A novel hydrophobin encoded by hgfII from Grifola frondosa exhibiting excellent self-assembly ability
Hydrophobins are small proteins from filamentous fungi, which have remarkable self-assembly properties of great potential, e.g., as drug carriers and as anti-bacterial agents, but different hydrophobins, with improved properties, are needed. HGFI (a hydrophobin from Grifola frondosa) is a class I hy...
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2022-09-01
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| Series: | Frontiers in Microbiology |
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| Online Access: | https://www.frontiersin.org/articles/10.3389/fmicb.2022.990231/full |
| _version_ | 1798003401997418496 |
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| author | Jiuxia Yang Jiuxia Yang Lu Ge Bo Song Zhongqiang Ma Xiaotian Yang Bo Wang Yixin Dai Haijin Xu Haijin Xu Mingqiang Qiao Mingqiang Qiao |
| author_facet | Jiuxia Yang Jiuxia Yang Lu Ge Bo Song Zhongqiang Ma Xiaotian Yang Bo Wang Yixin Dai Haijin Xu Haijin Xu Mingqiang Qiao Mingqiang Qiao |
| author_sort | Jiuxia Yang |
| collection | DOAJ |
| description | Hydrophobins are small proteins from filamentous fungi, which have remarkable self-assembly properties of great potential, e.g., as drug carriers and as anti-bacterial agents, but different hydrophobins, with improved properties, are needed. HGFI (a hydrophobin from Grifola frondosa) is a class I hydrophobin, which can self-assemble into rodlet structures with a length range 100–150 nm. In this study, we identified a new hydrophobin gene (hgfII) from the mycelium of G. frondosa with a much higher transcriptional level than hgfI. Heterologous expression of hgfII was accomplished in the Pichia pastoris. X-ray photoelectron spectroscopy and water contact angle assay measurements revealed that HGFII can self-assemble into a protein film at the air–solid interface, with circular dichroism and thioflavin T fluorescence studies showing that this effect was accompanied by a decrease in α-helix content and an increase in β-sheet content. Using atomic force microscopy, it was shown that HGFII self-assembled into rodlet-like structures with a diameter of 15–30 nm, showing that it was a class I hydrophobin, with self-assembly behavior different from HGFI. The surface hydrophobicity of HGFII was stronger than that of HGFI, meanwhile, in emulsification trials, HGFII displayed better dispersive capacity to the soybean oil than HGFI, producing a more stable and durable emulsion. |
| first_indexed | 2024-04-11T12:07:00Z |
| format | Article |
| id | doaj.art-1635a92fb00b447db29e817d8e797ce4 |
| institution | Directory Open Access Journal |
| issn | 1664-302X |
| language | English |
| last_indexed | 2024-04-11T12:07:00Z |
| publishDate | 2022-09-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Microbiology |
| spelling | doaj.art-1635a92fb00b447db29e817d8e797ce42022-12-22T04:24:42ZengFrontiers Media S.A.Frontiers in Microbiology1664-302X2022-09-011310.3389/fmicb.2022.990231990231A novel hydrophobin encoded by hgfII from Grifola frondosa exhibiting excellent self-assembly abilityJiuxia Yang0Jiuxia Yang1Lu Ge2Bo Song3Zhongqiang Ma4Xiaotian Yang5Bo Wang6Yixin Dai7Haijin Xu8Haijin Xu9Mingqiang Qiao10Mingqiang Qiao11NHC Key Laboratory of Critical Care Medicine, Tianjin First Central Hospital, Tianjin, ChinaThe Key Laboratory of Molecular Microbiology and Technology, Ministry of Education, College of Life Sciences, Nankai University, Tianjin, ChinaThe Key Laboratory of Molecular Microbiology and Technology, Ministry of Education, College of Life Sciences, Nankai University, Tianjin, ChinaThe Key Laboratory of Bioactive Materials, Ministry of Education, College of Life Sciences, Nankai University, Tianjin, ChinaThe Key Laboratory of Molecular Microbiology and