An Endogenous α-Amylase Inhibitor in Barley Kernels | Zendy

Randall J. Weselake | Zendy; A. W. MacGregor | Zendy; Robert D. Hill | Zendy

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An Endogenous α-Amylase Inhibitor in Barley Kernels

Author(s) -

Randall J. Weselake,

A. W. MacGregor,

Robert D. Hill

Publication year - 1983

Publication title -

plant physiology

Language(s) - Uncategorized

Resource type - Journals

SCImago Journal Rank - 3.554

H-Index - 312

eISSN - 1532-2548

pISSN - 0032-0889

DOI - 10.1104/pp.72.3.809

Subject(s) - hordeum vulgare , amylase , ultrafiltration (renal) , size exclusion chromatography , starch , chemistry , isoelectric focusing , fractionation , hydrolysis , alpha amylase , chromatography , ammonium sulfate , ammonium , ion chromatography , poaceae , biochemistry , hordeum , enzyme , biology , botany , organic chemistry

Barley (Hordeum distichum cv Klages) kernels were shown to contain a factor that converted malted barley alpha-amylase II to the alpha-amylase III form. After purification by ammonium sulfate fractionation, ion exchange chromatography on DEAE-Sephacel, and gel-filtration on Bio Gel P60, the factor gave a single band of protein on isoelectric focusing. The purified factor inhibited hydrolysis of soluble starch by alpha-amylase II from malted barley and germinated wheat (Triticum aestivum cv Neepawa). However, alpha-amylase I from these cereals was not affected. The inhibitor was not dialyzable and was retained by a PM 10 ultrafiltration membrane suggesting a molecular weight greater than 10,000 daltons. Heat treatment of the inhibitor at 70 degrees C for 15 minutes at pH 5.5 and 8.0 resulted in considerable loss of inhibitory activity.

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