Study of the Thermoresistance of the Allergenic Ara h1 Protein from Peanut (Arachis hypogaea)

Abstract

The effect of heat treatment on denaturation of Ara h1 protein, a major allergen from peanut, was studied using several techniques. Previously, Ara h1 protein was isolated from raw peanut using ammonium sulfate precipitation and chromatograpic techniques. Antibodies against Ara h1 protein were obtained in rabbits, conjugated with horseradish peroxidase, and used to develop a sandwich ELISA. Denaturation of Ara h1 protein was estimated by the loss of reactivity with its specific antibodies by ELISA. Kinetic and thermodynamic parameters of the denaturation process of Ara h1 protein were determined over a temperature range of 82-90 °C. Denaturation of Ara h1 was best described assuming a reaction order of 1.5. Thermal denaturation of Ara h1 protein was also studied by differential scanning calorimetry using several heating rates. The maximum peak temperature and the enthalpy of denaturation obtained by extrapolation to a scan rate of 0 °C/min were 90.22 °C and 1574 kJ/mol, respectively. The hydrophobicity of Ara h1 protein increased with the intensity of heat treatment, and aggregates were formed when the protein was treated at 90 °C for 10 min.

Impact of the vulcanization process on the structural characteristics and IgE recognition of two allergens, Hev b 2 and Hev b 6.02, extracted from latex surgical gloves

“…Thermal stability has been recognized as a common characteristic for many allergens (Montserrat et al, 2013;Sharp et al, 2014;Usui et al, 2013). In agreement with these reports, it is remarkable that proteins detected in the studied gloves were almost exclusively known allergenic proteins.…”

Quantitative and kinetic analyses of peanut allergens as affected by food processing

“…In order to understand how the peanut major allergens are changed under thermal processing in a quantitative way, developing kinetic models is important. There are some kinetic studies performed about denaturation of purified peanut allergen (Ara h 1) subjected to heat treatment studies (Koppelman et al, 1999, Montserrat et al, 2013). However, until now, a kinetic model has not been reported to assess the changes of soluble allergen (extracted from processed peanuts) content as a function of processing time under various thermal processing methods.…”

Rapid Detection of Food Allergens by Microfluidics ELISA-Based Optical Sensor

“…Peanut and tree nut allergies were reported to affect more than 1% of the US population and appear to be increasingly reported among children [ 6 ]. The allergenicity of peanut is heat-resistant because no reduction [ 7 , 8 ] or even an increase [ 9 ] of IgE binding to Ara h 1 protein occurs due to the structural conformation changes upon the heat treatment [ 10 ]. Consumers can be exposed to the risk of peanut allergens when foods become contaminated from shared production lines, raw materials, or ingredient supply chains [ 11 ].…”