Adsorption of hydrophobin proteins at hydrophobic and hydrophilic interfaces.
The surface activity of two hydrophobin proteins, HFBII and SC3, at the solid-liquid, liquid-liquid and liquid-vapor interface has been investigated. Hydrophobins are fungal proteins that are known to adsorb and affect the physico-chemical properties of an interface. In this study, the surface activity was determined by measuring the interaction of hydrophobin molecules with various liquids, solid particles and films that are commonly used or produced in industrial processes. We found that a very low concentration of hydrophobin is required to facilitate the wet-in of hydrophobic solid particles, such as Teflon, into aqueous solutions. It is also capable of stabilizing aqueous dispersions of Kevlar nanopulp, reversing the wettability of hydrophobic films and stabilizing polyunsaturated fatty acid (PUFA) oil-in-water emulsions.
Lumsdon
Simon O
SO
DuPont Company, Experimental Station, Wilmington, DE 19880, USA. simon.lumsdon@usa.dupont.com
Green
John
J
Stieglitz
Barry
B
D000327:Adsorption; D002627:Chemistry, Physical / Q000379:methods; D004655:Emulsions; D005231:Fatty Acids, Unsaturated / Q000737:chemistry; D005656:Fungal Proteins / Q000145:classification / Q000493:pharmacokinetics*; D057927:Hydrophobic and Hydrophilic Interactions; D007700:Kinetics; D009821:Oils / Q000737:chemistry; D011138:Polytetrafluoroethylene / Q000737:chemistry; D011208:Powders; D012567:Schizophyllum / Q000737:chemistry*; D013499:Surface Properties; D013500:Surface Tension; D014867:Water / Q000737:chemistry; D017155:Wettability
D004655:Emulsions; D005231:Fatty Acids, Unsaturated; D005656:Fungal Proteins; D009821:Oils; D011208:Powders; D014867:Water; D011138:Polytetrafluoroethylene