Adsorption of hydrophobized glucose oxidase at solution/air interface

A. Baszkin, M. M. Boissonnade, V. Rosilio, A. Kamyshny, S. Magdassi*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

41 Scopus citations

Abstract

The modification of glucose oxidase by palmitic acid ester of N-hydroxysuccinimide leads to the formation of a new hydrophobized enzyme with five covalently bound C16 groups. 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.

Original languageAmerican English
Pages (from-to)313-317
Number of pages5
JournalJournal of Colloid and Interface Science
Volume190
Issue number2
DOIs
StatePublished - 15 Jun 1997

Keywords

  • Adsorption
  • Glucose oxidase at solution/air interface
  • Hydrophobized glucose oxidase

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