[Formation of L-asparagine and L-glutamine deamidases by bacterial cultures].

Among studied 40 bacterial cultures, 17 strains catalysed hydroxylaminolysis of I.-asparagine and L-glutamine, and among these cultures seven strains belonged to the Pseudomonas genus. Extracts of the cells of Ps. boreopolis 526 (MGU), Ps. aurantiaca IBFM B-14, and Ps. septica IBFM B-40 had the maximum deamidase activity during the stage of decelerated growth. The activity of L-asparaginase 2 was practically the same upon various ways of disintegration of the cells of Ps. aurantiaca IBFM B-14: ballistic technique, ultrasound, extrusion form the solid state. Production of beta-aspartylhydroxamic acid by L-asparaginase 2 depended on the concentration of hydroxylamine and protein in the reaction mixture and on the duration of the reaction.