Adsorption of Hydrophobized Glucose Oxidase at Solution/Air Interface

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.