Review of conventional and novel food processing methods on food allergens

References

• Adler-Nissen, J. (1986). Enzymic hydrolysis of food proteins. Elsevier Applied Science Publishers; Sole distributor in the USA and Canada. Elsevier Science Pub. Co., London, New York; New York, NY, USA.
   Google Scholar
• Alun Jones, V., Shorthouse, M., McLaughlan, P., Workman, E. and Hunter, J. (1982). Food intolerance: A major factor in the pathogenesis of irritable bowel syndrome. Lancet. 320:1115–1117.
   Google Scholar
• Álvarez-Álvarez, J., Guillamón, E., Crespo, J. F., Cuadrado, C., Burbano, C., Rodríguez, J., Fernández, C. and Muzquiz, M. (2005). Effects of extrusion, boiling, autoclaving, and microwave heating on lupine allergenicity. J. Agric. Food Chem. 53:1294–1298.
   PubMed Web of Science ®Google Scholar
• Andreas, L. (2009). Allergenicity of Food and Impact of Processing. In: Novel Food Processing, pp. 459–478. Boca Raton, Florida, USA: CRC Press.
   Google Scholar
• Anekella, K. and Orsat, V. (2013). Optimization of microencapsulation of probiotics in raspberry juice by spray drying. LWT - Food Sci. Technol. 50:17–24.
   Web of Science ®Google Scholar
• Atanasiu, P., Barbu, E. and Basset, J. (1951). Effect of very high pressure on Newcastle virus. I. Dissociation of infectious power and of hemagglutination. Action des pressions très élevées sur le virus de Newcastle. I. Dissociation du pouvoir infectieux et de l'hémagglutination. 81:340–343.
   Google Scholar
• Ayerst, G. (1969). The effects of moisture and temperature on growth and spore germination in some fungi. J. Store. Prod. Res. 5:127–141.
   Web of Science ®Google Scholar
• Ayuso, R., Lehrer, S. B. and Reese, G. (2002). Identification of continuous, allergenic regions of the major shrimp allergen pen a 1 (Tropomyosin). Int. Arch. Allergy. Immunol. 127:27–37.
   PubMed Web of Science ®Google Scholar
• Baer, A., Oroz, M. and Blanc, B. (1976). Serological studies on heat-induced interactions of α-lactalbumin and milk proteins. J. Dairy Res. 43:419–432.
   Web of Science ®Google Scholar
• Bamforth, C. W. (2005). Food, Fermentation, and Micro-Organisms. Blackwell Science, Oxford, Ames, Iowa.
   Google Scholar
• Bang, H., Dyerberg, J. and Sinclair, H. M. (1980). The composition of the Eskimo food in north western Greenland. Amer. J. Clin. Nutr. 33:2657–2661.
   PubMed Web of Science ®Google Scholar
• Basset, J., Lépine, P. and Chaumont, L. (1956). Effects of high pressures on the poliomyelitis virus (Lansing strain). Ann. Inst. Pasteur. 90:575–596.
   PubMedGoogle Scholar
• Basset, J. and Macheboeuf, M. (1933). Etudes sur les effets biologiques des ultra-pressions. Etudes de l'immunité: Influence des pressions très élevées sur certains antigènes et anticorps. C. R. Acad. Sci. 196:67–69.
   Google Scholar
• Basset, J. and Macheboeuf, M. A. (1932). Etude sur les effets biologiques des ultrapressions: Résistance des bactéries, des diastases et des toxines aux pressions très élevées. C. R. Acad. Sci. 195:1431–1433.
   Google Scholar
• Basset, J., Nicolaus, S. and Macheboeuf, M. A. (1935a). L'action de l'ultrapression sur l'activité pathogène de quelques virus. C.R. Acad. Sci. 200:1882–1884.
   Google Scholar
• Basset, J., Wollman, E., Macheboeuf, M. A. and Bardach, M. (1935b). Etudes sur les effets biologiques des ultra-pressions: Action des pressions élevées sur les tumeurs. C. R. Hebd Acad. Sci. 200:200.
   Google Scholar
• Basset, J., W∫llman, E., Macheboeuf, M. A. and Bardach, M. (1933). Études sur les effets biologiques des ultrapressions: Action des pressions très élevées sur des bactériophages et sur un virus invisible (virus vaccinal). C. R. Acad. Sci. 196:1138–1139.
   Google Scholar
• Bernhisel-Broadbent, J., Scanlon, S. M. and Sampson, H. A. (1992a). Fish hypersensitivity. I. In vitro and oral challenge results in fish- allergic patients. J. Allergy Clin. Immunol. 89:730–737.
