[Comparative physico-chemical study of L-lysine-alpha-oxidase from surface and fermenter growth Trichoderma sp].
Homogeneous preparations of L-lysine-alpha-oxidase were obtained from Trichoderma sp cultivated by using a surface technique and a fermenter set. The homogeneous enzyme preparations were similar in molecular mass, isoelectric point and substrate specificity. There was the single difference in the absorbance spectra, which may occur due to the presence of cofactor FAD in various oxidation states. The findings suggest that cultivation of Trichoderma sp in the fermenter set did not alter properties of L-lysine-alpha-oxidase produced.
E V
EV
Lukasheva
V S
VS
Vesa
T T
TT
Berezov
D000594:Amino Acid Oxidoreductases / Q000378:metabolism*; D005285:Fermentation; D007526:Isoelectric Point; D008970:Molecular Weight; D013057:Spectrum Analysis; D013379:Substrate Specificity; D014242:Trichoderma / Q000201:enzymology*
D000594:Amino Acid Oxidoreductases; C041123:L-lysine oxidase
Sravnitel'noe fiziko-khimicheskoe izuchenie L-lizin-alpha-oksidazy iz poverkhnostno i glubinno vyrashchennoĭ Trichoderma sp.