Effects of Heat Treatment on the Antigenicity and Allergenicity of Grass Carp Muscles

References

• Arif, S. H., Jabeen, M., and Hasnain, A. 2007. Biochemical characterization and thermostable capacity of parvalbumins: The major fish-food allergens. J. Food Biochem. 31: 121–137.
   Web of Science ®Google Scholar
• Bernhisel-Broadbent, J., Strause, D., and Sampson, H. 1992. Fish hypersensitivity. II: Clinical relevance of altered fish allergenicity caused by various preparation methods. J. Allergy Clin. Immun. 90: 622–629.
   PubMed Web of Science ®Google Scholar
• Besler, M., Steinhart, H., and Paschke, A. 2001. Stability of food allergens and allergenicity of processed foods. J. Chromat. B 25: 207–228.
   Web of Science ®Google Scholar
• Bu, G., Lu, J., Zheng, Z., and Luo, Y. 2009. Influence of Maillard reaction conditions on the antigenicity of bovine α-lactalbumin using response surface methodology. J. Sci. Food. Agr. 89: 2428–2434.
   Web of Science ®Google Scholar
• Bu, G., Luo, Y., Zheng, Z., and Zheng, H. 2011. Effect of heat treatment on the antigenicity of bovine α-lactalbumin and β-lactoglobulin in whey protein isolate. Food Agr. Immunol. 20: 195–206.
   Web of Science ®Google Scholar
• Bugajska-Schretter, A., Grote, M., Vangelista, L., Valent, P., Sperr, W., Rumpold, H., Pastore, A., Reichelt, R., Valenta, R., and Spitzauer, S. 2000. Purification, biochemical, and immunological characterization of a major food allergen: Different immunoglobulin E recognition of the apo- and calcium-bound forms of carp parvalbumin. Gut 46: 661–669.
   Google Scholar
• Chatterjee, U., Mondal, G., Chakraborti, P., Patra, H. K., and Chatterjee, B. P. 2006. Changes in the allergenicity during different preparations of pomfret, hilsa, bhetki and mackerel fish as illustrated by enzyme-linked immunosorbent assay and immunoblotting. Int. Arch. Allergy Imm. 141: 1–10.
   PubMed Web of Science ®Google Scholar
• Ehn, B. M., Ekstrand, B., Bengtsson, U., and Ahlstedt, S. 2004. Modification of IgE binding during heat processing of the cow’s milk allergen β-Lactoglobulin. 2004. J. Agric. Food Chem. 52: 1398–1403.
   PubMed Web of Science ®Google Scholar
• Griesmeier, U., Bublin, M., Radauer, C., Vázquez-Cortés, S., Ma, Y., Fernández-Rivas, M., and Breiteneder, H. 2010. Physicochemical properties and thermal stability of Lep w 1, the major allergen of whiff. Mol. Nutr. Food Res. 54: 861–869.
   PubMed Web of Science ®Google Scholar
• Gronall, A., Bardawill, C. J., and David, M. M. 1949. Determination of serum proteins by means of the biuret reaction. J. Biol.Chem. 177: 751–766.
   PubMed Web of Science ®Google Scholar
• Hamada, Y., Nagashima, Y., Shiomi, K., Shimojo, N., Kohno, Y., Shibata, R., Nishima, S., Ohsuna, H., and Ikezawa, Z. 2003. Reactivity of IgE in fish-allergic patients to fish muscle collagen. Allergo. Int. 52: 139–147.
   Google Scholar
• Jenkins, J. A., Breiteneder, H., and Mills, E. N. C. 2007. Evolutionary distance from human homologs reflects allergenicity of animal food proteins. J. Allergy Clin. Immun. 120: 1399–1405.
   PubMed Web of Science ®Google Scholar
• Kim, K. B. W. R., Lee, S. Y., Song, E. J., Kim, K. E., and Ahn, D. H. 2011. Effect of heat and autoclave on allergenicity of porcine serum albumin. Food Sci. Biotechnol. 20: 455–459.