   PubMed Web of Science ®Google Scholar
• Bernhisel-Broadbent, J., Strause, D. and Sampson, H. A. (1992b). Fish hypersensitivity. II: Clinical relevance of altered fish allergenicity caused by various preparation methods. J. Allergy Clin. Immunol. 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. Chromatogr. B. 756:207–228.
   PubMed Web of Science ®Google Scholar
• Beyer, K., Morrow, E., Li, X. M., Bardina, L., Bannon, G. A., Burks, A. W. and Sampson, H. A. (2001). Effects of cooking methods on peanut allergenicity. J. Allergy Clin. Immunol. 107:1077–1081.
   PubMed Web of Science ®Google Scholar
• Bonomi, F., Fiocchi, A., Frøkiær, H., Gaiaschi, A., Iametti, S., Poiesi, C., Rasmussen, P., Restani, P. and Rovere, P. (2003). Reduction of immunoreactivity of bovine β-lactoglobulin upon combined physical and proteolytic treatment. J. Dairy Res. 70:51–59.
   PubMed Web of Science ®Google Scholar
• Boye, J., Ma, C. and Harwalkar, V. (1997). Thermal denaturation and coagulation of proteins. Food Sci. Technol. New York Marcel Dekker: 25–56.
   Google Scholar
• Boyle, M. A. Z. G. (1996). Personal Nutrition, 3rd ed. West Pub. Co., Minneapolis.
   Google Scholar
• Brenna, O., Pompei, C., Ortolani, C., Pravettoni, V., Farioli, L. and Pastorello, E. A. (2000). Technological processes to decrease the allergenicity of peach juice and nectar. J. Agric. Food Chem. 48:493–497.
   PubMed Web of Science ®Google Scholar
• Bu, G., Luo, Y., Zhang, Y. and Chen, F. (2010). Effects of fermentation by lactic acid bacteria on the antigenicity of bovine whey proteins. J. Sci. Food Agric. 90:2015–2020.
   PubMed Web of Science ®Google Scholar
• Byun, M.-W., Kim, J.-H., Lee, J.-W., Park, J.-W., Hong, C.-S. and Kang, I.-J. (2000). Effects of gamma radiation on the conformational and antigenic properties of a heat-stable major allergen in brown shrimp. J. Food Protect. 63:940–944.
   PubMed Web of Science ®Google Scholar
• Byun, M.-W., Lee, J.-W., Yook, H.-S., Jo, C. and Kim, H.-Y. (2002). Application of gamma irradiation for inhibition of food allergy. Radiat. Phys. Chem. 63:369–370.
   Web of Science ®Google Scholar
• Carpita, N. C. and Gibeaut, D. M. (1993). Structural models of primary cell walls in flowering plants: Consistency of molecular structure with the physical properties of the walls during growth. Plant J. 3:1–30.
   PubMed Web of Science ®Google Scholar
• Chicón, R., Belloque, J., Alonso, E. and López-Fandiño, R. (2008a). Immunoreactivity and digestibility of high-pressure-treated whey proteins. Int. Dairy J. 18:367–376.
   Web of Science ®Google Scholar
• Chicón, R., Belloque, J., Alonso, E., Martín-Álvarez, P. J. and López-Fandiño, R. (2008b). Hydrolysis under high hydrostatic pressure as a means to reduce the binding of β-lactoglobulin to immunoglobulin E from human sera. J. Food Protect. 71:1453–1459.
   PubMed Web of Science ®Google Scholar
• Chobert, J. M., Bertrand-Harb, C. and Nicolas, M. G. (1988). Solubility and emulsifying properties of caseins and whey proteins modified enzymically by trypsin. J. Agric. Food Chem. 36:883–892.
   Web of Science ®Google Scholar
• Chung, S. Y., Yang, W. and Krishnamurthy, K. (2008). Effects of pulsed UV-light on peanut allergens in extracts and liquid peanut butter. J. Food Sci. 73:C400–C404.
   PubMed Web of Science ®Google Scholar
• Cleaves, H. J. (2011). Quaternary Structure (Protein). Encyclopedia of Astrobiology, 1st ed.: 1396–1397.
   Google Scholar
• Cocco, R. R., Järvinen, K. M., Sampson, H. A. and Beyer, K. (2003). Mutational analysis of major, sequential IgE-binding epitopes in αs1-casein, a major cow's milk allergen. J. Allergy Clin. Immunol. 112:433–437.
   PubMed Web of Science ®Google Scholar
• Cuadrado, C., Cabanillas, B., Pedrosa, M. M., Varela, A., Guillamón, E., Muzquiz, M., Crespo, J. F., Rodriguez, J. and Burbano, C. (2009). Influence of thermal processing on IgE reactivity to lentil and chickpea proteins. Mol. Nutr. Food Res. 53:1462–1468.
