Enzyme and organic solvents: Horse liver alcohol dehydrogenase in non‐ionic microemulsion: Stability and activity

FEBS Letters

Lee, Kang Min¹  Biellmann, Jean-François¹ 

[1] Laboratoire de Chimie Organique Biologique, UA no. 31, Institut de Chimie, Université Louis Pasteur, 1 rue Blaise Pascal, 67008 Strasbourg, France

关键词: Alcohol dehydrogenase;    Enzyme stability;    Microemulsion;    Organic solvent;    Surfactant;    Water content;   

DOI  :  10.1016/0014-5793(87)80504-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

In a microemulsion made with Triton X-100, the stability of the enzymatic activity was higher than in ionic microemulsions. The stability increased with water content. The kinetic constants (Michaelis constant of NAD⁺ and maximum velocity) were close to those found in the previously studied microemulsions. The Michaelis constant of NAD⁺ expressed with respect to the buffer volume was higher than in water. The pH dependence of the kinetic constants in this microemulsion was determined. The activity determined by NAD⁺ reduction decreased with water content, whereas the redox activity determined via butanol oxidation coupled to retinal reduction was only slightly reduced.

【 授权许可】

Unknown