THE β-AMYLASE ENZYMES OF BARLEY AND MALT: I. PURIFICATION OF THE MALT ENZYMES*

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Abstract
Two β-amylase enzymes from malted barley were purified by successively fractionating an extract on CM-cellulose, Sephadex G-75, and DEAE-cellulose. The procedure resulted in a net recovery of 10% of the initial activity and a 10-fold and 16-fold purification of the individual enzymes. Each enzyme migrated as a single protein band during disc electrophoresis at pH 4·5, but each purified protein extract produced two active protein bands at pH 8·9. This heterogeneity within components appeared to be due to oxidation of essential SH groups at high pH that caused loss of enzymic activity.