   PubMed Web of Science ®Google Scholar
• Daul, C. B., Morgan, J. E., Hughes, J. and Lehrer, S. B. (1988). Provocation-challenge studies in shrimp-sensitive individuals. J. Allergy Clin. Immunol. 81:1180–1186.
   PubMed Web of Science ®Google Scholar
• Daul, C. B., Slattery, M., Reese, G. and Lehrer, S. B. (1994). Identification of the major brown shrimp (Penaeus aztecus) allergen as the muscle protein tropomyosin. Int. Arch. Allerg. Immunol. 105:49–55.
   PubMed Web of Science ®Google Scholar
• Davis, P. and Williams, S. (1998). Protein modification by thermal processing. Allergy. 53:102–105.
   PubMed Web of Science ®Google Scholar
• Davis, P. J., Smales, C. M. and James, D. C. (2001). How can thermal processing modify the antigenicity of proteins? Allergy: Eur. J. Allergy Clin. Immunol., Suppl. 56:56–60.
   Web of Science ®Google Scholar
• de Pomerai, D. I., Smith, B., Dawe, A., North, K., Smith, T., Archer, D. B., Duce, I. R., Jones, D. and Candido, E. P. M. (2003). Microwave radiation can alter protein conformation without bulk heating. FEBS Lett. 543:93–97.
   PubMed Web of Science ®Google Scholar
• Decareau, R. V. and Peterson, R. A. (1986). Microwave processing and engineering. Chichester: Ellis Horwood, 224 pgs.
   Google Scholar
• Diniz, F. and Martin, A. (1997). Effects of the extent of enzymatic hydrolysis on functional properties of shark protein hydrolysate. LWT-Food Sci. Technol. 30:266–272.
   Web of Science ®Google Scholar
• Doona, C. J. K. K. F. F. E. (2010). Case Studies in Novel Food Processing Technologies Innovations in Processing, Packaging and Predictive Modelling. Woodhead Publishing, Oxford.
   Google Scholar
• Ehn, B. M., Allmere, T., Telemo, E., Bengtsson, U. and Ekstrand, B. O. (2005). Modification of IgE binding to β-lactoglobulin by fermentation and Proteolysis of cow's milk. J. Agric. Food Chem. 53:3743–3748.
   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. J. Agric. Food Chem. 52:1398–1403.
   PubMed Web of Science ®Google Scholar
• Eichner, K. and Karel, M. (1972). Influence of water content and water activity on the sugar-amino browning reaction in model systems under various conditions. J. Agric. Food Chem. 20:218–223.
   Web of Science ®Google Scholar
• El-Ghaish, S., Ahmadova, A., Hadji-Sfaxi, I., El Mecherfi, K. E., Bazukyan, I., Choiset, Y., Rabesona, H., Sitohy, M., Popov, Y. G., Kuliev, A. A., Mozzi, F., Chobert, J.-M. and Haertlé, T. (2011a). Potential use of lactic acid bacteria for reduction of allergenicity and for longer conservation of fermented foods. Trends Food Sci. Technol. 22:509–516.
   Web of Science ®Google Scholar
• El-Ghaish, S., Dalgalarrondo, M., Choiset, Y., Sitohy, M., Ivanova, I., Haertlé, T. and Chobert, J. M. (2010a). Characterization of a new isolate of Lactobacillus fermentum IFO 3956 from Egyptian Ras cheese with proteolytic activity. Eur. Food Res. Technol. 230:635–643.
   Web of Science ®Google Scholar
• El-Ghaish, S., Dalgalarrondo, M., Choiset, Y., Sitohy, M., Ivanova, I., Haertlé, T. and Chobert, J. M. (2010b). Screening of strains of lactococci isolated from Egyptian dairy products for their proteolytic activity. Food Chem. 120:758–764.
   Web of Science ®Google Scholar
• El-Ghaish, S., Rabesona, H., Choiset, Y., Sitohy, M., Haertlé, T. and Chobert, J. M. (2011b). Proteolysis by Lactobacillus fermentum IFO3956 isolated from Egyptian milk products decreases immuno-reactivity of α s1-casein. J. Dairy Res. 78:203–210.
   PubMed Web of Science ®Google Scholar
• El-Mansi, M. (2012). Fermentation Microbiology and Biotechnology. CRC Press, Boca Raton, FL.
   Google Scholar
• Eliasson, A.-C. (2006). Carbohydrates in food. CRC/Taylor & Francis, Boca Raton, FL.
