Kinetic and Equilibrium Aspects of Adsorption and Desorption of Class II Hydrophobins HFBI and HFBII at Silicon Oxynitride/Water and Air/Water Interfaces
2013 (English)In: Langmuir, ISSN 0743-7463, E-ISSN 1520-5827, Vol. 29, no 8, 2683-2691 p.Article in journal (Refereed) Published
Hydrophobins are relatively small globular proteins produced by filamentous fungi. They display unusual high surface activity and are implied as mediators of attachment to surfaces, which has resulted in high scientific and technological interest. In this work we focus on kinetic and equilibrium aspects of adsorption and desorption properties of two representatives of class II hydrophobins, namely HFBI and HFBII, at a negatively charged hydrophilic solid/water interface and at the air/water interface. The layers formed at the air/liquid interface were examined in a Langmuir trough, whereas layers formed at the solid/liquid interface were studied using dual polarization interferometry (DPI) under different flow conditions. For comparison, another globular protein, lysozyme, was also investigated. It was found that both the adsorbed amount and the adsorption kinetics were different for HFBI and HFBII, and the adsorption behavior of both hydrophobins on the negatively charged surface displayed some unusual features. For instance, even though the adsorption rate for HFBI was slowed down with increasing adsorbed amount as expected from packing constraints at the interface, the adsorption kinetics curves for HFBII displayed a region indicating adsorption cooperativity. Further, it was found that hydrophobin layers formed under flow partly desorbed when the flow was stopped, and the desorption rate for HFBII was enhanced in the presence of hydrophobins in solution.
Place, publisher, year, edition, pages
2013. Vol. 29, no 8, 2683-2691 p.
Dual-Polarization Interferometry, Internal-Reflection Fluorescence, Air-Water-Interface, Trichoderma-Reesei, Surface Modification, Proteins, Films, Lysozyme, Binding, Layers
IdentifiersURN: urn:nbn:se:kth:diva-120312DOI: 10.1021/la3048888ISI: 000315618400028ScopusID: 2-s2.0-84874403963OAI: oai:DiVA.org:kth-120312DiVA: diva2:614305
QC 201304042013-04-042013-04-042013-04-04Bibliographically approved