Soybean is considered one of the "big eight" foods that are believed to be responsible for 90% of all allergenic reactions. Soy allergy is of particular importance, because soybeans are widely used in processed foods and, therefore, represent a particularly insidious source of hidden allergens. Although significant advances have been made in the identification and characterization of soybean allergens, scientists are not completely certain about which proteins in soy cause allergic reactions. At least 16 allergens have been identified. Most of them, as with other plant food allergens, have a metabolic, storage, or protective function. These allergens belong to protein families which have conserved structural features in relation with their biological activity, which explains the wide immunochemical cross-recognition observed among members of the legume family. Detailed analysis of the structure-allergenicity relationships has been hampered by the complexity and heterogeneity of soybean proteins. A variety of technological approaches have been attempted to decrease soybean allergenicity. This paper provides a comprehensive review of the current body of knowledge on the identification and characterization of soybean allergens, as well as an update on current hypoallergenization techniques.
: In this study, the effects of alcohol defatting using ethanol, methanol, and non‐alcoholic aqueous extraction methods on the yield, purity, and functionality of soy protein isolates were investigated. Soy protein extraction conditions were also modified (heat and mild acidic treatment before protein alkaline extraction, heat isoelectric precipitation, and non‐neutral resolubilization of proteins), and the effects on the isolate properties were evaluated. Results showed that ethanol and aqueous extraction were potential alternatives to hexane. The soy protein isolates (SPI) obtained from these samples had protein contents of more than 90% and 84%, respectively, with functional properties comparable to those of SPI prepared from hexane defatted meal. Major differences were a decrease in the emulsifying activity properties of the SPIs resulting from the alternative defatting techniques, with, however, improved emulsion stability and foaming properties for the aqueous extracted SPIs. A marked decrease in the fat‐holding capacity of the SPI made from methanol defatted meal was also noted. Modifying the protein isolation procedure also greatly influenced the functional properties of soy protein isolates. The results of the present investigation demonstrate that soy processing conditions can be modified to obtain soy proteins ingredients with specific functional properties.
A graphene-based label-free voltammetric immunosensor for the sensitive detection of the egg white allergen ovalbumin has been developed. Graphene-modified screen printed carbon electrodes have been covalently functionalized using electrochemical reduction of in situ generated aryl diazonium salt forming a carboxyphenyl film on the graphene surface. The blocking property of the carboxyphenyl film grafted on to the graphene electrodes using different cyclic voltammetry cycles has been characterized using differential pulse voltammetry in [Fe(CN)6](3-/4-) solution. Then, the terminal carboxylic groups on the graphene surface were activated using EDC/NHS and used to immobilize the ovalbumin antibody and construct the immunosensor. The fabrication steps of the immunosensor have also been characterized using differential pulse voltammetry. The decrease in the [Fe(CN)6](3-/4-) reduction peak current after the immunochemical reaction with ovalbumin has been used for the ovalbumin detection. The developed immunosensor has been used for ovalbumin detection in the concentration range of 1 pg mL(-1) to 0.5 μg mL(-1) with a detection limit of 0.83 pg mL(-1) in PBS buffer. The food matrix effect studied with ovalbumin spiked cake extract showed a good percentage of recovery, indicating the possible applicability of the developed immunosensor in real food samples.
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