Cox Andrew R, Cagnol Florence, Russell Andrew B, Izzard Martin J
Unilever R&D Colworth, Colworth Park, Sharnbrook, Bedfordshire, United Kingdom.
Langmuir. 2007 Jul 17;23(15):7995-8002. doi: 10.1021/la700451g. Epub 2007 Jun 20.
We report the remarkable surface behavior of class II hydrophobin proteins HFBI and HFBII from Trichoderma reesei and the resulting effect that these proteins have on the stability of air bubbles to the process of disproportionation. The surface properties were studied using surface tensiometry and surface shear rheology. Surface tensiometry data show that hydrophobins are very surface active proteins, reducing the surface tension to approximately 30 mN m-1. The rate at which the hydrophobins adsorb at the surface may also be related to the self-assembly behavior in aqueous solution. We further show that hydrophobins form air/water surfaces with high elasticity, the magnitude of which is well in excess of that of surface layers formed by other common proteins used as foam or emulsion stabilizers. The measured surface properties translate to the stability of bubbles with adsorbed hydrophobin, and in this study, we demonstrate the ability of hydrophobin to have a dramatic effect on the rate of disproportionation in some simple bubble dissolution studies.
我们报道了里氏木霉II类疏水蛋白HFBI和HFBII显著的表面行为，以及这些蛋白质对气泡歧化过程稳定性的影响。使用表面张力测定法和表面剪切流变学研究了其表面性质。表面张力测定数据表明，疏水蛋白是非常具有表面活性的蛋白质，可将表面张力降低至约30 mN m-1。疏水蛋白在表面的吸附速率也可能与在水溶液中的自组装行为有关。我们进一步表明，疏水蛋白形成具有高弹性的空气/水表面，其弹性大小远超过用作泡沫或乳液稳定剂的其他常见蛋白质形成的表面层。所测量的表面性质转化为吸附有疏水蛋白的气泡的稳定性，在本研究中，我们在一些简单的气泡溶解研究中证明了疏水蛋白对歧化速率具有显著影响的能力。
