Object structure
Title:

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:

2005

Type of object:

Journal/Article

Subject and Keywords:

biotechnology

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:

70

Issue:

3

Start page:

209

End page:

220

Resource type:

Text

Detailed Resource Type:

Article

Format:

application/pdf

Resource Identifier:

0860-7796 ; IChB B-66

Source:

Library of Institute of Bioorganic Chemistry PAS

Language:

pol

Language of abstract:

eng

Temporal coverage:

1988-2010

Rights:

Creative Commons Attribution BY-SA 4.0 license

Terms of use:

Copyright-protected material. [CC BY-SA 4.0] May be used within the scope specified in Creative Commons Attribution BY-SA 4.0 license, full text available at:

Digitizing institution:

Institute of Bioorganic Chemistry of the Polish Academy of Science

Original in:

Institute of Bioorganic Chemistry of the Polish Academy of Science

Projects co-financed by:

Operational Program Digital Poland, 2014-2020, Measure 2.3: Digital accessibility and usefulness of public sector information; funds from the European Regional Development Fund and national co-financing from the state budget.

Access:

Open

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