Glutamic acid deamination in the presence of montmorillonite

Abstract

AbstractGlutamic acid deamination was realized in the absence and in the presence of montmorillonite saturated with various metallic cations (Na+, Mn2+, Cu2+). 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.