Evaluation of electron beam irradiation to reduce the IgE binding capacity of frozen shrimp tropomyosin

Abstract

2017) Evaluation of electron beam irradiation to reduce the IgE binding capacity of frozen shrimp tropomyosin, Food and Agricultural Immunology, 28:2, 189-201, ABSTRACTThe aim was to determine the effect of electron beam (EB) irradiation on IgE binding capacity of shrimp tropomyosin (TM) at the frozen stage. Following EB irradiation, protein extracts were characterized by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and TM degradation was observed. The degradations were further recognized by IgE from a shrimp-allergic patient by immunoblots. Specific IgE binding results showed that capacity of shrimp extracts and TM initially increased by 10% after irradiation at 3 kGy doses, and then decreased by 20% with irradiation doses increased to 10 kGy. Further inhibition enzyme linked immunosorbent assay results showed that half-maximal inhibitory concentration of shrimp extract treated with 10 kGy doses enhanced to four times as compared with raw shrimp extracts. These results suggest that EB irradiation significantly changes the IgE binding capacity of frozen shrimp at 10 kGy doses by 20% and has the potential to reduce shrimp allergy risk. ARTICLE HISTORY

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

“…Because of the threat that allergens pose to human health, many scientists have been working on strategies to reduce allergenicity, including physical methods, such as heat processing (Lasekan & Nayak, 2016), irritation (Lemon-Mulé et al, 2008;Liu et al, 2017), and ultra-high pressure (Liang, Xu, Pan, Ge, & Zong, 2015); chemical methods, such as the Maillard reaction (Li, Jiang, You, Luo, & Feng, 2014;Li, Offengenden, Fentabil, Gänzle, & Wu, 2013), and enzymatic hydrolysis (Mine, 1995), and biological methods, such as traditional fermentation (Moon & Song, 2001), or gene silencing (KovacsNolan, Phillips, & Mine, 2005;Nicolai & Durand, 2013). 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).…”

An overview of tropomyosin as an important seafood allergen: Structure, cross‐reactivity, epitopes, allergenicity, and processing modifications

“…EB irradiation is another irradiation way, but it is less penetrable than γ‐irradiation at the same dose. It is worth noting that the general use of EB‐irradiation treatment for seafood cannot exceed 10 kGy, below which the irradiation should have no negative impact on food (Y. Liu et al., 2017b).…”

“…Y. Liu et al. (2017b) studied the effects of EB‐irradiation on frozen shrimp ( M. ensis ) and found that the trend of changes of IgE‐binding ability was increased at 0–3 kGy and then decreased at 3–10 kGy. It could be explained by that the energy of the EB‐irradiation was not able to penetrate the frozen shrimp.…”

“…Likewise, Guangyu Liu et al. (2017) studied the influence of polymer compounds forming from cross‐linking caused by tyrosine or horseradish peroxidase on the sensitization of TM. The results showed that the cross‐linking of tyrosinase and horseradish peroxidase reduced the IgE‐binding ability of TM by 34.5% and 63.5%, respectively, and the IgG‐binding ability of TM by 16.9% and 70.8%, respectively.…”

Whey allergens: Influence of nonthermal processing treatments and their detection methods

“…Food processing can lead to a number of protein structural modifications, such as aggregation, denaturation, oxidation, glycation, and crosslinking. Such modifications can influence the IgE/IgG-binding ability F I G U R E 2 Nonthermal processing-induced conformational changes and impacts on the allergenicity of milk proteins and thus significantly influence the allergenicity of proteins (Ahmed et al, 2018;Liu et al, 2017). Thermal processing may contribute to the formation of neoepitopes, which can potentially increase the allergenicity of proteins.…”