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European Biophysics Journal

, Volume 39, Issue 3, pp 457–468 | Cite as

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

  • Wendel WohllebenEmail author
  • Thomas Subkowski
  • Claus Bollschweiler
  • Bernhard von Vacano
  • Yaqian Liu
  • Wolfgang Schrepp
  • Ulf Baus
Original Paper

Abstract

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

Keywords

Hydrophobin Recombinant Self-association Analytical ultracentrifugation Interface elasticity Emulsion 

Abbreviations

PCR

Polymerase chain reaction

LB medium

Lysogeny broth medium

LAS

Linear alkylbenzene sulfonate

AUC

Analytical ultracentrifugation

Notes

Acknowledgement

We thank Monika Page and Werner Wacker for excellent laboratory support.

Supplementary material

249_2009_430_MOESM1_ESM.pdf (87 kb)
Supplementary material 1 (PDF 87 kb)

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Copyright information

© European Biophysical Societies' Association 2009

Authors and Affiliations

  • Wendel Wohlleben
    • 1
    Email author
  • Thomas Subkowski
    • 2
  • Claus Bollschweiler
    • 2
  • Bernhard von Vacano
    • 1
  • Yaqian Liu
    • 1
  • Wolfgang Schrepp
    • 1
  • Ulf Baus
    • 3
  1. 1.Polymer Physics ResearchBASF SELudwigshafenGermany
  2. 2.Fine Chemicals ResearchBASF SELudwigshafenGermany
  3. 3.New TechnologiesBASF SELudwigshafenGermany

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