Assessment of transglutaminase catalyzed cross-linking on the potential allergenicity and conformation of heterologous protein polymers

Transglutaminase (TGase)-mediated cross-linking has gained significant attention due to its potential to reduce the allergenicity of food proteins. This study investigates the effects of TGase cross-linking on allergenicity and conformational modifications in a dual-protein system comprising soy protein isolate (SPI) and β-lactoglobulin (β-LG). The results showed that TGase cross-linking effectively decreased the allergenic potential of both SPI and β-LG, with a more pronounced reduction observed in the allergenicity of soy protein in the dual-protein system. SDS-PAGE analysis revealed that the 7S and 11S subunits of soy protein were more easily cross-linked than β-LG. Secondary structure analysis indicated that TGase treatment disrupted β-sheet structures, increased the content of random coils, and enhanced protein flexibility. Ultraviolet absorption and intrinsic fluorescence analyses confirmed these structural alterations, with TGase treatment exposing additional aromatic amino acids. A reduction in free sulfhydryl groups and altered intermolecular forces further corroborated the occurrence of cross-linking. These findings suggest that TGase-mediated cross-linking effectively reduced the allergenicity of SPI and β-LG by modifying their conformations, offering potential strategies for the development of hypoallergenic dual-protein food products. Practical Application This study has practical applications in the food industry to develop hypoallergenic food products, particularly those that combine soy and dairy proteins. By using TGase to cross-link these proteins, the allergenicity can be reduced, resulting in products that are safer for consumers with food allergies.