   Google Scholar
• Elmer, G. W., Surawicz, C. M. and McFarland, L. V. (1996). Biotherapeutic agents: A neglected modality for the treatment and prevention of selected intestinal and vaginal infections. J. Amer. Med. Assoc. 275:870–876.
   PubMed Web of Science ®Google Scholar
• Farkas, J. (1998). Irradiation as a method for decontaminating food: A review. Int. J. Food Microbiol. 44:189–204.
   PubMed Web of Science ®Google Scholar
• Farkas, J. (2006). Irradiation for better foods. Trends Food Sci. Technol. 17:148–152.
   Web of Science ®Google Scholar
• Fellows, P. (2000). Food Processing Technology Principles and Practice. CRC Press; Woodhead Pub., Boca Raton, Fla.; Cambridge, England.
   Google Scholar
• Fellows, P. J. (2009). Food Processing Technology: Principles and Practice. Elsevier, 3rd ed., Boca Raton, Florida: CRC Press.
   Google Scholar
• Feng, H., Barbosa-Canovas, G. and Weiss, J. (2011). Ultrasound technologies for food and bioprocessing food engineering series. New York: Springer.
   Google Scholar
• Fiocchi, A., Restani, P., Bernardo, L., Martelli, A., Ballabio, C., D'Auria, E. and Riva, E. (2004). Tolerance of heat-treated kiwi by children with kiwifruit allergy. Pediatr. Allergy Immunol. 15:454–458.
   PubMed Web of Science ®Google Scholar
• Fruton, J. S. (1972). Molecules and life. History of Science, 13:114–121.
   Google Scholar
• Gall, H., Kalveram, K.-J., Forck, G. and Sterry, W. (1994). Kiwi fruit allergy: A new birch pollen–associated food allergy. J. Allergy Clin. Immunol. 94:70–76.
   PubMed Web of Science ®Google Scholar
• Gruber, P., Vieths, S., Wangorsch, A., Nerkamp, J. and Hofmann, T. (2004). Maillard reaction and enzymatic browning affect the allergenicity of Pru av 1, the major allergen from cherry (Prunus avium). J. Agric. Food Chem. 52:4002–4007.
   PubMed Web of Science ®Google Scholar
• Gu, J. and Bourne, P. E. (2009). Structural Bioinformatics. Vol. 44. Hoboken, New Jersey: John Wiley & Sons.
   Google Scholar
• Hansen, K. S., Ballmer-Weber, B. K., Lüttkopf, D., Skov, P. S., Wüthrich, B., Bindslev-Jensen, C., Vieths, S. and Poulsen, L. K. (2003). Roasted hazelnuts—Allergenic activity evaluated by double-blind, placebo-controlled food challenge. Allergy: Eur. J. Allergy Clin. Immunol. 58:132–138.
   Web of Science ®Google Scholar
• Hansen, T. K., Stahl Skov, P., Poulsen, L. K. and Bindslev-Jensen, C. (1994). Allergenic activity of processed fish. Allergy Clin. Immunol. News. 2:39–42.
   Google Scholar
• Herian, A. M., Taylor, S. L. and Bush, R. K. (1993). Allergenic reactivity of various soybean products as determined by RAST inhibition. J. Food Sci. 58:385–388.
   Web of Science ®Google Scholar
• Herman, E. M., Helm, R. M., Jung, R. and Kinney, A. J. (2003). Genetic modification removes an immunodominant allergen from soybean. Plant Physiol. 132:36–43.
   PubMed Web of Science ®Google Scholar
• Herrmann, W. O. R. (2011). Vitamins in the Prevention of Human Diseases. De Gruyter, Berlin, New York.
   Google Scholar
• Hettiarachchy, N. S. S. K. M. M. R. K. A. (2012). Food Proteins and Peptides Chemistry, Functionality, Interactions, and Commercialization. Taylor & Francis, Boca Raton, FL.
   Google Scholar
• Hite, B. H. (1899). The effect of pressure in the preservation of milk. Bull. West Virginia Univ. Agric. Exp. Stn. 58:15–35.
   Google Scholar
• Hite, B. H., Giddings, N. J. and Weakly, C. E. (1914). The effect of pressure on certain microorganisms encountered in the preservation of fruits and vegetables. Bull. West Virginia Univ. Agric. Exp. Stn. 146:1–67.
   Google Scholar
• Hoffman, D. R. (1983). Immunochemical identification of the allergens in egg white. J. Allergy Clin. Immunol. 71:481–486.
