Food Colloids Group, School of Food Science and Nutrition, University of Leeds, Leeds, United Kingdom.
J Agric Food Chem. 2013 Feb 20;61(7):1554-62. doi: 10.1021/jf304603m. Epub 2013 Feb 6.
Class II hydrophobin (HFBII) is a very promising ingredient for improving food foam stability. Pure HFBII-stabilized bubbles exhibited exceptional stability to disproportionation (dissolution) but were not stable to bubble coalescence induced by a pressure drop. Bubbles stabilized by mixtures of HFBII + sodium caseinate (SC) or β-lactoglobulin (BL) showed decreased shrinkage rates compared to pure SC or BL and improved the stability to pressure-drop-induced coalescence. Higher bubble stability was more closely correlated with higher surface shear viscosity than the surface dilatational elasticity of the mixed protein systems. Brewster angle microscopy observations and the high shear strength of adsorbed films, including HFBII, even in the presence of hydrophobic and hydrogen-bond-breaking agents, confirm that intermolecular attractive cross-links are unlikely to be the origin of the high strength of HFBII films. Possibly the HFBII molecules form a tightly interlocking monolayer of Janus-like particles at the air-water interface.
II 类疏水蛋白（HFBII）是一种很有前途的改善食品泡沫稳定性的成分。纯 HFBII 稳定的气泡表现出对歧化（溶解）的异常稳定性，但对由压降引起的气泡聚结不稳定。由 HFBII+酪蛋白酸钠（SC）或β-乳球蛋白（BL）混合物稳定的气泡与纯 SC 或 BL 相比，收缩率降低，并且改善了对压降诱导的聚结的稳定性。更高的气泡稳定性与更高的表面剪切粘度更密切相关，而不是混合蛋白体系的表面拉伸弹性。掠入射显微镜观察和吸附膜的高剪切强度，包括 HFBII，即使存在疏水性和破坏氢键的试剂，也证实分子间吸引力的交联不太可能是 HFBII 膜高强度的原因。可能 HFBII 分子在气-水界面形成紧密互锁的类似 Janus 的粒子单层。
