ADSORPTION OF HYDROPHOBIZED GLUCOSE-OXIDASE AT SOLUTION AIR INTERFACE/

The modification of glucose oxidase by palmitic acid ester of N-hydrox ysuccinimide leads to the formation of a new hydrophobized enzyme with five covalently bound C-16 groups. Such a modification was shown not to alter noticeably the native structure of the enzyme. The modified g lucose oxidase displays enhanced surface activity at the water/air int erface in comparison with the native enzyme. The maximum reduction of surface tension at all concentrations studied was higher for the modif ied 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 unmodif ied enzyme. (C) 1997 Academic Press.