Effect of processing on conformational changes of food proteins related to allergenicity

Effects of the Varietal Diversity and the Thermal Treatment on the Protein Profile of Peanuts and Hazelnuts

“…However, in many cases, it is not clear whether such treatments might alter the risk of eliciting an allergic reaction in sensitive consumers. ese processing methods may induce protein modification, altering its intrinsic allergenicity through protein aggregation via disulfides or other interchain covalent bonds; all structural changes at the protein level may induce a concomitant disappearance or appearance of new IgE-binding epitopes [10][11][12]. Several authors reported that the thermal treatment causes changes in the structure/conformation of proteins in different matrix [13][14][15], depending on the structural and chemical properties of the protein itself, the type of thermal processing and the operating conditions applied (temperature, pH, and time) [16][17][18][19].…”

Effects of heating, autoclaving and ultra-high pressure on the solubility, immunoreactivity and structure of major allergens in egg

“…These methods have diverse effects on allergens based on different principles, even leading to the formation of new allergenic compounds via the Maillard reaction (Rahaman, Vasiljevic, & Ramchandran, 2016;Yu, Goktepe, & Ahmedna, 2013). Among all of these strategies, thermal processing has been verified to be a promising tool that can lead to the destruction of the secondary and tertiary structures of proteins, along with disulfide bond cleavage and new disulfide bond formation, thereby masking protein epitomes and reducing the allergenicity of the allergen (Rao et al, 2016).…”

Mass spectrometry analysis and in silico prediction of allergenicity of peptides in tryptic hydrolysates of the proteins from Ruditapes philippinarum

“…These peptides can scarcely maintain stable structures in solution, decreasing the presence of potential conformational epitopes. Furthermore, the use of hydrolysates as food ingredients usually results in thermal treatment that can destroy conformational epitopes and influence the interaction with other food constituents . In addition, the presence of linear epitopes depends on the type of enzyme used and the degree of hydrolysis .…”