Allergenic characterization and biochemical stability of allergens in purple mud crab Scylla tranquabarica
<p></p><p>This study aims to characterize the allergenic properties and determine the</p><p>biochemical stability of allergens of purple mud crab, Scylla tranquebarica. Raw extracts were</p><p>prepared...
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Alsailawi, Hasan Ali Jasim Allergenic characterization and biochemical stability of allergens in purple mud crab Scylla tranquabarica |
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<p></p><p>This study aims to characterize the allergenic properties and determine the</p><p>biochemical stability of allergens of purple mud crab, Scylla tranquebarica. Raw extracts were</p><p>prepared from the muscle tissues of both mixed and specific body parts. Various treated extracts</p><p>were prepared from the muscles of mixed body parts. Protein profiles, allergenic proteins and</p><p>cross-reactive allergens were then identified by sodium dodecyl sulfate-polyacrylamide gel</p><p>electrophoresis (SDS-PAGE), immunoblotting and immunoblotting inhibition test techniques,</p><p>respectively, using sera from crab-allergic patients. The identification of major allergens were</p><p>analyzed by mass spectrometry. This study showed that raw mixed part extract contains the most</p><p>protein bands and allergenic proteins than the specific body parts and all treated extracts. Five</p><p>major allergens were identified at 38, 42, 50, 63 and 73 kDa. Mass spectrometry analysis identified</p><p>the 42 and 50 kDa as arginine kinase, while the 38, 63 and 73 kDa were identified as tropomyosin,</p><p>actin and hemocyanin, respectively. The allergen extracts stored at -80 C for all storage periods</p><p>of 3, 6, 9 and 12 months were indicated to have the same quality as the fresh raw mixed parts</p><p>extract. Immunoblotting inhibition tests showed the present of cross-reactivity among major and</p><p>minor allergens of crab, with either complete or partial inhibitions. Among the specific crab</p><p>parts, the female legs was found as the most allergenic parts, while the male abdomen was indicated</p><p>as the least allergenic. The high pressure steamed and white vinegar treated crabs were found to</p><p>have the lowest degree of stability and allergenicity among the thermal and non-thermal treated</p><p>crabs, respectively. As a conclusion, the allergenicity of S. tranquebarica varies depending on the</p><p>crab parts, processing treatments and storage conditions applied. Tropomyosin, arginine kinase,</p><p>actin and hemocyanin are identified as the major and cross-reactive allergens in this crab</p><p>species. Tropomyosin is indicated as the most stable allergen of S. tranquebarica. The</p><p>implication of this study is to provide insights into local mud crab allergens to improve strategy</p><p>of diagnosis, management, therapeutic and food</p><p>manufacturing for crab allergic patients in this country.</p><p></p> |
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Alsailawi, Hasan Ali Jasim |
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Alsailawi, Hasan Ali Jasim |
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Alsailawi, Hasan Ali Jasim |
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Allergenic characterization and biochemical stability of allergens in purple mud crab Scylla tranquabarica |
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Allergenic characterization and biochemical stability of allergens in purple mud crab Scylla tranquabarica |
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Allergenic characterization and biochemical stability of allergens in purple mud crab Scylla tranquabarica |
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Allergenic characterization and biochemical stability of allergens in purple mud crab Scylla tranquabarica |
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Allergenic characterization and biochemical stability of allergens in purple mud crab Scylla tranquabarica |
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allergenic characterization and biochemical stability of allergens in purple mud crab scylla tranquabarica |
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oai:ir.upsi.edu.my:86002023-01-16 Allergenic characterization and biochemical stability of allergens in purple mud crab Scylla tranquabarica 2020 Alsailawi, Hasan Ali Jasim <p></p><p>This study aims to characterize the allergenic properties and determine the</p><p>biochemical stability of allergens of purple mud crab, Scylla tranquebarica. Raw extracts were</p><p>prepared from the muscle tissues of both mixed and specific body parts. Various treated extracts</p><p>were prepared from the muscles of mixed body parts. Protein profiles, allergenic proteins and</p><p>cross-reactive allergens were then identified by sodium dodecyl sulfate-polyacrylamide gel</p><p>electrophoresis (SDS-PAGE), immunoblotting and immunoblotting inhibition test techniques,</p><p>respectively, using sera from crab-allergic patients. The identification of major allergens were</p><p>analyzed by mass spectrometry. This study showed that raw mixed part extract contains the most</p><p>protein bands and allergenic proteins than the specific body parts and all treated extracts. Five</p><p>major allergens were identified at 38, 42, 50, 63 and 73 kDa. Mass spectrometry analysis identified</p><p>the 42 and 50 kDa as arginine kinase, while the 38, 63 and 73 kDa were identified as tropomyosin,</p><p>actin and hemocyanin, respectively. The allergen extracts stored at -80 C for all storage periods</p><p>of 3, 6, 9 and 12 months were indicated to have the same quality as the fresh raw mixed parts</p><p>extract. Immunoblotting inhibition tests showed the present of cross-reactivity among major and</p><p>minor allergens of crab, with either complete or partial inhibitions. Among the specific crab</p><p>parts, the female legs was found as the most allergenic parts, while the male abdomen was indicated</p><p>as the least allergenic. The high pressure steamed and white vinegar treated crabs were found to</p><p>have the lowest degree of stability and allergenicity among the thermal and non-thermal treated</p><p>crabs, respectively. As a conclusion, the allergenicity of S. tranquebarica varies depending on the</p><p>crab parts, processing treatments and storage conditions applied. Tropomyosin, arginine kinase,</p><p>actin and hemocyanin are identified as the major and cross-reactive allergens in this crab</p><p>species. Tropomyosin is indicated as the most stable allergen of S. tranquebarica. The</p><p>implication of this study is to provide insights into local mud crab allergens to improve strategy</p><p>of diagnosis, management, therapeutic and food</p><p>manufacturing for crab allergic patients in this country.</p><p></p> 2020 thesis https://ir.upsi.edu.my/detailsg.php?det=8600 https://ir.upsi.edu.my/detailsg.php?det=8600 text eng closedAccess Doctoral Universiti Pendidikan Sultan Idris Fakulti Sains dan Matematik <p>Abbas, A. K., Lichtman, A. H. & Pillai, S. (2012). Cellular and molecular</p><p>immunology. Elsevier Saunders. pp. 426.</p><p></p><p>Abdel Rahman, A., Kamath, S., Lopata, A. & Helleur, R. (2010). Analysis of the allergenic proteins</p><p>in black tiger prawn (Penaeus monodon) and characterization of the major allergen</p><p>tropomyosin using mass spectrometry. Rapid Communications in Mass Spectrometry, 24(16), 24622470.</p><p></p><p>Abdel Rahman, A., Kamath, S., Lopata, A., Robinson, J. & Helleur, R. (2011). 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