Purification and properties of an endo-(1→3)-β-d-glucanase from malted barley

David J Manners; Glynn Wilson

Purification and properties of an endo-(1→3)-β-d-glucanase from malted barley

David J Manners
, Glynn Wilson

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

Abstract

An endo-(1?3)-ß-d-glucanase has been isolated from malted barley and purified 92-fold. The enzyme preparation appeared to be physically homogeneous and had a molecular weight of about 12,800 daltons. The enzyme is highly specific for (1?3)-ß-d-glucosidic linkages, and has an endo action on laminaran. The effect of certain group-specific reagents on the enzyme has been examined. © 1974.

Original language	English
Pages (from-to)	9-22
Number of pages	14
Journal	Carbohydrate Research
Volume	37
Issue number	1
Publication status	Published - Oct 1974

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title = "Purification and properties of an endo-(1→3)-β-d-glucanase from malted barley",

abstract = "An endo-(1?3)-{\ss}-d-glucanase has been isolated from malted barley and purified 92-fold. The enzyme preparation appeared to be physically homogeneous and had a molecular weight of about 12,800 daltons. The enzyme is highly specific for (1?3)-{\ss}-d-glucosidic linkages, and has an endo action on laminaran. The effect of certain group-specific reagents on the enzyme has been examined. {\textcopyright} 1974.",

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journal = "Carbohydrate Research",

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T1 - Purification and properties of an endo-(1→3)-β-d-glucanase from malted barley

AU - Manners, David J

AU - Wilson, Glynn

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N2 - An endo-(1?3)-ß-d-glucanase has been isolated from malted barley and purified 92-fold. The enzyme preparation appeared to be physically homogeneous and had a molecular weight of about 12,800 daltons. The enzyme is highly specific for (1?3)-ß-d-glucosidic linkages, and has an endo action on laminaran. The effect of certain group-specific reagents on the enzyme has been examined. © 1974.

AB - An endo-(1?3)-ß-d-glucanase has been isolated from malted barley and purified 92-fold. The enzyme preparation appeared to be physically homogeneous and had a molecular weight of about 12,800 daltons. The enzyme is highly specific for (1?3)-ß-d-glucosidic linkages, and has an endo action on laminaran. The effect of certain group-specific reagents on the enzyme has been examined. © 1974.

M3 - Article

SN - 0008-6215

VL - 37

SP - 9

EP - 22

JO - Carbohydrate Research

JF - Carbohydrate Research

IS - 1

ER -

Purification and properties of an endo-(1→3)-β-d-glucanase from malted barley

Abstract

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