Structure and allergenicity of α-lactalbumin: effects of ultrasonic prior to glycation and subsequent phosphorylation

Bovine α-lactalbumin (BLA) induced severe cow's milk allergy. In this study, a novel strategy combining ultrasonication, performed before glycation, and phosphorylation was proposed to reduce BLA allergenicity. Result showed that IgE- and IgG-binding capacities and the release rates of histamin...

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Main Authors: Wenmei Chen, Qiongzhen Chen, Houze Zhou, Yanhong Shao, Yang Wang, Jun Liu, Zongcai Tu
Format: Article
Language:English
Published: Tsinghua University Press 2023-05-01
Series:Food Science and Human Wellness
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Online Access:http://www.sciencedirect.com/science/article/pii/S2213453022002087
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author Wenmei Chen
Qiongzhen Chen
Houze Zhou
Yanhong Shao
Yang Wang
Jun Liu
Zongcai Tu
author_facet Wenmei Chen
Qiongzhen Chen
Houze Zhou
Yanhong Shao
Yang Wang
Jun Liu
Zongcai Tu
author_sort Wenmei Chen
collection DOAJ
description Bovine α-lactalbumin (BLA) induced severe cow's milk allergy. In this study, a novel strategy combining ultrasonication, performed before glycation, and phosphorylation was proposed to reduce BLA allergenicity. Result showed that IgE- and IgG-binding capacities and the release rates of histamine and interleukin-6 from RBL-2H3 were reduced. Moreover, intrinsic fluorescence intensity and surface hydrophobicity were decreased, whereas glycated sites (R10, N44, K79, K108, N102 and K114) and phosphorylated sites (Y36 and S112) of BLA were increased. Minimum allergenicity was detected during BLA treatment after ultrasonic prior to glycation and subsequent phosphorylation because of considerable increase in glycated and phosphorylated sites. Therefore, the decrease in allergenicity of BLA, the effect correlated well with the shielding effect of glycated sites combined with phosphorylated sites and the conformational changes. This study provides important theoretical foundations for improving and using the ultrasonic technology combined with protein modification in allergenic protein processing.
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series Food Science and Human Wellness
spelling doaj-art-04135b05221d4441bb295b889718e2332025-02-03T05:15:35ZengTsinghua University PressFood Science and Human Wellness2213-45302023-05-01123825831Structure and allergenicity of α-lactalbumin: effects of ultrasonic prior to glycation and subsequent phosphorylationWenmei Chen0Qiongzhen Chen1Houze Zhou2Yanhong Shao3Yang Wang4Jun Liu5Zongcai Tu6National R & D Center for Freshwater Fish Processing, College of Life Science, Jiangxi Normal University, Nanchang 330022, ChinaNational R & D Center for Freshwater Fish Processing, College of Life Science, Jiangxi Normal University, Nanchang 330022, ChinaNational R & D Center for Freshwater Fish Processing, College of Life Science, Jiangxi Normal University, Nanchang 330022, ChinaNational R & D Center for Freshwater Fish Processing, College of Life Science, Jiangxi Normal University, Nanchang 330022, ChinaNational R & D Center for Freshwater Fish Processing, College of Life Science, Jiangxi Normal University, Nanchang 330022, ChinaNational R & D Center for Freshwater Fish Processing, College of Life Science, Jiangxi Normal University, Nanchang 330022, China; Corresponding authors at: College of Life Science, Jiangxi Normal University, Nanchang 330022, ChinaNational R & D Center for Freshwater Fish Processing, College of Life Science, Jiangxi Normal University, Nanchang 330022, China; State Key Laboratory of Food Science and Technology, Nanchang University, Nanchang 330047, China; Corresponding authors at: College of Life Science, Jiangxi Normal University, Nanchang 330022, ChinaBovine α-lactalbumin (BLA) induced severe cow's milk allergy. In this study, a novel strategy combining ultrasonication, performed before glycation, and phosphorylation was proposed to reduce BLA allergenicity. Result showed that IgE- and IgG-binding capacities and the release rates of histamine and interleukin-6 from RBL-2H3 were reduced. Moreover, intrinsic fluorescence intensity and surface hydrophobicity were decreased, whereas glycated sites (R10, N44, K79, K108, N102 and K114) and phosphorylated sites (Y36 and S112) of BLA were increased. Minimum allergenicity was detected during BLA treatment after ultrasonic prior to glycation and subsequent phosphorylation because of considerable increase in glycated and phosphorylated sites. Therefore, the decrease in allergenicity of BLA, the effect correlated well with the shielding effect of glycated sites combined with phosphorylated sites and the conformational changes. This study provides important theoretical foundations for improving and using the ultrasonic technology combined with protein modification in allergenic protein processing.http://www.sciencedirect.com/science/article/pii/S2213453022002087Bovine α-lactalbuminAllergenicityUltrasonicProtein modification
spellingShingle Wenmei Chen
Qiongzhen Chen
Houze Zhou
Yanhong Shao
Yang Wang
Jun Liu
Zongcai Tu
Structure and allergenicity of α-lactalbumin: effects of ultrasonic prior to glycation and subsequent phosphorylation
Food Science and Human Wellness
Bovine α-lactalbumin
Allergenicity
Ultrasonic
Protein modification
title Structure and allergenicity of α-lactalbumin: effects of ultrasonic prior to glycation and subsequent phosphorylation
title_full Structure and allergenicity of α-lactalbumin: effects of ultrasonic prior to glycation and subsequent phosphorylation
title_fullStr Structure and allergenicity of α-lactalbumin: effects of ultrasonic prior to glycation and subsequent phosphorylation
title_full_unstemmed Structure and allergenicity of α-lactalbumin: effects of ultrasonic prior to glycation and subsequent phosphorylation
title_short Structure and allergenicity of α-lactalbumin: effects of ultrasonic prior to glycation and subsequent phosphorylation
title_sort structure and allergenicity of α lactalbumin effects of ultrasonic prior to glycation and subsequent phosphorylation
topic Bovine α-lactalbumin
Allergenicity
Ultrasonic
Protein modification
url http://www.sciencedirect.com/science/article/pii/S2213453022002087
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