   PubMed Web of Science ®Google Scholar
• Houska, M., Heroldova, M., Vavrova, H., Kucera, P., Setinova, I., Havranova, M., Honzova, S., Strohalm, J., Kminkova, M., Proskova, A. and Novotna, P. (2009). Is high-pressure treatment able to modify the allergenicity of the main apple juice allergen, Mal d1? High Press. Res. 29:14–22.
   Web of Science ®Google Scholar
• Hsu, J., Heatherbell, D., Flores, J. and Watson, B. (1987). Heat-unstable proteins in grape juice and wine. II. Characterization and removal by ultrafiltration. Amer. J. Enol. Viticult. 38:17–22.
   Web of Science ®Google Scholar
• Hunt, J. and Stubbs, D. (1975). The volume and energy content of meals as determinants of gastric emptying. J. Physiol. 245:209–225.
   PubMed Web of Science ®Google Scholar
• Jankiewicz, A., Aulepp, H., Baltes, W., Bögl, K. W., Dehne, L. I., Zuberbier, T. and Vieths, S. (1996). Allergic sensitization to native and heated celery root in pollen-sensitive patients investigated by skin test and IgE binding. Int. Arch. Allerg. Immunol. 111:268–278.
   PubMed Web of Science ®Google Scholar
• Jankiewicz, A., Baltes, W., Bögl, K. W., Dehne, L. I., Jamin, A., Hoffmann, A., Haustein, D. and Vieths, S. (1997). Influence of food processing on the immunochemical stability of celery allergens. J. Sci. Food Agric. 75:359–370.
   Web of Science ®Google Scholar
• Jasim, A., Hosahalli, S. R., Stefan, K. and Joyce, I. B. (2009). From odors to behaviors in caenorhabditis elegans. In: Novel Food Processing, pp. 1–6. Boca Raton, Florida: CRC Press.
   Google Scholar
• Jedrychowski, L. (1999). Reduction of the antigenicity of whey proteins by lactic acid fermentation. Food Agric. Immunol. 11:91–99.
   Web of Science ®Google Scholar
• Jiraratananon, R. and Chanachai, A. (1996). A study of fouling in the ultrafiltration of passion fruit juice. J. Membrane Sci. 111:39–48.
   Web of Science ®Google Scholar
• Jiraratananon, R., Uttapap, D. and Tangamornsuksun, C. (1997). Self-forming dynamic membrane for ultrafiltration of pineapple juice. J. Membrane Sci. 129:135–143.
   Web of Science ®Google Scholar
• Karel, M. (1985). Effects of water activity and water content on mobility of food components, and their effects on phase transitions in food systems. In: Properties of Water in Foods, pp. 153–169. Simatos, D. and Multon, J. L., Eds., Springer, Netherlands.
   Google Scholar
• Kato, T., Katayama, E., Matsubara, S., Omi, Y. and Matsuda, T. (2000). Release of allergenic proteins from rice grains induced by high hydrostatic pressure. J. Agric. Food Chem. 48:3124–3129.
   PubMed Web of Science ®Google Scholar
• Katz, E. E. and Labuza, T. P. (1981). Effect of water activity on the sensory crispness and mechanical deformation of snack food products. J. Food Sci. 46:403–409.
   Web of Science ®Google Scholar
• Kim, S.-M., Park, J.-G., Kim, K., Lee, J., Byun, M., Park, S. and Ahn, D. (2006). Study on the changes in allergen allergenicity originated from shrimp by physical treatments. J. Korean Soc. Food Sci. Nutr. 35.
   Google Scholar
• Kirk, D., Montgomery, M. and Kortekaas, M. (1983). Clarification of pear juice by hollow fiber ultrafiltration. J. Food Sci. 48:1663–1667.
   Web of Science ®Google Scholar
• Kleber, N., Maier, S. and Hinrichs, J. (2007). Antigenic response of bovine β-lactoglobulin influenced by ultra-high pressure treatment and temperature. Innov. Food Sci. Emerg. Technol. 8:39–45.
   Web of Science ®Google Scholar
• Kleine-Tebbe, J., Wangorsch, A., Vogel, L., Crowell, D. N., Haustein, U. F. and Vieths, S. (2002). Severe oral allergy syndrome and anaphylactic reactions caused by a Bet v 1-related PR-10 protein in soybean, SAM22. J. Allergy Clin. Immunol. 110:797–804.
   PubMed Web of Science ®Google Scholar
• Klotz, I. M., Langebman, N. and Dahnall, D. (1970). Quaternary structure of proteins. Ann. Rev. Biochem. 39:25–62.
   PubMed Web of Science ®Google Scholar
• Knorr, D. (1993). Effects of high-hydrostatic-pressure processes on food safety and quality. Food Technol. 47:156–161.
