@misc{Wołosowska_Sylwia_Immobilization_2005, author={Wołosowska, Sylwia and Synowiecki, Józef}, volume={70}, number={3}, copyright={Creative Commons Attribution BY-SA 4.0 license}, journal={Biotechnologia, vol.70, 3 (2005)-.}, howpublished={online}, year={2005}, publisher={Committee on Biotechnology PAS}, publisher={Institute of Bioorganic Chemistry PAS}, language={pol}, abstract={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.}, type={Text}, title={Immobilization of recombinant B-galactosidase in reactions catalysed by transglutaminase}, URL={http://www.rcin.org.pl/Content/91959/PDF/POZN271_118389_biotechnologia-2005-no3-wolosowska.pdf}, keywords={biotechnology}, }