Naturwissenschaftliche Fakultät der Leibniz Universität Hannover, Institut für Lebensmittelchemie, Hannover, Germany.
Biotechnol Appl Biochem. 2013 Mar-Apr;60(2):147-54. doi: 10.1002/bab.1077.
The pfah2 gene coding for a novel hydrophobin PfaH2 from the ascomycete Paecilomyces farinosus was identified during sequencing of random clones from a cDNA library. The corresponding protein sequence of PfaH2 deduced from the cDNA comprised 134 amino acids (aa). A 16 aa signal sequence preceded the N-terminus of the mature protein. PfaH2 belonged to the class Ia hydrophobins. The protein was isolated using trifluoroacetic acid extraction and purified via SDS-PAGE and high-performance liquid chromatography. The surface activity of the recently described PfaH1 and of PfaH2 was compared by the determination of contact angles (CAs) on glass slides and Teflon tape, and the CA of distilled water droplets was measured on glass slides coated with hydrophobin PfaH1 or PfaH2. Surprisingly, both hydrophobins adsorbed to hydrophilic surfaces and changed their physicochemical properties to a similar quantitative extent, although little aa sequence homology was found.
在对来自曲霉属的粉拟青霉 cDNA 文库中的随机克隆进行测序的过程中，鉴定了编码新型亲脂性蛋白 PfaH2 的 pfah2 基因。从 cDNA 推导出的 PfaH2 对应蛋白序列由 134 个氨基酸组成。成熟蛋白的 N 端前有一个 16 个氨基酸的信号序列。PfaH2 属于 I 类亲脂性蛋白。该蛋白使用三氟乙酸提取，通过 SDS-PAGE 和高效液相色谱进行纯化。通过测量玻璃载玻片和铁氟龙胶带的接触角（CA），比较了最近描述的 PfaH1 和 PfaH2 的表面活性，并在涂有亲脂性蛋白 PfaH1 或 PfaH2 的玻璃载玻片上测量了蒸馏水液滴的 CA。令人惊讶的是，尽管发现的氨基酸序列同源性很小，但两种亲脂性蛋白都吸附在亲水表面上，并将其物理化学性质改变到相似的定量程度。