   Web of Science ®Google Scholar
• Koppelman, S. J., Bruijnzeel-Koomen, C. A. F. M., Hessing, M. and De Jongh, H. H. J. (1999). Heat-induced conformational changes of Ara h 1, a major peanut allergen, do not affect its allergenic properties. Journal of Biological Chemistry. 274:4770–4777.
   Google Scholar
• Koshland Jr, D. (1958). Application of a theory of enzyme specificity to protein synthesis. Proc. Natl. Acad. Sci. USA 44:98.
   Google Scholar
• Koutchma, T. N. F. L. J. M. C. I. (2009). Ultraviolet Light in Food Technology Principles and Applications. CRC Press, Boca Raton.
   Google Scholar
• Kuehler, C. and Stine, C. (1974). Effect of enzymatic hydrolysis on some functional properties of whey protein. J. Food Sci. 39:379–382.
   Web of Science ®Google Scholar
• Kume, T. and Matsuda, T. (1995). Changes in structural and antigenic properties of proteins by radiation. Radiat. Phys. Chem. 46:225–231.
   Web of Science ®Google Scholar
• Lado, B. H. and Yousef, A. E. (2002). Alternative food-preservation technologies: Efficacy and mechanisms. Microb. Infect. 4:433–440.
   PubMed Web of Science ®Google Scholar
• Lagunas-Solar, M. C. (1995). Radiation processing of foods: An overview of scientific principles and current status. J. Food Protect.®. 58:186–192.
   PubMed Web of Science ®Google Scholar
• Ledikwe, J. H., Blanck, H. M., Khan, L. K., Serdula, M. K., Seymour, J. D., Tohill, B. C. and Rolls, B. J. (2006). Dietary energy density is associated with energy intake and weight status in US adults. Amer. J. Clin. Nutr. 83:1362–1368.
   PubMed Web of Science ®Google Scholar
• Leduc, V., Moneret-Vautrin, D. A., Guerin, L., Morisset, M. and Kanny, G. (2003). Anaphylaxis to wheat isolates: Immunochemical study of a case proved by means of double-blind, placebo-controlled food challenge [1]. J. Allergy Clin. Immunol.; 111:897–899.
   PubMed Web of Science ®Google Scholar
• Lee, D. and Putnam, G. (1973). The response of rainbow trout to varying protein/energy ratios in a test diet. J. Nutr. 103:916–922.
   PubMed Web of Science ®Google Scholar
• Lee, J.-W., Kim, J.-H., Yook, H.-S., Kang, K.-O., Lee, S.-Y., Hwang, H.-J. and Byun, M.-W. (2001). Effects of gamma radiation on the allergenic and antigenic properties of milk proteins. J. Food Protect. 64:272–276.
   PubMed Web of Science ®Google Scholar
• Lee, J. W., Seo, J. H., Kim, J. H., Lee, S. Y., Kim, K. S. and Byun, M. W. (2005). Changes of the antigenic and allergenic properties of a hen's egg albumin in a cake with gamma-irradiated egg white. Radiat. Phys. Chem. 72:645–650.
   Web of Science ®Google Scholar
• Lehrer, S. B., Ayuso, R. and Reese, G. (2002). Current understanding of food allergens. Annal. New York Acad. Sci. 964:69–85.
   PubMed Web of Science ®Google Scholar
• Lew, A., Krutzik, P. O., Hart, M. E. and Chamberlin, A. R. (2002). Increasing rates of reaction: Microwave-assisted organic synthesis for combinatorial chemistry. J. Combinat. Chem. 4:95–105.
   PubMed Web of Science ®Google Scholar
• Li, H., Zhu, K., Zhou, H. and Peng, W. (2012). Effects of high hydrostatic pressure treatment on allergenicity and structural properties of soybean protein isolate for infant formula. Food Chem. 132:808–814.
   Web of Science ®Google Scholar
• Li, Y., Yang, W., Chung, S.-Y., Chen, H., Ye, M., Teixeira, A. A., Gregory, J. F., Welt, B. A. and Shriver, S. (2013). Effect of pulsed ultraviolet light and high hydrostatic pressure on the antigenicity of almond protein extracts. Food Bioproc. Technol. 6:431–440.
   Web of Science ®Google Scholar
• Li, Z. X., Lin, H., Cao, L. M. and Jameel, K. (2006). Effect of high intensity ultrasound on the allergenicity of shrimp. J. Zhejiang Univer. Sci. B. 7:251–256.
   PubMedGoogle Scholar
• Liu, B.-L. and Tzeng, Y.-M. (1999). Water content and water activity for the production of cyclodepsipeptides in solid-state fermentation by Metarhizium anisopliae. Biotechnol. Lett. 21:657–661.
