Effects of pH on the activity and structure of choline oxidase from Alcaligenes species

• Authors: Azadeh Hekmat , Ali Akbar Saboury , Ali Akbar Moosavi-Movahedi , Hedayatollah Ghourchian , Faizan Ahmad
• Languages of publication: EN

Abstracts

EN

A reversible effect of pH on the ionization of amino-acid residues at the active center of choline oxidase was observed near the optimum pH (8). Inactivation of choline oxidase took place in the pH ranges 3-6 and 9-11, in which irreversible changes in the structure occur leading to the enzyme inactivation. The first order rate constants of the enzyme's inactivation at various pH values were estimated for the irreversible changes. The Arrhenius analysis revealed no significant changes in the activation enthalpy, while an increase in the activation entropy reflected an increase in the conformational freedom.

Keywords

EN

optimum pH; choline oxidase; nile red; glycine-betaine

• Publisher: Polish Biochemical Society
• Journal: Acta Biochimica Polonica
• Year: 2008
• Volume: 55
• Issue: 3
• Pages: 549-557

Dates

published

2008

received

2008-05-12

revised

2008-08-11

accepted

2008-08-18

(unknown)

2008-09-04

Contributors

author

Azadeh Hekmat

• Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran

author

Ali Akbar Saboury

• Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran

author

Ali Akbar Moosavi-Movahedi

• Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran

author

Hedayatollah Ghourchian

• Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran

author

Faizan Ahmad

• Centre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, New Delhi, India

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