Interfacial study of class II hydrophobin and its mixtures with milk proteins: relationship to bubble stability.
作者： Yiwei Wang , Cédric Bouillon , Andrew Cox , Eric Dickinson , Kalpana Durga
DOI: 10.1021/JF304603M
关键词:
摘要: 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 bubble coalescence induced by pressure drop. Bubbles stabilized mixtures of HFBII + sodium caseinate (SC) or β-lactoglobulin (BL) showed decreased shrinkage rates compared pure SC BL and improved the pressure-drop-induced coalescence. Higher was more closely correlated with higher surface shear viscosity than dilatational elasticity mixed protein systems. Brewster angle microscopy observations high strength adsorbed films, including HFBII, even in presence hydrophobic hydrogen-bond-breaking agents, confirm that intermolecular attractive cross-links are unlikely be origin films. Possibly molecules form tightly interlocking monolayer Janus-like particles at air-water interface.
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