[Alpha-chymotrypsin immobilized on ferromagnetic particles coated with titanium oxide: production and catalytic properties].
Immobilization of alpha-chymotrypsin on magnetic particles with stable coat with titanium oxides as a main constituent allowed the biocatalytic system to be quickly and qualitatively separated into the components after completion of the enzymatic reaction. X-ray phase analysis demonstrated that the coat of magnetic particles is composed mainly of titanium dioxide in brookite modification. The maximal capacity of the particles amounted to 0.3 mg protein/mg particles. It was demonstrated that the reaction catalyzed by immobilized alpha-chymotrypsin proceeds in a kinetic mechanism due to a high dispersion of the ferromagnetic particles. The catalytic constant (25 s-1) and KM (0.17 mM) for the immobilized enzyme for the hydrolysis of N-acetyl-L-tyrosine ethyl ester are comparable to the corresponding characteristics for the free enzyme.
Izmaĭlov
A F
AF
Chemical Department, Moscow State University, Russia.
Kiselev
M V
MV
Vakurov
A V
AV
Gladilin
A K
AK
Levashov
A V
AV
D002384:Catalysis; D002918:Chymotrypsin / Q000737:chemistry*; D005290:Ferric Compounds; D014025:Titanium
D005290:Ferric Compounds; C001215:ferrite; C009495:titanium dioxide; D014025:Titanium; D002918:Chymotrypsin; C117608:alpha-chymotrypsin