Roles of Ammonium and Chloride Ions in the Conversion of L-Glutamic Acid Fermentation to L-Glutamine and N-Acetyl-L-Glutamine Fermentation by Corynebacterium glutamicum
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The roles of NH_4^+ and Cl^- in the conversion of L-glutamic acid fermentation to L-glutamine and N-acetyl-L-glutamine (N-AGM) production by Corynebacterium glutamicum were investigated. It was confirmed that the presence of a high concentration of Cl^- in the medium in the growth phase of the bacterium was essential for the effective production of L-glutamine and N-AGM. As for NH_4^+, both (NH_4)_2SO_4 and NH_4Cl were similarly effective for the formation of these amides. Although both L-glutamine and N-AGM synthesizing enzyme activities decreased with increasing concentrations of either ammonium salt, there was no difference of degrees in the effect of the two ammonium salts on these enzyme activities. Both L-glutaminase and N-AGM deacetylating enzyme activities decreased with the increase in concentration of the ammonium salts. However, there was little difference between the effects of (NH_4)_2SO_4 and NH_4Cl on these two enzyme activities. The amount of L-glutamic acid released from the cells by washing with solutions of such salts as NaCl, (NH_4)_2SO_4 and NH_4Cl was much less than by washing with water. However, no difference was found between these salt solutions in their effect on the release of L-glutamic acid, L-glutamine and N-AGM. On the other hand, cells grown on a high concentration of NH_4Cl retained a much higher amount of free L-glutamic acid within the cells than cells grown on (NH_4)_3SO_4. This finding suggests that the presence of Cl^- in the medium in the growth phase affects cell permeability toward L-glutamic acid. L-Glutamine and N-AGM synthesizing reactions were each catalyzed by two different enzymes, whereas in the degradation, N-AGM was first deacetylated to L-glutamine, and L-glutamine was decomposed to L-glutamic acid by L-glutaminase.
- 公益社団法人日本生物工学会の論文
- 1978-06-25
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