Kvasny Prum. 1971; 17(5): 103-106 | DOI: 10.18832/kp1971018

Partition of malt proteins by disc electrophoresis.Peer-reviewed article

M. NENTWICHOVÁ, M. KOTASOVÁ, Z. PECHAN

The article deals with the technique elaborated for the partition of malt proteins by means of polyacrylamidegel disc electrophoresis. The samples of beer and wort were first concentrated through lyophilization. The partition technique did not practically differ from that applied by Cebecauer for the partition of blood serum proteins [ tris-glycine buffer, 10-B amide red as dyeing agent]. The proportion of monomer concentrate to structure-forming agent determining the porosity of the carrier was also the same as in Cebecaurers experiments. The partition takes place in the colums of dense gel [7% of acryl-amide, 0,17% of structure-forming agent, pH 8,9]. The sample is concentrated in a layer of thin gel [2,5% of acrylamide, 0,62 % of structure-forming agent, pH 6,7]. The discontinuity of pH in the boundary between the dense and thin gels ensures an outstanding partitioning efficiency. The proteins are separated from one another in accordance with their different electric charges and molecular masses. Densitometric evaluation of microfilms reproducing electrophoreograms permits to identify 8-11 protein fractions. The results are therefore comparable with Szilvinyi's data. The described method belongs to modern analytic methods applied at present in brewing industry and should be combined with gel chromatography or immunoelectrophoresis and used thus to the identification of protein components in wort. This in its will contribute to more correct evaluation of brewing barley properties prior to malting.
(In Czech, English summary only)

Keywords: malt, proteins, disc electrophoresis

Published: May 1, 1971