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.
College of Light Textile Engineering & Art, Taiyuan University of Technology, Taiyuan 030024, PR China.
Int J Biol Macromol. 2015 Jan;72:658-63. doi: 10.1016/j.ijbiomac.2014.09.014. Epub 2014 Sep 19.
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.
在真菌的生长和形态中，水蛋白发挥着各种功能。这些蛋白质可以在亲水/疏水界面上自组装，形成两亲性膜。根据其物理性质和亲水性模式，水蛋白分为两类（I 类和 II 类）。为了鉴定重组的 I 类水蛋白 rHGFI，研究了 rHGFI 与典型的 II 类水蛋白 rHFBI 之间的不同性质。与 rHGFI 不同，rHFBI 涂覆云母表面上没有观察到棒状结构，并且 rHFBI 在硅化玻璃表面上形成的膜不够坚固，无法抵抗 60%乙醇和 2%热 SDS 的处理。相比之下，rHGFI 在硅化玻璃表面上形成的膜非常坚固，可以抵抗热洗涤剂和酒精溶液的洗涤。此外，rHFBI 在水-气界面上的自组装并没有伴随着二级结构的变化。同时，rHGFI 在水-气界面上自组装后，β-折叠结构显著增加，这导致了硫黄素 T 的荧光强度增加和刚果红和 CD 吸收光谱的位移。用 rHGFI 和 rHFBI 制备的不溶于水的曙红 B 分散体都稳定了一个多月，这表明曙红 B 与 rHGFI/rHFBI 之间的相互作用很强。这可能促进 rHGFI 和 rHFBI 被认为是稳定不溶于水的曙红 B 的潜在分散剂。
