title: [Catalytic properties of induced L-lysine-alpha-oxidase].
abstract: Regulation of biosynthesis of L-lysine-alpha-oxidase from Trichoderma sp using biostimulators was studied. Specific activity of L-lysine-alpha-oxidase was increased 2.7-fold in presence of biostimulators; this occurred due to induction of the enzyme, properties of which were described previously. Catalytic and physico-chemical properties of the enzyme studied were not altered after addition of stimulators into the cultivation medium of the producing strain. Small amounts of L-lysine-alpha-oxidase isozyme were detected in the medium during cultivation; the isozyme was less active and had lower molecular mass as compared with the enzyme studied.
authors.forename: O L
authors.initials: OL
authors.lastname: Potapova
authors.forename: I P
authors.initials: IP
authors.lastname: Smirnova
authors.forename: V S
authors.initials: VS
authors.lastname: Vesa
authors.forename: O M
authors.initials: OM
authors.lastname: Bykova
authors.forename: N F
authors.initials: NF
authors.lastname: Laugalene
mesh_terms: D000594:Amino Acid Oxidoreductases / Q000096:biosynthesis*; D002384:Catalysis; D004591:Electrophoresis, Polyacrylamide Gel; D004790:Enzyme Induction; D004795:Enzyme Stability; D006863:Hydrogen-Ion Concentration; D013379:Substrate Specificity; D014242:Trichoderma / Q000201:enzymology
chemical_list: D000594:Amino Acid Oxidoreductases; C041123:L-lysine oxidase
vernacular_title: Izuchenie kataliticheskikh svoĭstv indutsirovannoĭ L-lizin-alpha- oksidazy.