B-galactosidase activity of proteins extracted from Sulfolobus shibatae
Committee on Biotechnology PAS ; Institute of Bioorganic Chemistry PAS
The cytoplasmic p-galactosidase/p-glucosidase from hyperthermophilicarchaeon Sulfolobus shibatae has been characterized with regard to its use in lactose hydrolysis. Cell extract was purified 16-fold to a specific activity 29.5 U/mgusing ammonium sulfate precipitation, ion-exchange chromatography, and gelfiltration. Isolated enzyme exhibited optimum activity at pH 5.5 and 98°C andhad a half-life of 7 h in acetate buffer (pH 5.5) at 90°C. Cu2+, Hg2+ and Zn^+strongly inhibited the enzyme, whereas catalytic properties of other investigated cations were barely influenced. Glucose and galactose were predominantly produced from lactose. However, at the substrate concentration of 0.15 M,small amount of lactose was converted into transgalactosylation products.
Biotechnologia, vol.61, 2 (2003)-.
0860-7796 ; oai:rcin.org.pl:135754 ; IChB B-57
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
Aug 20, 2020
167
https://rcin.org.pl./publication/170596
Edition name | Date |
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Charakterystyka preparatów B-galaktozydazy z Sulfolobus shibatae | Oct 2, 2020 |
Synowiecki, Józef Wołosowska, Sylwia
Wołosowska, Sylwia Synowiecki, Józef
Borkowska, Bożenna
Ziółkowski, Piotr Babula- Skowrońska, Danuta Kaczmarek, Małgorzata Cieśla, Agata Sadowski, Jan
Synowiecki, Józef