title: [Isolation and properties of aminocaprolactam hydrolase from Providencia alcalifaciens].
abstract: L-alpha-aminocaprolactam hydrolase possessing the L-lysinamidase activity was isolated and purified from Providencia alcalifaciens. The purification procedure of enzymes included cell destruction on USDL-1, fractionation by ammonium sulfate, gel-chromatography on G-100, ion exchange chromatography on DEAE-cellulose. The purification resulted in a homogeneous enzyme which possessed the both activities. The enzyme molecular weight (180 kDa) was estimated by gel chromatography on Sephadex G-200. Km was 3.5 mM in the phosphate buffer (pH 7.2). L-alpha-aminocaprolactam hydrolase and L-lysinamidase may be related to metal-dependent enzymes requiring Mg++.
mesh_terms: D000581:Amidohydrolases / Q000032:analysis / Q000302:isolation & purification*; D002850:Chromatography, Gel; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D011511:Proteus / Q000201:enzymology*; D011532:Providencia / Q000201:enzymology*; D013379:Substrate Specificity
chemical_list: D000581:Amidohydrolases; C019680:L-alpha-amino-epsilon-caprolactamase
vernacular_title: Poluchenie i svoĭstva aminokaprolaktamgidrolazy iz Providencia alcalifaciens.