Abstract
A galactose oxidase electrode was constructed. Galactose oxidase (Gal-OD) was placed, after its immobilisation in gelatine, between two dialysis membranes and tightened to a silver-platinum electrode. The activity of the enzyme electrode was increased greatly through applying potassium ferricyanide and copper chloride. The optimum position for the mechanism of the Gal-OD reaction was discussed. A pH optimum of 7·0 was determined for the Gal-OD electrode. Below pH 5·0 a strong decrease in activity was observed. The sodium acetate and citric acid-phosphate buffers caused a strong decrease in activity. Gal-OD showed an “apparent” activity 6 times higher for dihydroxyacetone than that for D-galactose. The “apparent” activity for D-galactose, D-lactose, D-melibiose, raffinose and stachyose are 7·5%, 82·7%, 85·1% and 113·3%, respectively. A linear measuring range was determined for D-galactose, D-lactose, D-melibiose, stachyose and raffinose up to 50 mM, 60 mM, 70 mM, 70 mM and 100 mM, respectively.
Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
