title: Identification properties of a recombinant class I hydrophobin rHGFI.
abstract: Hydrophobins fulfill various functions in fungal growth and morphology. These proteins can self-assemble at hydrophilic/hydrophobic interfaces and form amphipathic membranes. Based on their physical properties and hydropathy patterns, hydrophobins are divided into two classes (I and II). In order to identify the recombinant class I hydrophobin rHGFI, the different properties between rHGFI and the typical class II hydrophobin rHFBI were investigated. In contrast to rHGFI, no rodlet structure was observed on rHFBI coated mica surface, and the membranes formed on siliconized glass surfaces by rHFBI were not robust enough to resist treatment with 60% ethanol and 2% hot SDS. In contrast, the membranes formed by rHGFI on siliconized glass surfaces were so strong that could resist hot detergent and alcohol solution washing. Moreover, self-assembly of rHFBI at the water-air interface was not accompanied by a change in secondary structure. Meanwhile, β-sheet structures dramatically increased after rHGFI self-assembled at water-air interface, which could cause the fluorescence intensity of Thioflavin T increased and Congo Red and CD absorption spectra shift. Water-insoluble erythrosin B dispersion prepared with rHGFI and rHFBI were both stable for more than one month, which indicated that the interaction between erythrosin B and rHGFI/rHFBI was strong. This might promote rHGFI and rHFBI to be considered as potential dispersing agents to stabilize water-insoluble erythrosin B.
authors.affiliation: Key Laboratory of Interface Science and Engineering in Advanced Materials, Taiyuan University of Technology, Ministry of Education, Taiyuan 030024, PR China; College of Materials Science and Engineering, Taiyuan University of Technology, Taiyuan 030024, PR China.
authors.forename: Wenfeng
authors.initials: W
authors.lastname: Li
authors.affiliation: College of Light Textile Engineering & Art, Taiyuan University of Technology, Taiyuan 030024, PR China.
authors.forename: Yanbo
authors.initials: Y
authors.lastname: Gong
authors.affiliation: State Key Laboratory of Medicinal Chemical Biology, College of Life Sciences, Nankai University, Tianjin 300071, PR China.
authors.forename: Haijin
authors.initials: H
authors.lastname: Xu
authors.affiliation: State Key Laboratory of Medicinal Chemical Biology, College of Life Sciences, Nankai University, Tianjin 300071, PR China. Electronic address: Mingqiangqiao@live.com.
authors.forename: Mingqiang
authors.initials: M
authors.lastname: Qiao
authors.affiliation: Key Laboratory of Interface Science and Engineering in Advanced Materials, Taiyuan University of Technology, Ministry of Education, Taiyuan 030024, PR China; College of Materials Science and Engineering, Taiyuan University of Technology, Taiyuan 030024, PR China. Electronic address: blniunankai@hotmail.com.
authors.forename: Baolong
authors.initials: B
authors.lastname: Niu
mesh_terms: D003224:Congo Red; D004923:Erythrosine / Q000737:chemistry / Q000378:metabolism; D005285:Fermentation; D005656:Fungal Proteins / Q000737:chemistry / Q000235:genetics*; D048691:Grifola / Q000235:genetics; D010843:Pichia / Q000235:genetics; D017433:Protein Structure, Secondary / Q000235:genetics; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics*; D013499:Surface Properties; D014242:Trichoderma / Q000235:genetics; D014867:Water / Q000737:chemistry
chemical_list: D005656:Fungal Proteins; D011994:Recombinant Proteins; D014867:Water; D003224:Congo Red; D004923:Erythrosine
keywords: Hydrophobin; Rodlet structure; Self-assembly