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Effect of Pulsed Light treatment on β-lactoglobulin immunoreactivity
This study investigates the effects of different Pulsed Light (PL) treatments (from 4 to 16 J/cm2 of total fluence) on the immunoreactivity and digestibility of β-lactoglobulin (β-lg), one of the main allergens in milk. Our findings show that PL significantly decreases the recognition of β-lg by bot...
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Published in: | Food science & technology 2019-09, Vol.112, p.108231, Article 108231 |
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Main Authors: | , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | This study investigates the effects of different Pulsed Light (PL) treatments (from 4 to 16 J/cm2 of total fluence) on the immunoreactivity and digestibility of β-lactoglobulin (β-lg), one of the main allergens in milk.
Our findings show that PL significantly decreases the recognition of β-lg by both IgG and IgE, up to an average 85% and 45% of reduction, respectively, compared to the untreated protein, especially when the protein is treated in a solution at pH 6.8. The reduction in IgE binding was also evidenced in acid and sweet whey. However, in this product, the presence of other components could protect the protein from denaturation by the effect of light, and only a maximum reduction of 37% in IgE-binding was achieved. Moreover, this work has confirmed that PL treatment may also contribute to accelerate protein digestibility, under simulated gastric conditions (pepsin digestion).
Our results suggest that this technology, under the suitable conditions, could be used as a valuable alternative treatment for reducing the immunoreactivity of allergenic proteins. Also, we reveal new findings on the allergen modifications due to food processing, that will improve knowledge-based ways to managing allergens risks in food industry.
•Pulsed Light is an efficient non-thermal process to alter the conformation of proteins.•PL modifies the β-lactoglobulin (β-lg) structure favoring protein aggregation.•These changes are reflected in a reduced IgG- and IgE-binding to the allergen.•Results have confirmed that PL also increases protein digestibility. |
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ISSN: | 0023-6438 1096-1127 |
DOI: | 10.1016/j.lwt.2019.05.129 |