The Hydrophobins HFBI and HFBII from Trichoderma reesei Showing Efficient Interactions with Nonionic Surfactants in Aqueous Two-Phase Systems
- 17 May 2001
- journal article
- research article
- Published by American Chemical Society (ACS) in Biomacromolecules
- Vol. 2 (2), 511-517
- https://doi.org/10.1021/bm0001493
Abstract
Fungal hydrophobins are a group of surface active, self-assembling proteins. The filamentous fungus Trichoderma reesei produces two (class II) hydrophobins, HFBI and HFBII. We have studied how these water-soluble hydrophobins behave in two-phase systems using a series of nonionic surfactants with different characteristics. It was found that both hydrophobins, but especially HFBI, had a very high affinity for the surfactants. The highest partitioning coefficient, over 2500, was observed for HFBI with C11EO2. Reducing the disulfides in the protein resulted in a complete loss of affinity for the surfactant, which demonstrates that the interaction is dependent on the disulfide-stabilized conformation. The hydrophobins could be efficiently extracted back from the surfactant phase by addition of alcohols such as isobutanol. Effects of the type of surfactant, temperature, pH, and ionic strength were investigated. The use of this method for purifying the proteins from crude fungal culture supernatants is demonstrated and implications of the protein−polymer interaction are discussed.Keywords
This publication has 26 references indexed in Scilit:
- Differential Expression of the Vegetative and Spore‐Bound Hydrophobins of Trichoderma Reesei Cloning and Characterization of the Hfb2 GeneEuropean Journal of Biochemistry, 1997
- An abundant hydrophobin (ABH1) forms hydrophobic rodlet layers in Agaricus bisporus fruiting bodiesMicrobiology, 1996
- Genetic and Biochemical Characterization of the Trichoderma Reesei Hydrophobin HFBIEuropean Journal of Biochemistry, 1996
- Production of recombinant proteins in the filamentous fungus Trichoderma reeseiCurrent Opinion in Biotechnology, 1995
- Effect of a Virus on Accumulation of a Tissue-Specific Cell-Surface Protein of the FungusCryphonectria (Endothia) parasiticaMolecular Plant-Microbe Interactions®, 1992
- The thn mutation of Schizophyllum commune, which suppresses formation of aerial hyphae, affects expression of the Sc3 hydrophobin geneJournal of General Microbiology, 1991
- The surface activity of the phytotoxin cerato-ulminCanadian Journal of Botany, 1982
- A simple method for displaying the hydropathic character of a proteinJournal of Molecular Biology, 1982
- Pathogenicity and cerato-ulmin production in Ceratocystis ulmiNature, 1974
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970