Technology, Ministry of Education, College of Life Sciences, Nankai University, Tianjin, ChinaThe Key Laboratory of Molecular Microbiology and Technology, Ministry of Education, College of Life Sciences, Nankai University, Tianjin, ChinaThe Key Laboratory of Molecular Microbiology and Technology, Ministry of Education, College of Life Sciences, Nankai University, Tianjin, ChinaThe Key Laboratory of Bioactive Materials, Ministry of Education, College of Life Sciences, Nankai University, Tianjin, ChinaThe Key Laboratory of Molecular Microbiology and Technology, Ministry of Education, College of Life Sciences, Nankai University, Tianjin, ChinaThe Key Laboratory of Bioactive Materials, Ministry of Education, College of Life Sciences, Nankai University, Tianjin, ChinaThe Key Laboratory of Molecular Microbiology and Technology, Ministry of Education, College of Life Sciences, Nankai University, Tianjin, ChinaThe Key Laboratory of Bioactive Materials, Ministry of Education, College of Life Sciences, Nankai University, Tianjin, ChinaHydrophobins are small proteins from filamentous fungi, which have remarkable self-assembly properties of great potential, e.g., as drug carriers and as anti-bacterial agents, but different hydrophobins, with improved properties, are needed. HGFI (a hydrophobin from Grifola frondosa) is a class I hydrophobin, which can self-assemble into rodlet structures with a length range 100–150 nm. In this study, we identified a new hydrophobin gene (hgfII) from the mycelium of G. frondosa with a much higher transcriptional level than hgfI. Heterologous expression of hgfII was accomplished in the Pichia pastoris. X-ray photoelectron spectroscopy and water contact angle assay measurements revealed that HGFII can self-assemble into a protein film at the air–solid interface, with circular dichroism and thioflavin T fluorescence studies showing that this effect was accompanied by a decrease in α-helix content and an increase in β-sheet content. Using atomic force microscopy, it was shown that HGFII self-assembled into rodlet-like structures with a diameter of 15–30 nm, showing that it was a class I hydrophobin, with self-assembly behavior different from HGFI. The surface hydrophobicity of HGFII was stronger than that of HGFI, meanwhile, in emulsification trials, HGFII displayed better dispersive capacity to the soybean oil than HGFI, producing a more stable and durable emulsion.https://www.frontiersin.org/articles/10.3389/fmicb.2022.990231/fullGrifola frondosamyceliumhydrophobinself-assemblysurface hydrophobicity |
| spellingShingle | Jiuxia Yang Jiuxia Yang Lu Ge Bo Song Zhongqiang Ma Xiaotian Yang Bo Wang Yixin Dai Haijin Xu Haijin Xu Mingqiang Qiao Mingqiang Qiao A novel hydrophobin encoded by hgfII from Grifola frondosa exhibiting excellent self-assembly ability Frontiers in Microbiology Grifola frondosa mycelium hydrophobin self-assembly surface hydrophobicity |
| title | A novel hydrophobin encoded by hgfII from Grifola frondosa exhibiting excellent self-assembly ability |
| title_full | A novel hydrophobin encoded by hgfII from Grifola frondosa exhibiting excellent self-assembly ability |
| title_fullStr | A novel hydrophobin encoded by hgfII from Grifola frondosa exhibiting excellent self-assembly ability |
| title_full_unstemmed | A novel hydrophobin encoded by hgfII from Grifola frondosa exhibiting excellent self-assembly ability |
| title_short | A novel hydrophobin encoded by hgfII from Grifola frondosa exhibiting excellent self-assembly ability |
| title_sort | novel hydrophobin encoded by hgfii from grifola frondosa exhibiting excellent self assembly ability |
| topic | Grifola frondosa mycelium hydrophobin self-assembly surface hydrophobicity |
| url | https://www.frontiersin.org/articles/10.3389/fmicb.2022.990231/full |
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