ArticleNutrients2021
Limited Lactosylation of Beta-Lactoglobulin from Cow's Milk Exerts Strong Influence on Antigenicity and Degranulation of Mast Cells.
Article in Nutrients, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Multiscale Structural Remodeling of Oleosins by Thermal Processing: Mechanisms and Implications for Allergenicity Modulation in Oilseed Crops.Comprehensive reviews in food science and food safety · 2026Review
- Tannin-Rich Chestnut and Persimmon Extracts in Puddings: Gelation, Proteins, and Antioxidant Activity.Gels (Basel, Switzerland) · 2026Article
- High-Temperature, Solid-Phase Reaction of α-Amino Groups in Peptides with Lactose and Glucose: An Alternative Mechanism Leading to an α-Ketoacyl Derivative.Journal of agricultural and food chemistry · 2023Article
- Diagnosis and Rationale for Action against Cow's Milk Allergy (DRACMA) Guidelines update - III - Cow's milk allergens and mechanisms triggering immune activation.The World Allergy Organization journal · 2022Article
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Authors and funding
10 authors.
Funding
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Abstract
backgroundbeta-lactoglobulin (BLG) is one of the major cow's milk proteins and the most abundant allergen in whey. Heating is a common technologic treatment applied during milk transformational processes. Maillardation of BLG in the presence of reducing sugars and elevated temperatures may influence its antigenicity and allergenicity. PRIMARY
objectiveto analyze and identify lactosylation sites by capillary electrophoresis mass spectrometry (CE-MS). SECONDARY
objectiveto assess the effect of lactosylated BLG on antigenicity and degranulation of mast cells.
methodsBLG was lactosylated at pH 7, a water activity (aw) of 0.43, and a temperature of 65 °C using a molar ratio BLG:lactose of 1:1 by incubating for 0, 3, 8, 16 or 24 h. For the determination of the effect on antibody-binding capacity of lactosylated BLG, an ELISA was performed. For the assessment of degranulation of the cell-line RBL-hεIa-2B12 transfected with the human α-chain, Fcε receptor type 1 (FcεRI) was used.
resultsBLG showed saturated lactosylation between 8 and 16 incubation hours in our experimental setup. Initial stage lactosylation sites L1 (N-terminus)-K47, K60, K75, K77, K91, K138 and K141-have been identified using CE-MS. Lactosylated BLG showed a significant reduction of both the IgG binding ( CONCLUSIONS AND CLINICAL RELEVANCE: this study shows that lactosylation of BLG decreases both the antigenicity and degranulation of mast cells and can therefore be a promising approach for reducing allergenicity of cow's milk allergens provided that the process is well-controlled.
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