Author:

Keywords:

hydrophobins, self-assembly proteins, gushing, Science & Technology, Life Sciences & Biomedicine, Food Science & Technology, Hydrophobins, self-assembly proteins, gushing, HFBII HYDROPHOBIN, RESOLUTION STRUCTURE, SURFACE-ACTIVITY

Abstract:

Class II hydrophobins produced by Ascomycetes exhibit interesting properties as surface active proteins, they are capable of changing the hydropathy of a surface or to behave as an emulsifier due to their globular structure. They are currently known as one the main causes for primary gushing in carbonated beverages by their ability to interact strongly with CO2 molecules forming nanobubbles. To extend the scope of possibilities for hydrophobin applications four different class II hydrophobins were studied and compared for their ability to adhere to surfaces, their surface tension acitivity and ability to interact with CO2 molecules. By using Quartz crystal microbalance with dissipation monitoring, water contact angle, gushing potential and computer modelization, it is attempted to understand how small differences in their structures and amino acid sequences can lead to differences in physicochemical properties and behavior.