[Catalytic activity and the stability of horseradish peroxidase increase as a result of its incorporation into a polyelectrolyte complex with chitosan].
The incorporation of horseradish peroxidase into polyelectrolyte complexes with chitosans of different molecular weights (MW 5-150 kDa) yielded highly active and stable enzyme preparations. As a result of the selection of optimal conditions for the formation of peroxidase-chitosan complexes, it was found that 0.1% chitosan with a MW of 10 kDa had the strongest activatory effect on peroxidase (activation degree, > 70%) in the reaction of o-dianisidine oxidation by hydrogen peroxide. The complex formed by 0.001% chitosan with a molecular weight of 150 kDa was most stable: when immobilized on foamed polyurethane, it retained at least 50% of the initial activity for 550 days. The highest catalytic activity was exhibited in a 0.05 M phthalate buffer (pH 5.9-6.2) by the complex containing 0.006-0.009% chitosan in the indicator reaction. The activatory effect of the polysaccharide on the enzyme was determined by its influence on the binding and conversion of the reducting substrate peroxidase.
Veselova
I A
IA
Koreĭko
A V
AV
Shekhovtsova
T N
TN
D002384:Catalysis; D048271:Chitosan / Q000737:chemistry*; D004800:Enzymes, Immobilized / Q000737:chemistry*; D006735:Horseradish Peroxidase / Q000737:chemistry*; D006861:Hydrogen Peroxide / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D011140:Polyurethanes / Q000737:chemistry*
D004800:Enzymes, Immobilized; D011140:Polyurethanes; D048271:Chitosan; D006861:Hydrogen Peroxide; D006735:Horseradish Peroxidase