   Google Scholar
• Kobayashi, A., Tanaka, H., Hamada, Y., Ishizaki, S., Nagashima, Y., and Shiomi, K. 2006. Comparison of allergenicity and allergens between fish white and dark muscles. Allergy 61: 357–363.
   PubMed Web of Science ®Google Scholar
• Li, Z., Luo, Y., and Feng, L. 2011. Effects of Maillard reaction conditions on the antigenicity of α-lactalbumin and β-lactoglobulin in whey protein conjugated with maltose. Eur. Food Res. Technol. 233: 387–394.
   Google Scholar
• Lim, D. L. C., Neo, K. H., Yi, F. C., Chua, K. Y., Goh, D. L. M., Shek, L. P. C., Giam, Y. C., and Lee, B. W. 2008. Parvalbumin–The major tropical fish allergen. Pediatr. Allergy Immu. 19: 399–407.
   PubMed Web of Science ®Google Scholar
• Martos, G., Lopez-Exposito, I., Bencharitiwong, R., Berin, M. C., and Nowak-Wegrzyn, A. 2011. Mechanisms underlying differential food allergy response to heated egg. J. Allergy Clin. Immun. 127: 990–997.
   PubMed Web of Science ®Google Scholar
• Perez-Gordo M., Cuesta-Herranz J., Maroto A. S., Cases B., Ibáñez, M. D., and Vivanco, F. 2011. Identification of sole parvalbumin as a major allergen: Study of cross-reactivity between parvalbumins in a Spanish fish-allergic population. Clin. Exp. Allergy 41: 750–758.
   Web of Science ®Google Scholar
• Schretter-Bugajska, A. 1998. Parvalbumin, a cross-reactive fish allergen, contains IgE-binding epitopes sensitive to periodate treatment and Ca2+ depletion. J. Allergy Clin. Immun. 101: 69–74.
   Web of Science ®Google Scholar
• Sletten, G., Van Do, T., Lindvik, H., Egaas, E., and Florvaag, E. 2010. Effects of industrial processing on the immunogenicity of commonly ingested fish species. Int. Arch. Allergy Immu. 151: 223–236.
   PubMed Web of Science ®Google Scholar
• Starkl, P., Krishnamurthy, D., Szalai, K., Felix, F., Lukschal, A., Oberthuer, D., Sampson, H. A., and Jensen-Jarolim, E. 2011. Heating affects structure, enterocyte adsorption and signalling, as well as immunogenicity of the peanut allergen Ara h 2. Open Allergy J. 4: 24–34.
   PubMedGoogle Scholar
• Swoboda, I., Bugajska-Schretter, A., Valenta, R., and Spitzauer, S. 2002. Recombinant fish parvalbumins: Candidates for diagnosis and treatment of fish allergy. Allergy 57: 94–96.
   PubMed Web of Science ®Google Scholar
• Takahashi, K., Terada, C., Tashiro, M., and Asao, T. 2007. Effects of heat treatment and pepsin digestion on trypsin inhibitory activity and ovomucoid antigenicity of Japanese quail egg white. J. Food Biochem. 27: 423–434.
   Web of Science ®Google Scholar
• Thomas K., Herouet-Guicheney C., Ladics G., Bannon G., Cockburn A., Crevel R., Fitzpatrick, J., and Vieths, S. 2007. Evaluating the effect of food processing on the potential human allergenicity of novel proteins: International workshop report. Food Chem. Toxicol. 45: 1116–1122.
   Web of Science ®Google Scholar
• Tong, P., Gao, J., Chen, H., Li, X., Zhang, Y., Jian, S., Wichers, H., and Liu, F. 2012. Effect of heat treatment on the potential allergenicity and conformational structure of egg allergen ovotransferrin. Food Chem. 131: 603–610.
   Web of Science ®Google Scholar