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Main Title: Immunological Analysis of Isothiocyanate-Modified α-Lactalbumin Using High-Performance Thin Layer Chromatography
Author(s): Spöttel, Jenny
Brockelt, Johannes
Badekow, Svenja
Rohn, Sascha
Type: Article
Language Code: en
Abstract: Undirected modifications between food proteins and secondary plant metabolites can occur during food processing. The results of covalent interactions can alter the functional and biological properties of the proteins. The present work studied the extent of which covalent conjugation of the bioactive metabolite benzyl isothiocyanate (BITC; a glucosinolate breakdown product) to the whey protein α-lactalbumin affects the protein’s allergenicity. Additional to the immunological analysis of native untreated and BITC-modified α-lactalbumin, the analysis of antigenic properties of proteolytically digested protein derivatives was also performed by high performance thin layer chromatography and immunostaining. As a result of the chemical modifications, structural changes in the protein molecule affected the allergenic properties. In this process, epitopes are destroyed or inactivated, but at the same time, buried epitopes can be exposed or newly formed, so that the net effect was an increase in allergenicity, in this case. Results from the tryptic hydrolysis suggest that BITC conjugation sterically hindered the cleavage sites for the enzyme, resulting in reduced digestibility and allergenicity. Residual antigenicity can be still present as short peptide fragments that provide epitopes. The desire to make food safer for allergy sufferers and to protect sensitized individuals from an allergenic reaction makes it clear that the detection of food antigens is mandatory; especially by considering protein interactions.
Issue Date: 25-Mar-2021
Date Available: 12-Apr-2021
DDC Class: 540 Chemie und zugeordnete Wissenschaften
Subject(s): whey proteins
protein modifications
protein antigenicity
peptide antigenicity
HPTLC immunostaining
food processing
Journal Title: Molecules
Publisher: MDPI
Publisher Place: Basel
Volume: 26
Issue: 7
Article Number: 1842
Publisher DOI: 10.3390/molecules26071842
EISSN: 1420-3049
Appears in Collections:FG Lebensmittelchemie und Analytik » Publications

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