Abstract
Formation of quinoprotein methanol dehydrogrnase (MDH) in Methylobacillus glycogenes, an obligate methylotroph, was strictly controlled by calcium (Ca) in the culture medium. Both the growth of the organism and the total enzyme activity of MDH were also repressed at less than 1 ppm of Ca, although specific activity of MDH showed a similar level. Ca in MDH was replaced with other metals during cultivation of M. glycogenes. When strontium (Sr) chloride was fed instead of CaCl2, Ca in MDH was completely replaced by Sr and showed a specific activity over ten times higher than Ca-containing MDH, although there was no appreciable increase in the MDH content in cells cultured in Sr medium. Methanol oxidase activity was also elevated in the cells that were cultured in the medium with Sr.
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