Adsorption of Hydrophobized Glucose Oxidase at Solution/Air Interface

• Published in: Journal of colloid and interface science Vol. 190; no. 2; pp. 313 - 317
• Main Authors: Baszkin, A., Boissonnade, M.M., Rosilio, V., Kamyshny, A., Magdassi, S.
• Format: Journal Article
• Language: English
• Published: San Diego, CA Elsevier Inc 15.06.1997; Elsevier
• Subjects: adsorption; Biological and medical sciences; Biotechnology; Chemical synthesis for preparing modified enzymes, enzyme fragments and enzyme analogs; Enzyme engineering; Fundamental and applied biological sciences. Psychology; glucose oxidase at solution/air interface; hydrophobized glucose oxidase; Methods. Procedures. Technologies; Production of selected enzymes; glucose oxidase at solution/air interface; hydrophobized glucose oxidase; adsorption; Glucose oxidase; Chemical modification; Adsorption; Molecular structure; Enzyme; Surface properties; Oxidoreductases; Air water interface; Surface activity; Comparative study
• ISSN: 0021-9797; 1095-7103
• DOI: 10.1006/jcis.1997.4874

The modification of glucose oxidase by palmitic acid ester ofN-hydroxysuccinimide leads to the formation of a new hydrophobized enzyme with five covalently bound C16groups. Such a modification was shown not to alter noticeably the native structure of the enzyme. The modified glucose oxidase displays enhanced surface activity at the water/air interface in comparison with the native enzyme. The maximum reduction of surface tension at all concentrations studied was higher for the modified glucose oxidase than for the native one. The modified enzyme also displayed a much steeper rise of the surface potential with time and a much more rapid attainment of the saturation plateau than the unmodified enzyme.