Effects of ohmic heating on the immunoreactivity of beta-lactoglobulin - a relationship towards structural aspects

• Type: Article in International Scientific Journal
• Date: 2020

Authors

Pereira, RN (Author) Other; Joana Costa (Author) FFUP; Rodrigues, RM (Author) Other; Villa, C (Author) Other; Machado, L (Author) Other; Mafra, I (Author) Other; Vicente, A (Author) Other

Journal

Title: Food and Function

Vol. 11

Pages: 4002-4013

ISSN: 2042-6496

Publisher: Royal Society of Chemistry

Indexing

ISI Web of Knowledge - 0 Citations

Scopus - 5 Citations

Other information

Authenticus ID: P-00S-8HA

DOI: 10.1039/c9fo02834j

Abstract (EN): beta-Lactoglobulin (beta-LG) encompasses important biological functions, but it is also a major milk allergen, being responsible for the high incidence of cow's milk allergy in childhood. Despite numerous studies addressing the effect of thermal processing on the immunoreactivity of beta-LG, little is known about the impact of emergent food processing technologies, such as ohmic heating (OH), on its immunoreactivity. This study describes, for the first time, the effects of thermal and electric effects of OH on the immunoreactivity of beta-LG. The influence of high-temperature short time (HTST; 72.5 degrees C for 15 and 90 degrees C for 1 s) and low-temperature long time (LTLT; 65 degrees C for 30 min) pasteurization binomials combined with different electrical variables (electric field intensity and electrical frequency) was evaluated and compared with that of conventional heating. HTST at 90 degrees C for 1 s extensively affects the protein secondary structure and increases the levels of reactive aggregates, resulting in increased total immunoreactivity (assessed by ELISA and immunoblotting). OH at 4 V cm(-1) and a frequency of 25 kHz reduced the immunoreactivity of monomeric beta-LG and its resultant aggregates, compared with conventional heat treatments. In contrast, the presence of electric fields (4 V cm(-1) and 25 kHz) during LTLT increased the immunoreactivity of monomeric beta-LG. The thermal and electrical variables of OH change the balance between monomeric and aggregated forms of beta-LG, affecting their ability to bind specific antibodies. These outcomes bring novel insights into how to modulate OH aiming at reducing the allergenic potential of beta-LG based products.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 12