Studies on the Enzymatic Production ofl-Aspartic Acid from Maleic Acid

Publisher Website
Google Scholar
Abstract
The enzymatic production of l-aspartic acid from maleic acid with cell suspensions of Alcaligenes faecalis 5-24, isolated from solid by the authors, was investigated. The optimum conditions of this reaction and some cultural conditions which influenced on the ability of the cells to catalyze the above reaction were mainly studied. The cells grown on maleic acid as a sole source of carbon showed exclusively the strong ability. The cells grown on a carbon source other than maleic acid showed no activity of this reaction. It was concluded that an inducibles enzyme whose formation was stimulated by the presence of maleic acid might be involved in the reaction for the production of l-aspartic acid from maleic acid. It was found that malonic acid was replaceable for maleic acid which played an inductive role for the formation of the enzyme system concerned with the reaction of l-aspartic acid production from maleic acid. The cells grown in the medium containing malonic acid showed a stronger activity of the above reaction than the cells grown on maleic acid. The induction effect of malonic acid was remarkable when the organism was cultured in an acid medium. Whereas, consumption of C14-malonic acid in the medium by the organism was not observed at all in any pH milieu even where the formation of the enzyme system essential for the reaction was fully conducted. It indicated that malonic acid penetrated preferentially in acid milieu into the cells was a non-metabolic inducer like thiomethyl-β-d-galactoside in β-galactosidase system and that permeability barrier might exist in the organism. The formation of cis-trans isomerase which catalyzed the conversion of maleic acid to fumaric acid was much stimulated by the addition of either malonic acid or maleic acid. From these results, it was concluded that l-aspartic acid was produced from maleic acid and ammonium ion by both actions of the inducible cis-trans isomerase and the constitutive aspartase.

This publication has 3 references indexed in Scilit: