[Catalytic properties of induced L-lysine-alpha-oxidase].
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.
Potapova
O L
OL
Smirnova
I P
IP
Vesa
V S
VS
Bykova
O M
OM
Laugalene
N F
NF
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
D000594:Amino Acid Oxidoreductases; C041123:L-lysine oxidase
Izuchenie kataliticheskikh svoĭstv indutsirovannoĭ L-lizin-alpha- oksidazy.