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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Tsinghua University Press
2023-05-01
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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. |
format | Article |
id | doaj-art-04135b05221d4441bb295b889718e233 |
institution | Kabale University |
issn | 2213-4530 |
language | English |
publishDate | 2023-05-01 |
publisher | Tsinghua University Press |
record_format | Article |
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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