Unieruchamianie rekombinowanej B-galaktozydazy w reakcjach katalizowanych transglutaminazą

Thermostable (3-galactosidase from Escherichia coli transformant containing the enzyme gene from Pyrococcus woesei was immobilized at pH 5.5 on silica gel by crosslinking with transglutaminase. The obtained preparations had a specific activity of 11.573 U/g of support at 70°C using oNPG as a substrate. The optimum pH and temperature for immobilized p-galactosidase activity were 5.5 and 95°C. The immobilized enzyme is stable at the temperatures close to the optimal value and the residual activity for oNPG hydrolysis of the preparations incubated 1 h in 0.1 M phosphate citrate buffer (pH 5.5) at 100°C was about 70% of the initial value.