Conformational changes in bovine α-lactalbumin and β-lactoglobulin evoked by interaction with C18 unsaturated fatty acids provide insights into increased allergic …

X Meng, Z Zeng, J Gao, P Tong, Y Wu, X Li, H Chen - Food & function, 2020 - pubs.rsc.org
Bovine α-lactalbumin (BLA) and β-lactoglobulin (BLG) are the most common and severe
food allergens in milk and they can bind C18 unsaturated fatty acids (UFAs) and their …

Dietary linolenic acid increases sensitizing and eliciting capacities of cow's milk whey proteins in BALB/c mice

X Meng, Y Wu, X Wen, J Gao, Y Xie, X Zhao, J Yuan… - Nutrients, 2022 - mdpi.com
α-Lactalbumin (BLA) and β-lactoglobulin (BLG) are the major whey proteins causing allergic
reactions. Polyunsaturated fatty acids (PUFAs) stand among the extrinsic factors of the food …

[HTML][HTML] The conformational structural change of β-lactoglobulin via acrolein treatment reduced the allergenicity

L Lv, X Qu, N Yang, I Ahmed - Food chemistry: X, 2021 - Elsevier
Abstract β-lactoglobulin (BLG) is a major allergen of milk. Since lipid peroxidation such as
acrolein commonly exists during milk processing, it is necessary to evaluate its influence on …

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

W Chen, Q Chen, H Zhou, Y Shao, Y Wang… - Food Science and …, 2023 - Elsevier
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 …

Deciphering the competitive binding interaction of β-lactoglobulin with benzaldehyde and vanillic acid via high-spatial-resolution multi-spectroscopic

R Zhang, W Jia - Food Hydrocolloids, 2023 - Elsevier
Interaction between protein and added flavor constituents strongly affects the sensory quality
and consumer acceptability of dairy products. Here, the molecular basis of how …

Potential allergenicity response to structural modification of irradiated bovine α-lactalbumin

X Meng, X Li, X Wang, J Gao, H Yang, H Chen - Food & function, 2016 - pubs.rsc.org
Bovine α-lactalbumin (α-La) is a major food allergen found in milk and is characterized by
high conformational stability because of its four disulfide bridges and being calcium bound …

The mechanism of the reduction in allergenic reactivity of bovine α-lactalbumin induced by glycation, phosphorylation and acetylation

J Liu, W Chen, Y Shao, J Zhang, Z Tu - Food chemistry, 2020 - Elsevier
Bovine α-lactalbumin (α-Lac) allergy is a common health problem. This study assesses the
allergenic reactivity and the structural properties of α-Lac after protein modification …

Bovine β-lactoglobulin covalent modification by flavonoids: Effect on the allergenicity and human intestinal microbiota

J Liu, Y Wang, Z Tu, W Chen… - Journal of Agricultural and …, 2021 - ACS Publications
The present study aims to investigate the structure of covalent conjugates of bovine β-
lactoglobulin (BLG) and flavonoids (luteolin, myricetin, and hyperoside), and their effect on …

Reducing the allergenicity of α-lactalbumin after lipid peroxidation

L Lv, K He, F Sun, X Lin, L Ye, Y Lyu, L Liu… - Journal of Agricultural …, 2021 - ACS Publications
This study analyzed the effect of lipid peroxidation using 2, 2′-azobis (2-amidinopropane)
dihydrochloride (AAPH) and acrolein on the in vitro and in vivo allergenicity of α-lactalbumin …

Potential allergenicity assessment after bovine apo‐α‐lactalbumin binding to calcium ion

M Huang, X Li, P Tong, J Gao, J Yuan… - Journal of Food …, 2020 - Wiley Online Library
Bovine α‐lactalbumin (α‐LA) is recognized as a major milk allergen. Generally, α‐LA in the
natural state combines with a calcium ion, however, some studies have shown that calcium …