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THERMAL STABILITY OF FOOD ALLERGENS AND NONALLERGENIC PROTEINS: A COMPARATIVE STUDY
Title
THERMAL STABILITY OF FOOD ALLERGENS AND NONALLERGENIC PROTEINS: A COMPARATIVE STUDY
Creator
Wu, Yan
Date
2015, 2015-07
Description
Thermal stability has been proposed as a criterion to assess the allergenic potential of genetically modified foods, but there is a lack of...
Show moreThermal stability has been proposed as a criterion to assess the allergenic potential of genetically modified foods, but there is a lack of information on the relative thermal stability of food allergens vs. nonallergenic proteins. This study compared the thermal stability of several paired food allergens and nonallergenic proteins by measuring the changes in their solubility, antigenicity and thermodynamic properties after thermal treatment using BCA total protein assay, inhibition ELISA assay, Differential Scanning Calorimetry and Far-UV Circular Dichroism Spectroscopy. The selected protein pairs included bovine α-lactalbumin (allergen) vs. human α-lactalbumin (nonallergen), peanut lectin (allergen) vs. concanavalin A (nonallergen), soybean trypsin inhibitor (allergen) vs. lima bean trypsin inhibitor (nonallergen). With respect to protein solubility, a greater thermal stability was observed for: (1) bovine α-lactalbumin (bovine ALA) when it was autoclaved in water compared with human α-lactalbumin (human ALA) (2) peanut lectin when it was boiled or autoclaved in water compared with concanavalin A (ConA) and (3) soybean trypsin inhibitor (STI) when it was boiled in water or PBS, or autoclaved in water compared with lima bean trypsin inhibitor (LTI). Regarding TM values determined by DSC: (1) bovine ALA was more thermally stable than human ALA under both dry-heat treatment and moist-heat treatment (2) ConA was more thermally stable than peanut lectin during moist-heat treatment, while a greater thermal stability was observed for peanut lectin when the protein was under dry-heat treatment (3) LTI was more thermally stable than STI during heating in water or under dry-heat treatment, while a greater thermal stability was observed for STI when the protein was heated in PBS. Based on CD analyses, (1) bovine ALA was more thermally stable than human ALA (2) peanut lectin was more thermally stable than ConA (3) STI and LTI showed similar thermal stability. With respect to antigenicity, a greater thermal stability was observed for: (1) human ALA when it was autoclaved in water compared with bovine ALA (2) ConA when it was boiled or autoclaved in water, or under dry-heat treatment at 176℃ compared with peanut lectin (3) STI when it was autoclaved in PBS compared with LTI. In summary, allergens tended to be more thermally stable than nonallergenic proteins with respect to solubility, but there was no consistent trend in the relative thermal stability of these protein pairs regarding the antigenicity or the TM values. No correlation between thermal stability of the proteins and their allergenic potential was observed.ConA (3) STI and LTI showed similar thermal stability. With respect to antigenicity, a greater thermal stability was observed for: (1) human ALA when it was autoclaved in water compared with bovine ALA (2) ConA when it was boiled or autoclaved in water, or under dry-heat treatment at 176℃ compared with peanut lectin (3) STI when it was autoclaved in PBS compared with LTI. In summary, allergens tended to be more thermally stable than nonallergenic proteins with respect to solubility, but there was no consistent trend in the relative thermal stability of these protein pairs regarding the antigenicity or the TM values. No correlation between thermal stability of the proteins and their allergenic potential was observed.
M.S. in Food Safety and Technology, July 2015
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