Effect of heat treatment on the potential allergenicity and conformational structure of egg allergen ovotransferrin

Detection of Allergens in a Multiple Allergen Matrix and Study of the Impact of Thermal Processing

“…Furthermore, the protein extraction data showed that the soluble protein recovery as a percentage of the total protein content decreased with increasing processing temperature for the three buffers which can further limit the accuracy of determination of allergen quantities. These results are in agreement with previous findings [5,6,[22][23][24].…”

“…140OA from Morinaga Institute of Biological Science was able to detect egg allergens in the processed food matrix because of the extraction buffer used (i.e., SDS and 2-ME extraction buffer) and the protocol employed. Other studies have also reported that heat treatment decreased the antigenicity of the egg allergens ovomucoid [27] and ovotransferrin [6].…”

“…Diaz-Amigo [31] reported a decrease in detection of egg allergens in baked cookie extracts using ELISA kits due to the reduced quantity of protein extracted with the buffers employed. Other workers have shown changes in secondary structure and sulfhydryl-disulfide interchange reactions on thermal treatment of egg proteins which affected protein antigenicity [6]. A decrease of soy allergen recovery has also been explained by the interactions occurring between soy and flour gluten proteins as a consequence of dough mixing and the formation of high molecular weight complex between soy 11S globulin and prolamin of wheat dough [32].…”

“…One of the major concerns for legislators and food manufacturers is that processing may alter allergen detection in processed foods. In fact, the effect of thermal processing on allergen quantization is of growing interest especially in regards to the detection of allergenic food residues at low levels [5][6][7]. Food processing treatments such as thermal treatment, pressurization and sterilization cause denaturation of proteins.…”

Effect of cosolvents (polyols) on structural and foaming properties of soy protein isolate

“…Second-derivative UV spectra of soy protein isolates in the absence and presence of 15% (w/w) polyols Food Sci., 35, 2017(1): 57-66 doi: 10.17221/35/2016 194 nm indicated the existence of β-sheet structure and the negative peak at 209 nm was characteristic of α-helical structure (Choi & Ma 2007;. As polyols were added, the positive and negative molar residue ellipticity peaks of SPI samples increased, which showed that the amounts of α-helix and β-sheet had risen (Tong et al 2012). This result was proved by the changes of secondary structure contents of SPI with and without the addition of polyols calculated by JASCO secondary structure software (Figure 6).…”