Yang Jiuxia, Ge Lu, Song Bo, Ma Zhongqiang, Yang Xiaotian, Wang Bo, Dai Yixin, Xu Haijin, Qiao Mingqiang
NHC Key Laboratory of Critical Care Medicine, Tianjin First Central Hospital, Tianjin, China.
The Key Laboratory of Molecular Microbiology and Technology, Ministry of Education, College of Life Sciences, Nankai University, Tianjin, China.
Front Microbiol. 2022 Sep 9;13:990231. doi: 10.3389/fmicb.2022.990231. eCollection 2022.
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 ) 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 () from the mycelium of with a much higher transcriptional level than . Heterologous expression of was accomplished in the . 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.
疏水蛋白是丝状真菌产生的小蛋白，具有显著的自组装特性，具有很大的潜力，例如作为药物载体和抗菌剂，但需要具有改进特性的不同疏水蛋白。HGFI（一种来自……的疏水蛋白）是I类疏水蛋白，它可以自组装成长度范围为100 - 150 nm的杆状结构。在本研究中，我们从……的菌丝体中鉴定出一个新的疏水蛋白基因（……），其转录水平比……高得多。……中实现了……的异源表达。X射线光电子能谱和水接触角测定表明，HGFII可以在气固界面自组装成蛋白质膜，圆二色性和硫黄素T荧光研究表明，这种效应伴随着α - 螺旋含量的减少和β - 折叠含量的增加。使用原子力显微镜显示，HGFII自组装成直径为15 - 30 nm的杆状结构，表明它是I类疏水蛋白，其自组装行为与HGFI不同。HGFII的表面疏水性比HGFI强，同时，在乳化试验中，HGFII对大豆油的分散能力比HGFI更好，产生更稳定、更持久的乳液。
