Recombinantly produced hydrophobins from fungal analogues as highly surface-active performance proteins

摘要: Hydrophobins are available from natural resources only in milligram amounts. BASF succeeded a recombinant production process, up-scaled to pilot plant kilogram scale. Strain and protein optimization by modulation of gene expression generation fusion proteins finally leads two class I hydrophobins called H*Protein A B. By analytical ultracentrifugation, we confirm that the self-association H*Proteins solution is governed their sequence, because oligomerization induced same mechanisms (pH > 6, temperature ≫ 5°C, concentration 0.2 mg/ml) as for well-known native SC3 HFB II. Additionally, established triggering structure formation bridging with divalent ions stabilization dimers tetramers monovalent or surfactants. This interplay surfactants can be exploited synergistically: The capacity emulsification 300 ppm standard surfactant boosted 0 100% addition mere 1 our new hydrophobins, B having specific application profiles. astonishing performance rationalized finding minute admixtures enhance significantly interfacial elastic modulus, thus stabilizing interfaces against coalescence phase separation.