Abstract
Under specific processing conditions, globular food protein can form amyloid fibrils with excellent functional properties in food processing. Amyloid fibrils can be adsorbed on the surface of oil droplets to improve the stability of oil-in-water emulsion. The protein can form monomers oligomers, protofibrils and mature fibrils of which the concentrations increase with the prolonging acidic-heating time. However, the structural advantages of these aggregates when adsorbing at oil-water interface are unclear and the emulsifying ability and adsorption mechanism of food protein amyloid fibrils with different morphology at oil-water interface need to be studied in depth. Herein, four kinds of soy protein amyloid fibrils (SAFs) with distinct morphology were prepared by changing the acidic heating time (3, 6, 12 and 24 h), which were referred as SAFs-3, SAFs-6, SAFs-12 and SAFs-24. Their interfacial adsorption behavior at the oil-water interface were studied systematically by three-phase contact angle, interfacial tension, CLSM, Cryo-SEM and other characterization techniques. The results suggested that the length and flexibility of the fibrils have a great influence on the interface properties, including the rheological properties such as viscosity and modulus. These properties determine the emulsifying capacity of the fibrils. The emulsion stabilized by SAFs-12 was the most resistant to coalescence because SAFs-12 formed a stronger interfacial layer around the oil droplets and a denser viscoelastic network in the continuous phase. In our study, a stabilizing emulsion was prepared using SAFs, which provided potential applications for amyloid fibrils in the food field.
Published Version
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