Identification of oxidative modification of shrimp (Metapenaeus ensis) tropomyosin induced by malonaldehyde

Effect of malonaldehyde cross-linking on the ability of shrimp tropomyosin to elicit the release of inflammatory mediators and cytokines from activated RBL-2H3 cells

“…As a major peroxidant of lipid oxidation, MDA contains two reactive carbonyl functional groups that react with free amino groups in proteins, especially the ϵ ‐amino of Lys, and with the nucleophilic side chains in Cys and His . Indeed, we demonstrated in previous studies that cross‐linking tropomyosin with 100 mmol L −1 malonaldehyde reduced free amines and available Lys to 46% and 77%, respectively, by modifying Lys, Gln, and Asn residues . These reactions may damage the structure of shrimp tropomyosin and alter its allergenicity.…”

Effect of 4-hydroxy-2-nonenal treatment on the IgE binding capacity and structure of shrimp (Metapenaeus ensis) tropomyosin

“…Overall, the tropomyosin bands from the different HNE treatments were nearly identical, and there were no other bands associated with the treatment. In our previous study, MDA cross-linked with tropomyosin, resulted in the formation of several new bands with molecular masses greater than the native tropomyosin protein (Lv et al, 2014). The possible reason for the differences observed is that MDA possesses two aldehyde groups which can bind with two or more proteins, whereas HNE possesses only one aldehyde group which can bind with one protein.…”

“…LC-MS/MS was performed using the method described by Lv (2014). Analysis of the peptide samples was performed using an LTQ-Orbitrap mass spectrometer (Thermo Fisher Scientific) equipped with a nano-electrospray ionization source.…”

“…However, allergens formed by oxidation reactions during food processing and preservation have been neglected over the past decades. In 2014, our research team reported that malondialdehyde (MDA) could reduce the allergenicity of shrimp tropomyosin through structural modification, but information about the detailed mechanisms involved remains limited (Lv et al, 2014;Song et al, 2015). With the increasing knowledge that food allergens are both sources and targets for reactive oxygen species and other peroxides, allergen oxidation modification is currently one of the most important research topics within the field of food allergens (Li, Lu, Khan, Lin, & Zhang, 2014).…”

Effect of pH shifts on IgE-binding capacity and conformational structure of tropomyosin from short-neck clam (Ruditapes philippinarum)

“…The effect of food processing on the allergenicity of tropomyosin has been studied. These studies focused primarily on thermal processes or non-thermal processes such as high hydro pressure and irradiation (Li, Lin, Cao, & Khalid, 2006;Lv et al, 2014). It has been reported that the conformational stability of tropomyosin, to some extent, depends on hydrogen bonds and Van der Waals forces.…”