The relation between solution association and surface activity of the hydrophobin HFBI from Trichoderma reesei

• Published in: FEBS letters 2007-06, Vol.581 (14), p.2721-2726
• Main Authors: Szilvay, Géza R., Kisko, Kaisa, Serimaa, Ritva, Linder, Markus B.
• Format: Article
• Language: English
• Subjects: Adsorption; Amino Acid Sequence; Ascomycota - chemistry; Ascomycota - genetics; Chromatography, Gel; Crystallography, X-Ray; Dimerization; dithiothreitol; DTT; Fungal Proteins - chemistry; Fungal Proteins - genetics; Fungal Proteins - isolation & purification; Hydrophobic and Hydrophilic Interactions; Hydrophobin; Hypocrea jecorina; Molecular Sequence Data; Polymers - chemistry; Protein Conformation; Protein multimerization; Protein self-assembly; QCM; quartz crystal microbalance; SAXS; SEC; Sequence Homology, Amino Acid; size exclusion chromatography; small angle X-ray scattering; Solutions - chemistry; Surface active protein; Surface Properties; Thermodynamics; Water - chemistry
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/j.febslet.2007.05.024

Hydrophobins are small fungal surface active proteins that self-assemble at interfaces into films with nanoscale structures. The hydrophobin HFBI from Trichoderma reesei has been shown to associate in solution into tetramers but the role of this association on the function of HFBI has remained unclear. We produced two HFBI variants that showed a significant shift in solution association equilibrium towards the tetramer state. However, this enhanced solution association did not alter the surface properties of the variant HFBIs. The results show that there is not a strong relationship between HFBI solution association state and surface properties such as surface activity.