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Immobilization of recombinant B-galactosidase in reactions catalysed by transglutaminase
Committee on Biotechnology PAS ; Institute of Bioorganic Chemistry PAS
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.
Biotechnologia, vol.70, 3 (2005)-.
0860-7796 ; oai:rcin.org.pl:91959 ; IChB B-66
Library of Institute of Bioorganic Chemistry PAS
Creative Commons Attribution BY-SA 4.0 license
Institute of Bioorganic Chemistry of the Polish Academy of Science
Institute of Bioorganic Chemistry of the Polish Academy of Science
Oct 2, 2020
Dec 19, 2019
123
https://rcin.org.pl./publication/118389
Edition name | Date |
---|---|
Unieruchamianie rekombinowanej B-galaktozydazy w reakcjach katalizowanych transglutaminazą | Oct 2, 2020 |
Wołosowska, Sylwia Synowiecki, Józef
Synowiecki, Józef Wołosowska, Sylwia
Borkowska, Bożenna
Ziółkowski, Piotr Babula- Skowrońska, Danuta Kaczmarek, Małgorzata Cieśla, Agata Sadowski, Jan
Synowiecki, Józef