[Purification and properties of L-glutamine and L-asparagine deaminase from Pseudomonas aurantiaca IBPM-14]

An enzymic preparation of L-glutamine and L-asparagine deamidase was obtained from Pseudomonas auractiaca IBPM B-14. The preparation was purified 100--150-fold by thermal treatment and chromotography on columns with biogel P-150 and DEAE-cellulose. The enzymic activity was measured by the methods of hydroxylaminolysis and direct nesslerization. The deamidase preparation had an activity of 51 i. u. by glutamine and 15 i. e. by asparagine. Evidence on the pH effect on the deamidase activity was accumulated.