The enzymic synthesis and degradation of starch. Part XVI. The purification and properties of the β-amylase of soya bean

Stanley Peat; S. J. Pirt; W. J. Whelan

doi:10.1039/JR9520000714

The enzymic synthesis and degradation of starch. Part XVI. The purification and properties of the β-amylase of soya bean

Stanley Peat, S. J. Pirt, W. J. Whelan

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Abstract

A method is described for the purification of the β-amylase of soya bean, the product of which is amorphous but is virtually free from Z-enzyme as well as from α-amylase and maltase. The elimination of Z-enzyme has been studied in detail and it is shown that for the structural analysis of amylaceous polysaccharides the purified soya-bean β-amylase is exactly equivalent to the crystalline enzyme of sweet potato. It is established that the amyloses of sago, tapioca, and maize are branched in the same way as potato amylose and that the branch points are attacked by Z-enzyme.

Original language	English (US)
Pages (from-to)	714-722
Number of pages	9
Journal	Journal of the Chemical Society (Resumed)
DOIs	https://doi.org/10.1039/JR9520000714
State	Published - Jan 1 1952
Externally published	Yes

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Chemistry(all)

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10.1039/JR9520000714

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title = "The enzymic synthesis and degradation of starch. Part XVI. The purification and properties of the β-amylase of soya bean",

abstract = "A method is described for the purification of the β-amylase of soya bean, the product of which is amorphous but is virtually free from Z-enzyme as well as from α-amylase and maltase. The elimination of Z-enzyme has been studied in detail and it is shown that for the structural analysis of amylaceous polysaccharides the purified soya-bean β-amylase is exactly equivalent to the crystalline enzyme of sweet potato. It is established that the amyloses of sago, tapioca, and maize are branched in the same way as potato amylose and that the branch points are attacked by Z-enzyme.",

author = "Stanley Peat and Pirt, {S. J.} and Whelan, {W. J.}",

year = "1952",

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doi = "10.1039/JR9520000714",

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AU - Peat, Stanley

AU - Pirt, S. J.

AU - Whelan, W. J.

PY - 1952/1/1

Y1 - 1952/1/1

N2 - A method is described for the purification of the β-amylase of soya bean, the product of which is amorphous but is virtually free from Z-enzyme as well as from α-amylase and maltase. The elimination of Z-enzyme has been studied in detail and it is shown that for the structural analysis of amylaceous polysaccharides the purified soya-bean β-amylase is exactly equivalent to the crystalline enzyme of sweet potato. It is established that the amyloses of sago, tapioca, and maize are branched in the same way as potato amylose and that the branch points are attacked by Z-enzyme.

AB - A method is described for the purification of the β-amylase of soya bean, the product of which is amorphous but is virtually free from Z-enzyme as well as from α-amylase and maltase. The elimination of Z-enzyme has been studied in detail and it is shown that for the structural analysis of amylaceous polysaccharides the purified soya-bean β-amylase is exactly equivalent to the crystalline enzyme of sweet potato. It is established that the amyloses of sago, tapioca, and maize are branched in the same way as potato amylose and that the branch points are attacked by Z-enzyme.

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The enzymic synthesis and degradation of starch. Part XVI. The purification and properties of the β-amylase of soya bean

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