   Web of Science ®Google Scholar
• Liu, G. M., Cheng, H., Nesbit, J. B., Su, W. J., Cao, M. J. and Maleki, S. J. (2010). Effects of boiling on the IgE-binding properties of tropomyosin of shrimp (Litopenaeus vannamei). J. Food Sci. 75:T1–T5.
   PubMed Web of Science ®Google Scholar
• Lopata, A. and Potter, P. (2000). Allergy and other adverse reactions to seafood. Allergy Clin. Immunol. Int. 12:271–281.
   Google Scholar
• Lopata, A. L. and Lehrer, S. B. (2009). New insights into seafood allergy. Current Opinion in Allergy and Clinical Immunology. 9:270–277.
   Google Scholar
• López-Expósito, I., Chicón, R., Belloque, J., López-Fandiño, R. and Berin, M. C. (2012). In vivo methods for testing allergenicity show that high hydrostatic pressure hydrolysates of β-lactoglobulin are immunologically inert. J. Dairy Sci. 95:541–548.
   PubMed Web of Science ®Google Scholar
• Macfarlane, G. T. and Cummings, J. H. (1999). Probiotics and prebiotics: Can regulating the activities of intestinal bacteria benefit health? Brit. Med. J. 318:999–1003.
   PubMed Web of Science ®Google Scholar
• Malanin, K., Lundberg, M. and Johansson, S. G. O. (1995). Anaphylactic reaction caused by neoallergens in heated pecan nut. Allergy: Eur. J. Allergy Clin. Immunol. 50:988–991.
   Web of Science ®Google Scholar
• Maleki, S. J., Chung, S. Y., Champagne, E. T. and Raufman, J. P. (2000). The effects of roasting on the allergenic properties of peanut proteins. J. Allergy Clin. Immunol. 106:763–768.
   PubMed Web of Science ®Google Scholar
• Manzocco, L., Panozzo, A. and Nicoli, M. C. (2012). Effect of ultraviolet processing on selected properties of egg white. Food Chem. 135:522–527.
   PubMed Web of Science ®Google Scholar
• Marzban, G., Herndl, A., Pietrozotto, S., Banerjee, S., Obinger, C., Maghuly, F., Hahn, R., Boscia, D., Katinger, H. and Laimer, M. (2009). Conformational changes of Mal d 2, a thaumatin-like apple allergen, induced by food processing. Food Chem. 112:803–811.
   Web of Science ®Google Scholar
• Matsuzaki, T. and Chin, J. (2000). Modulating immune responses with probiotic bacteria. Immunol. Cell Biol. 78:67–73.
   PubMed Web of Science ®Google Scholar
• McFeeters, R. (1988). Effects of fermentation on the nutritional properties of food. In: Nutritional Evaluation of Food Processing, 1st ed., pp. 423–446. Karmas, E. and Harris, R., Eds., Springer, Netherlands.
   Google Scholar
• Meda, V., Orsat, V., Raghavan, V., Schubert, H. and Regier, M. (2005). Microwave heating and the dielectric properties of foods. The Microwave Processing of Foods: 61–75.
   Google Scholar
• Metchnikoff, E. (1907). The prolongation of life. Optimistic studies. Prolongat. Life. 1st ed.
   Google Scholar
• Mittag, D., Vieths, S., Vogel, L., Becker, W. M., Rihs, H. P., Helbling, A., Wüthrich, B. and Ballmer-Weber, B. K. (2004). Soybean allergy in patients allergic to birch pollen: Clinical investigation and molecular characterization of allergens. J. Allergy Clin. Immunol. 113:148–154.
   PubMed Web of Science ®Google Scholar
• Morild, E. (1981). The Theory of Pressure effects on enzymes. Adv. Prot. Chem. 34:93–166.
   PubMedGoogle Scholar
• Mottram, D. S., Wedzicha, B. L. and Dodson, A. T. (2002). Food chemistry: Acrylamide is formed in the Maillard reaction. Nature. 419:448–449.
   PubMed Web of Science ®Google Scholar
• Mudgett, R. (1989). Microwave food processing. Food Technol. (USA).
   PubMed Web of Science ®Google Scholar
• Nagpal, S., Rajappa, L., Metcalfe, D. D. and Subba Rao, P. V. (1989). Isolation and characterization of heat-stable allergens from shrimp (Penaeus indicus). J. Allergy Clin. Immunol. 83:26–36.
   PubMed Web of Science ®Google Scholar
• Nanda, R., James, R., Smith, H., Dudley, C. and Jewell, D. (1989). Food intolerance and the irritable bowel syndrome. Gut. 30:1099–1104.
