AI Article Synopsis
- Tropomyosin is identified as an allergen in finfish, with this study focusing on its purification from Atlantic cod fillets using a two-step method involving isoelectric precipitation and anion-exchange chromatography.
- The structural properties of tropomyosin were analyzed using various forms of polyacrylamide gel electrophoresis, revealing its stability and antigenicity after heat treatment.
- Three isoforms of tropomyosin were identified, and it consistently maintained its antigenicity across different structural conditions, suggesting its potential role in allergic reactions.
Article Abstract
Tropomyosin, a myofibrillar muscle protein, has been recognized as a finfish allergen. In this study, tropomyosin from Atlantic cod fillets (Gadus morhua, C) was purified using a two-step purification strategy (isoelectric precipitation and anion-exchange chromatography). C structural configuration in two sample matrices (impure and pure) were elaborated using different polyacrylamide gel electrophoresis (native, non-reducing, and reducing PAGE). Their corresponding immunoblots were conducted to investigate C antigenicity under three conditions. Overall, C retained solubility, integrity, and antigenicity after heat treatment. Three C monomeric α-type isoforms (33 kDa) were identified using two-dimensional PAGE. Under native condition, the vast majority of C existed in the disulfide-reduced dimeric form (66 kDa). Under non-reducing condition, sodium dodecyl sulfate (anionic surfactant) broke C dimers, leaving monomers and disulfide-induced tetramers. Under reducing condition, β-mercaptoethanol (thiol reducing agent) dissociated disulfide-linked C tetramers (132 kDa) into monomers (33 kDa). C retained antigenicity regardless of structural configuration under different conditions.
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| http://dx.doi.org/10.1016/j.foodchem.2022.133966 | DOI Listing |
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