Inny tytuł:

Immobilization of recombinant B-galactosidase in reactions catalysed by transglutaminase

Wydawca:

Committee on Biotechnology PAS ; Institute of Bioorganic Chemistry PAS

Typ obiektu:

Journal/Article

Abstrakt:

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.

Czasopismo/Seria/cykl:

Biotechnologia, vol.70, 3 (2005)-.

Tom:

70

Zeszyt:

3

Strona pocz.:

209

Strona końc.:

220

Szczegółowy typ zasobu:

Article

Format:

application/pdf

Identyfikator zasobu:

0860-7796 ; oai:rcin.org.pl:91959 ; IChB B-66

Źródło:

Library of Institute of Bioorganic Chemistry PAS

Język:

pol

Język streszczenia:

eng

Zakres czasowy:

1988-2010

Prawa:

Creative Commons Attribution BY-SA 4.0 license

Zasady wykorzystania:

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:

Digitalizacja:

Institute of Bioorganic Chemistry of the Polish Academy of Science

Lokalizacja oryginału:

Institute of Bioorganic Chemistry of the Polish Academy of Science

Dofinansowane ze środków:

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.

Dostęp:

Open