Interaction and Comparison of a Class I Hydrophobin from Schizophyllum commune and Class II Hydrophobins from Trichoderma reesei
Division of Microbiology, Utrecht University, Utrecht, Utrecht, Netherlands Biomacromolecules
(Impact Factor: 5.75).
05/2006; 7(4):1295-301. DOI: 10.1021/bm050676s
Hydrophobins fulfill a wide spectrum of functions in fungal growth and development. These proteins self-assemble at hydrophilic-hydrophobic interfaces into amphipathic membranes. Hydrophobins are divided into two classes based on their hydropathy patterns and solubility. We show here that the properties of the class II hydrophobins HFBI and HFBII of Trichoderma reesei differ from those of the class I hydrophobin SC3 of Schizophyllum commune. In contrast to SC3, self-assembly of HFBI and HFBII at the water-air interface was neither accompanied by a change in secondary structure nor by a change in ultrastructure. Moreover, maximal lowering of the water surface tension was obtained instantly or took several minutes in the case of HFBII and HFBI, respectively. In contrast, it took several hours in the case of SC3. Oil emulsions prepared with HFBI and SC3 were more stable than those of HFBII, and HFBI and SC3 also interacted more strongly with the hydrophobic Teflon surface making it wettable. Yet, the HFBI coating did not resist treatment with hot detergent, while that of SC3 remained unaffected. Interaction of all the hydrophobins with Teflon was accompanied with a change in the circular dichroism spectra, indicating the formation of an alpha-helical structure. HFBI and HFBII did not affect self-assembly of the class I hydrophobin SC3 of S. commune and vice versa. However, precipitation of SC3 was reduced by the class II hydrophobins, indicating interaction between the assemblies of both classes of hydrophobins.
Available from: Karin Scholtmeijer
- "Dispersal of hydrophobic solids, liquids and air Both class I and class II hydrophobins can be used to disperse hydrophobic solids in water (Wösten et al. 1994; de Vocht et al. 1998; Lumsdon et al. 2005; Askolin et al. 2006). High concentrations of non-ionic surfactants are usually used to disperse Teflon particles in aqueous solutions (e.g., in coatings and lubricants). "
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ABSTRACT: Hydrophobins are proteins exclusively produced by filamentous fungi. They self-assemble at hydrophilic-hydrophobic interfaces into an amphipathic film. This protein film renders hydrophobic surfaces of gas bubbles, liquids, or solid materials wettable, while hydrophilic surfaces can be turned hydrophobic. These properties, among others, make hydrophobins of interest for medical and technical applications. For instance, hydrophobins can be used to disperse hydrophobic materials; to stabilize foam in food products; and to immobilize enzymes, peptides, antibodies, cells, and anorganic molecules on surfaces. At the same time, they may be used to prevent binding of molecules. Furthermore, hydrophobins have therapeutic value as immunomodulators and can been used to produce recombinant proteins.
Applied Microbiology and Biotechnology 01/2015; 99(4). DOI:10.1007/s00253-014-6319-x · 3.34 Impact Factor
Available from: Seunghwan Lee
- "Based on the comparison of amino acid residue sequence, hydrophobins are classified into two groups, type I and type II       . Surfaceactive properties of hydrophobins have drawn particular interests in self-assembled adsorption behavior of hydrophobins at air/water   , water/oil    , and water/solid interfaces        . This, in turn, sparked intensive researches to utilize hydrophobins as coating materials for biomedical, technical, and personal care products [23–28]. "
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ABSTRACT: Two type II fungal hydrophobins, HFBI and FpHYD5, have been studied as aqueous lubricant additive at a nonpolar, compliant sliding contact (self-mated poly(dimethylsiloxane) (PDMS) contact) at two different concentrations, 0.1 mg/mL and 1.0 mg/mL. The two hydrophobins are featured as non-glycosylated (HFBI, m.w. ca. 7 kDa) vs glycosylated (FpHYD5, m.w. ca. 10 kDa) proteins. Far UV CD spectra of the two hydrophobins were very similar, suggesting overall structural similarity, but showed a noticeable difference according to the concentration. This is proposed to be related to the formation of multimers at 1.0 mg/mL. Despite 10-fold difference in the bulk concentration, the adsorbed masses of the hydrophobins onto PDMS surface obtained from the two solutions (0.1 and 1.0 mg/mL) were nearly identical, suggesting that a monolayer of the hydrophobins are formed from 0.1 mg/mL solution. PDMS–PDMS sliding interface was effectively lubricated by the hydrophobin solutions, and showed a reduction in the coefficient of friction by as much as ca. two orders of magnitude. Higher concentration solution (1.0 mg/mL) provided a superior lubrication, particularly in low-speed regime, where boundary lubrication characteristic is dominant via ‘self-healing’ mechanism. FpHYD5 revealed a better lubrication than HFBI presumably due to the presence of glycans and improved hydration of the sliding interface. Two type II hydrophobins function more favorably compared to a synthetic amphiphilic copolymer, PEO–PPO–PEO, with a similar molecular weight. This is ascribed to higher amount of adsorption of the hydrophobins to hydrophobic surfaces from aqueous solution.
Colloids and surfaces B: Biointerfaces 01/2015; 125:264-269. DOI:10.1016/j.colsurfb.2014.10.044 · 4.15 Impact Factor
Available from: Frank Delvigne
- "Improvement in production of HFBII can be done by optimizing the medium composition. Lactose has been found to be a strong promoter of cellulolytic activity and HFBII production through expression of the hfb2 gene and repression of hfb1   . On the opposite, glucose has been found to promote the production of HFBI . "
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ABSTRACT: Production and purification of hydrophobin HFBII has recently been the subject of intensive research, but the yield of production needs to be further improved for a generic use of this molecule at industrial scale. In a first step, the influence of different carbon sources on the growth of Trichoderma reesei and the production of HFBII was investigated. The optimum productivity was obtained by using 40 g/L lactose. Carbon starvation and excretion of extracellular enzyme were determined as two main conditions for the production of HFBII. In the second phase, and according to the physiological mechanisms observed during the screening phase, a bioreactor set up has been designed and two modes of cultures have been investigated, i.e. the classical submerged fermentation and a fungal biofilm reactor. In this last set-up, the broth is continuously recirculated on a metal packing exhibiting a high specific surface. In this case, the fungal biomass was mainly attached to the metal packing, leading to a simplification of downstream processing scheme. More importantly, the HFBII concentration increased up to 48.6 +/- 6.2 mg/L which was 1.8 times higher in this reactor configuration and faster than the submerged culture. X-ray tomography analysis shows that the biofilm overgrowth occurs when successive cultures are performed on the same packing. However, this phenomenon has no significant influence on the yield of HFBII, suggesting that this process could be operated in continuous mode. Protein hydrolysis during stationary phase was observed by MALDI-TOF analysis according to the removal of the last amino acid from the structure of HFBII after 48 h from the beginning of fermentation in biofilm reactor. Hopefully this modification does not lead to alternation of the main physicochemical properties of HFBII.
Biochemical Engineering Journal 07/2014; 88. DOI:10.1016/j.bej.2014.05.001 · 2.47 Impact Factor
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