Glutamic acid deamination in the presence of montmorillonite

Abstract Glutamic acid deamination was realized in the absence and in the presence of montmorillonite saturated with various metallic cations (Na + , Mn 2+ , Cu 2+ ). The catalytic activity depends upon the interlayer exchangeable cation and the pH of the suspension. A maximum was observed near pH = 5–6. In the presence of the enzyme l-glutamate dehydrogenase and the coenzyme nicotinamide adenine dinucleotide, glutamic acid transforms into α -ketoglutaric acid, but in the presence of montmorillonite, it yields α -hydroxyglutaric acid and traces of butyric acid. However, kinetic and reaction yield are significantly reduced compared to the biological system.