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Immobilization of recombinant B-galactosidase in reactions catalysed by transglutaminase
Subtitle:Immobilization of recombinant B-galactosidase in reactions catalysed by transglutaminase
Creator:Wołosowska, Sylwia ; Synowiecki, Józef
Publisher:Committee on Biotechnology PAS ; Institute of Bioorganic Chemistry PAS
Date issued/created: Type of object: Subject and Keywords: 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.
Relation:Biotechnologia, vol.70, 3 (2005)-.
Volume: Issue: Start page: End page: Resource type: Detailed Resource Type: Format: Resource Identifier: Source:Library of Institute of Bioorganic Chemistry PAS
Language: Language of abstract: Temporal coverage: Rights:Creative Commons Attribution BY-SA 4.0 license
Terms of use: Digitizing institution:Institute of Bioorganic Chemistry of the Polish Academy of Science
Original in:Institute of Bioorganic Chemistry of the Polish Academy of Science
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