Subtitle:

B-galactosidase activity of proteins extracted from Sulfolobus shibatae

Publisher:

Committee on Biotechnology PAS ; Institute of Bioorganic Chemistry PAS

Abstract:

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.

Relation:

Biotechnologia, vol.61, 2 (2003)-.

Volume:

61

Issue:

2

Start page:

268

End page:

279

Detailed Resource Type:

Article

Format:

application/pdf

Resource Identifier:

0860-7796 ; oai:rcin.org.pl:135754 ; IChB B-57

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