Comparison of a new amylase found in barley with the amylases of the fungi of barley husk

Niku‐Paavola, Marja‐Leena; Heikkinen, Marko

doi:10.1002/jsfa.2740260215

J Sci Food Agric

1975

DOI: 10.1002/jsfa.2740260215

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Comparison of a new amylase found in barley with the amylases of the fungi of barley husk

Marja‐Leena Niku‐Paavola

Marko Heikkinen

Abstract: The electrophoretic and antigenic properties of a new, partly characterised barley amylase have been compared with those of the different amylases produced by fungi living on barley husk. The purpose of this work was to ascertain whether the new amylase originates from barley or from the fungal contaminant. It was found that none of the fungi enriched from the grains in question produced amylases which had the same electrophoretic mobility as the new barley amylase or reacted with the antiserum made against it… Show more

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ISOLATION, PURIFICATION AND ELECTROPHORETIC PROPERTIES OF AN Α-Amylase FROM MALTED BARLEY

MacGregor¹

1977

Journal of the Institute of Brewing

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An a-amylase component from malted barley was isolated and purified using aqueous extraction at pH 8-0, heat treatment of the extract at 70°C, specific precipitation with glycogen and ion ex change chromatography on carboxymethyl (CM) and diethylaminoethyl (DEAE) cellulose. The enzyme preparation was shown to be pure by disc electrophoresis at pH 8-9 and iso-electricfocusing on polyacrylamide gel in a pH 4-8 gradient.

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ISOLATION, PURIFICATION AND ELECTROPHORETIC PROPERTIES OF AN Α-Amylase FROM MALTED BARLEY

MacGregor¹

1977

Journal of the Institute of Brewing

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Partial characterisation of a new barley amylase

Niku‐Paavola

1977

J Sci Food Agric

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A new amylolytic enzyme found in barley (Hordeurn vulgare) grain was partially characterised with respect to physicochemical properties and enzymatic activity. The enzyme preparation showed one antigenically homogeneous amylolytic band. Isoelectric focusing resolved the new amylase into two components, one isoelectric at pH 4.5, the other at pH 3.0. During focusing the original activity of the new amylase decreased by 80 %. The purified preparation was inactivated by pH-values below 4.5 and above 9.0 and also by temperatures above + 40°C for 1 h. The new amylase splits the 1,4-a-glycosidic linkages, clearly by endo-attack, of starch, amylopectin, amylose and P-limit dextrin optimally at pH 6.5 at +40°C giving Km-values 8.9 x 4.4 x 10-3, 6.6 x 10-3 and 1.7 x g/ml, respectively. The hydrolysis products from P-limit dextrin were 24% glucose and 46% maltose in the total digest. Mercuric chloride, PCMB,~ EDTAU and T R I P have no noticeable effect on the new amylase, indicating that it is stable under conditions where the other amylolytic enzymes are deactivated. The new amylase seems to be a hydrolase acting on 0-glycosyl compounds, EC 3.2.1., but could not be identified with any of the amylolytic enzymes of vegetable orjgin studied previously.

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Further purification and characterisation of a new amylase found in barley

MacGregor¹,

Daussant²,

Niku‐Paavola³

1979

J Sci Food Agric

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An amylase, previously detected in barley and described as a new barley amylase, has been further purified by immuno-affinity and ion exchange chromatography on CMcellulose. Analysis by isoelectricfocusing and immunochemical techniques showed that the enzyme preparation did not contain the normal a-and P-amylases usually found in barley and malt. The enzyme had a very low isoelectric point (ca pH 3.0) and was identified as an a-amylase on the basis of its action pattern on amylose.

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Comparison of a new amylase found in barley with the amylases of the fungi of barley husk

Cited by 3 publications

References 3 publications

ISOLATION, PURIFICATION AND ELECTROPHORETIC PROPERTIES OF AN Α-Amylase FROM MALTED BARLEY

ISOLATION, PURIFICATION AND ELECTROPHORETIC PROPERTIES OF AN Α-Amylase FROM MALTED BARLEY

Partial characterisation of a new barley amylase

Further purification and characterisation of a new amylase found in barley

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