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Structural analysis and allergenicity assessment of an enzymatically cross-linked bovine α-lactalbumin polymer

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Abstract

Enzymatic cross-linking is frequently used in bio-processing of dairy products since it could change the physiochemical and functional characterization. In our study, bovine α-lactalbumin was cross-linked by polyphenol oxidase from Agaricus bisporus and the changes in the structure, digestibility and allergenicity of α-lactalbumin were explored after cross-linking, and the structural alterations of the polymers were analyzed by circular dichroism spectroscopy, ultraviolet absorption spectroscopy and fluorescence spectroscopy. The digestibility of cross-linked α-lactalbumin was evaluated by simulated digestion in vitro. After that, the allergenicity of α-lactalbumin polymers was evaluated by detection of the specific IgE binding ability using an animal model. The results showed that the secondary and tertiary structures of various α-lactalbumin polymers exhibited a significant variation compared with those of untreated α-lactalbumin, and the cross-linked α-lactalbumin was relatively less susceptible to digestion. Moreover, the allergenicity of cross-linked polymers decreased significantly. These results suggested that there was a direct correlation between a loss of an α-helix and IgE binding to α-lactalbumin, which indicated that enzymatic cross-linking might be an efficient approach to reduce the allergenicity of bovine α-lactalbumin.

Graphical abstract: Structural analysis and allergenicity assessment of an enzymatically cross-linked bovine α-lactalbumin polymer

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Article information


Submitted
24 Sep 2019
Accepted
09 Nov 2019
First published
09 Dec 2019

Food Funct., 2020, Advance Article
Article type
Paper

Structural analysis and allergenicity assessment of an enzymatically cross-linked bovine α-lactalbumin polymer

X. Li, H. Bai, Y. Wu, W. Cheng, Y. Wu, Z. Wu, A. Yang, P. Tong and H. Chen, Food Funct., 2020, Advance Article , DOI: 10.1039/C9FO02238D

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