中文摘要：

将巴斯德毕赤酵母异源表达出的疏水蛋白rHGFI和rHFBI修饰硅化玻璃后进行玻璃表面接触角测定.结果显示：蛋白处理的硅化玻璃表面由疏水变为亲水.蛋白溶液表面张力测定结果表明：rHGFI和rHFBI是表面活性非常强的蛋白,均可使表面张力降低.以常用的食品乳化剂酪蛋白酸钠为对照,检测rHGFI和rHFBI蛋白的发泡能力和泡沫稳定性.0.1%的rHGFI和rHFBI蛋白溶液发泡能力明显高于同浓度的酪蛋白酸钠溶液,rHFBI蛋白溶液的泡沫稳定性最佳.

英文摘要：

After the hydrophobins HGFI and HFBI had been heterologously expressed in Pichia pastoris,the recombinant protein rHGFI and rHFBI were purified by ultrafiltration.Water contact angle measurement indicated that both recombinant hydrophobins could reserve the hydrophilic-hydrophobic character of a siliocnized glass surface.A further data of surface tensiometry showed that rHGFI and rHFBI were very surface active proteins,reducing the surface tension to 46.7mN/m and 41.6mN/m respectively.The foam capability and stability of aerated solutions containing rHGFI or rHFBI had been investigated and compared with another typical food aerating agent and emulsifier sodium caseinate（Na-Cas）.The magnitude of foam capability of hydrophobins was well excess of that formed by Na-Cas.The foam stability of rHGFI protein solution.however,was not as well as the one of rHFBI solution.Their stability effect was far better than the food-aerating agent Na-Cas.