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Updated: Jul 18, 2026

Direct Detection of the Acetate-forming Activity of the Enzyme Acetate Kinase
Published on: December 19, 2011
Kinetics of the methanogenic fermentation of acetate
S Fukuzaki1, N Nishio, S Nagai
1Department of Fermentation Technology, Faculty of Engineering, Hiroshima University, Saijo-Cho, Higashi-Hiroshima 724, Japan.
Abstract:
Inhibition of the fermentation of acetate to methane and carbon dioxide by acetate was analyzed with an acetate-acclimatized sludge and with Methanosarcina barkeri Fusaro under mesophilic conditions. A second-order substrate inhibition model, q(ch(4) ) = q(m)S/[K(s) + S + (S/K(i))], where S was the concentration of undissociated acetic acid, not ionized acetic acid, could be applicable in both cases. The analysis resulted in substrate saturation constants, K(s), of 4.0 muM for the acclimatized sludge and 104 muM for M. barkeri. The threshold concentrations of undissociated acetic acid when no further acetate utilization was observed were 0.078 muM (pH 7.50) for the acclimatized sludge and 4.43 muM (pH 7.45) for M. barkeri. These kinetic results suggested that the concentration of undissociated acetic acid became a key factor governing the actual threshold acetate concentration for acetate utilization and that the acclimatized sludge in which Methanothrix spp. appeared dominant could utilize acetate better and survive at a lower concentration of undissociated acetic acid than could M. barkeri.
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