)-ß-D-glucanase. These two enzymes were then separated by molecular-sieve chromatography on Sephadex G-150. The purified exo-(1?3)-ß-D-glucanase has a relatively high specificity for (1?3)-ß-D-glucosidic linkages, and has no action on lichenin. © 1976.

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M3 - Article

SN - 0008-6215

VL - 49

SP - 383

EP - 388

JO - Carbohydrate Research

JF - Carbohydrate Research

IS - C

ER -

Some properties of a fungal β-D-glucanase preparation

Abstract

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