Intracellular L-aspartate-beta-decarboxylase of Pseudomonas sp. and Alcaligenes sp. and its immobilization
Abelian, B.A.; Bagdarsarian, S.N.; Afrikian, E.G.
Biokhimiia 56(7): 1288-1295
1991
ISSN/ISBN: 0320-9725 PMID: 1932353 Document Number: 378941
Intracellular L-aspartate-beta-decarboxylase of Pseudomonas sp. and Alcaligenes sp. was isolated, purified and characterized. The cells were destroyed by ultrasonic treatment; the enzymes were precipitated by ammonium sulfate fractionation, dialyzed and lyophylized using Biogel P-150. After gel electrophoresis homogeneous enzyme preparations were obtained. The activity of L-aspartate-beta-decarboxylase is rather high--up to 92.1 U/min/mg of protein and is maximal at pH 5.5 and at temperatures of 45-55 degrees C. The Km and Vmax values for the Pseudomonas sp. enzyme are 0.1 M and 0.33 mM/min, respectively: those for the Alcaligenes sp. enzyme are 0.15 M and 1.0 mM/min, respectively. The results of amino acid analysis suggest that the enzymes slightly differ from one another with regard to aspartic and glutamic acid, alanine, valine and isoleucine content. Immobilization of the enzymes on various carriers was performed.