Interaction and comparison of a class I hydrophobin from Schizophyllum commune and class II Hydrophobins Trichoderma reesei

Sanna Askolin, Markus Linder, Karin Scholtmeijer, Maija Tenkanen, Merja Penttilä, Marcel L. de Vocht, Han A.B. Wösten

Research output: Contribution to journalArticleScientificpeer-review

101 Citations (Scopus)

Abstract

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 α-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.

Original languageEnglish
Pages (from-to)1295-1301
Number of pages7
JournalBiomacromolecules
Volume7
Issue number4
DOIs
Publication statusPublished - 1 Apr 2006
MoE publication typeA1 Journal article-refereed

Fingerprint

Polytetrafluoroethylenes
Self assembly
Detergents
Dichroism
Emulsions
Surface tension
Water
Solubility
Proteins
Membranes
Coatings
Polytetrafluoroethylene
Air
1-(heptafluorobutyryl)imidazole
Oils

Keywords

  • hydrophobins
  • fungal
  • filamentous fungi
  • Trichoderma reesei
  • proteins

Cite this

Askolin, Sanna ; Linder, Markus ; Scholtmeijer, Karin ; Tenkanen, Maija ; Penttilä, Merja ; de Vocht, Marcel L. ; Wösten, Han A.B. / Interaction and comparison of a class I hydrophobin from Schizophyllum commune and class II Hydrophobins Trichoderma reesei. In: Biomacromolecules. 2006 ; Vol. 7, No. 4. pp. 1295-1301.
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abstract = "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 α-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.",
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Interaction and comparison of a class I hydrophobin from Schizophyllum commune and class II Hydrophobins Trichoderma reesei. / Askolin, Sanna; Linder, Markus; Scholtmeijer, Karin; Tenkanen, Maija; Penttilä, Merja; de Vocht, Marcel L.; Wösten, Han A.B.

In: Biomacromolecules, Vol. 7, No. 4, 01.04.2006, p. 1295-1301.

Research output: Contribution to journalArticleScientificpeer-review

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T1 - Interaction and comparison of a class I hydrophobin from Schizophyllum commune and class II Hydrophobins Trichoderma reesei

AU - Askolin, Sanna

AU - Linder, Markus

AU - Scholtmeijer, Karin

AU - Tenkanen, Maija

AU - Penttilä, Merja

AU - de Vocht, Marcel L.

AU - Wösten, Han A.B.

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N2 - 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 α-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.

AB - 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 α-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.

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KW - filamentous fungi

KW - Trichoderma reesei

KW - proteins

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U2 - 10.1021/bm050676s

DO - 10.1021/bm050676s

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