Abstract
A number of studies were devoted to understanding an immunological effect of pressure-treated β-lactoglobulin. In our previous work we have proved that high pressure significantly modifies β-lactoglobulin conformation and consequently its physicochemical properties. Here, structure of β-lactoglobulin complex with myristic acid determined at the highest accepted by the crystal pressure value of 550 MPa is reported. Our results structurally prove that pressure noticeably modifies positions of the major β-lactoglobulin epitopes. Considering the biological impact of observed changes in epitope regions, high pressure β-lactoglobulin structure presents a step forward in understanding the pressure modification of food protein allergenicity. The conformational changes of pressurized β-lactoglobulin did not support the hypothesis that proteolytic digestion facilitated by pressure is caused by an exposure of the digestive sites. Our findings demonstrate that high pressure protein crystallography can potentially identify the most pressure-sensitive fragments in allergens, and can therefore support development of hypoallergenic food products.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
