FRACTIONATION STUDY OF BARLEY AND MALT PROTEINS

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Abstract
The protein of O.A.C. 21 barley and of the malt produced from it were fractionated by means of various solvents and the fractions were analyzed. The results of the solubility studies and of the analyses support the use of 5% potassium sulphate for the quantitative separation of the albumin and globulin from the less soluble proteins. Fractions of the protein undissolved by potassium sulphate solution decreased in amide nitrogen and increased in arginine nitrogen with decreasing solubility. The results suggest that the protein is a complex, only part of which is soluble in 70% alcohol, and that the selection of this solution for separating it into two fractions is entirely arbitrary.The grains of barley and malt were separated into hulls, germs and "kernels." The total weight and nitrogen content of these fractions, and the distribution of the proteins amongst them was determined. Malting causes no appreciable changes in the hulls. In the "kernel" there is a general breaking down of protein to simpler forms. In the acrospire there is an increase in non-protein nitrogen, salt-soluble protein and glutelin, but no appreciable increase in hordein. The glutelin of the acrospire differs from that of the malt "kernel" both in amide- and argenine-nitrogen content and must be regarded as a distinct protein.

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