Changes in Interfacial and Emulsifying Properties of β-Lactoglobulin Protein during Its Fibrillation

doi:10.7506/spkx1002-6630-201806004

Abstract

Abstract: When heated under acidic conditions, protein is self-assembled into fibrils. In this paper, the formation of β-lactoglobulin protein fibrils was characterized by fluorescence spectroscopy and transmission electron microscopy (TEM). Interfacial adsorption and interfacial viscoelasticity of the samples at different fibrillation stages were analyzed with an interfacial rheometer, and then their emulsifying behaviors were studied. Different interfacial and emulsifying properties of the dispersions from different fibrillation stages were observed. The interfacial adsorption ability and the viscoelasticity of the dispersions were increased as fibrillation progressed. Stable emulsions with average droplet size (D[3,2]) ranging from 8.5 to 10.5 μm could be formed from the fibrillation products at different stages, and the emulsifying capacity of the dispersions were shown to be increased with increasing degree of fibrillation. However, excessive fibrillation had a negative effect on the storage stability of the emulsions.

Key words: β-lactoglobulin, nanofibril, interfacial property, emulsifying property

CLC Number:

TS252.1

HUANG Ying, GAO Zhiming, WU Binxian, LIN Zhantuo, ZHAO Junjun, FANG Yapeng. Changes in Interfacial and Emulsifying Properties of β-Lactoglobulin Protein during Its Fibrillation[J]. FOOD SCIENCE, 2018, 39(6): 20-25.

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Changes in Interfacial and Emulsifying Properties of β-Lactoglobulin Protein during Its Fibrillation

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