The Release of Enzymes and Proteins from Baker's Yeast Disrupted by a Agitator Bead Mill [Translated]†

Abstract

Baker's yeast suspended in pure water was disintegrated by the agitator bead mill using glass beads having a diameter of 0.5 to 2.0 mm. ADH (alcohol dehydrogenase) was released faster than protein and G-6-PDH (glucose-6-phosphate dehydrogenase), and a concept of the selective release of enzyme was defined. The final weight of the protein released and the activities of enzymes, the release rate constant for protein and ADH, and the release selectivity between the protein and ADH were dependent on the bead size, the weight of beads and the agitation speed. The optimum condition for release existed for each operation parameter. The electrical conductivity of the yeast slurry had good correlation with the amount of G-6-PDH and protein released. This result indicated that the degree of release for these substances could be estimated from the measurement of electric conductivity.† This report was originally printed in J. Soc. Powder Technology, Japan. 26(6), 424-429 (1989) in Japanese, before being translated into English by KONA Editorial Committee with the permission of the editorial committee of the Soc. Powder Technology, Japan.