   PubMed Web of Science ®Google Scholar
• Naqpal, S., Rajappa, L., Metcalfe, D. D. and Rao, P. V. (1989). Isolation and characterization of heat-stable allergens from shrimp (Penaeus indicus). J. Allergy Clin. Immunol. 83:26–36.
   PubMed Web of Science ®Google Scholar
• Ogawa, A., Samoto, M. and Takahashi, K. (2000). Soybean allergens and hypoallergenic soybean products. J. Nutr. Sci. Vitaminol. 46:271–279.
   PubMed Web of Science ®Google Scholar
• Oliveira, M. E. C. and Franca, A. S. (2002). Microwave heating of foodstuffs. J. Food Eng. 53:347–359.
   Web of Science ®Google Scholar
• Olofsson, M., Buhler, M. and Wood, R. (1981). Process for the preparation of a purified protein hydrolysate. Google Patents. US Patent 4,293,571.
   Google Scholar
• Opitz, C. A., Kulke, M., Leake, M. C., Neagoe, C., Hinssen, H., Hajjar, R. J. and Linke, W. A. (2003). Damped elastic recoil of the titin spring in myofibrils of human myocardium. Proc. Natl. Acad. Sci. 100:12688–12693.
   Google Scholar
• Oriol, E., Raimbault, M., Roussos, S. and Viniegra-Gonzales, G. (1988). Water and water activity in the solid state fermentation of cassava starch by Aspergillus niger. Appl. Microbiol. Biotechnol. 27:498–503.
   Web of Science ®Google Scholar
• Panyam, D. and Kilara, A. (1996). Enhancing the functionality of food proteins by enzymatic modification. Trends Food Sci. Technol. 7:120–125.
   Web of Science ®Google Scholar
• Peñas, E., Gomez, R., Frias, J., Baeza, M. L. and Vidal-Valverde, C. (2011). High hydrostatic pressure effects on immunoreactivity and nutritional quality of soybean products. Food Chem. 125:423–429.
   Web of Science ®Google Scholar
• Peñas, E., Préstamo, G., Luisa Baeza, M., Martínez-Molero, M. I. and Gomez, R. (2006a). Effects of combined high pressure and enzymatic treatments on the hydrolysis and immunoreactivity of dairy whey proteins. Int. Dairy J. 16:831–839.
   Web of Science ®Google Scholar
• Peñas, E., Snel, H., Floris, R., Préstamo, G. and Gomez, R. (2006b). High pressure can reduce the antigenicity of bovine whey protein hydrolysates. Int. Dairy J. 16:969–975.
   Web of Science ®Google Scholar
• Pereira, R. N. and Vicente, A. A. (2010). Environmental impact of novel thermal and non-thermal technologies in food processing. Food Res. Int. 43:1936–1943.
   Web of Science ®Google Scholar
• Pescuma, M., Hébert, E. M., Dalgalarrondo, M., Haertlé, T., Mozzi, F., Chobert, J. M. and De Valdez, G. F. (2009). Effect of exopolysaccharides on the hydrolysis of ß-lactoglobulin by lactobacillus acidophilus CRL 636 in an in vitro gastric/pancreatic system. J. Agric. Food Chem. 57:5571–5577.
   PubMed Web of Science ®Google Scholar
• Pescuma, M., Hébert, E. M., Rabesona, H., Drouet, M., Choiset, Y., Haertlé, T., Mozzi, F., De Valdez, G. F. and Chobert, J. M. (2011). Proteolytic action of Lactobacillus delbrueckii subsp. bulgaricus CRL 656 reduces antigenic response to bovine β-lactoglobulin. Food Chem. 127:487–492.
   PubMed Web of Science ®Google Scholar
• Pomeranz, Y. (1985). Functional Properties of Food Components. Academic Press, Orlando, Fla.
   Google Scholar
• Ponne, C. T. and Bartels, P. V. (1995). Interaction of electromagnetic energy with biological material—relation to food processing. Radiat. Phys. Chem. 45:591–607.
   Web of Science ®Google Scholar
• Popper, L. and Knorr, D. (1990). Applications of high-pressure homogenization for food preservation. Food Technol. 44:84–89.
   Web of Science ®Google Scholar
• Privalov, P., Tiktopulo, E., Venyaminov, S. Y., Griko, Y. V., Makhatadze, G. and Khechinashvili, N. (1989). Heat capacity and conformation of proteins in the denatured state. J. Mol. Biol. 205:737–750.
   PubMed Web of Science ®Google Scholar
• Qi, M., Hettiarachchy, N. and Kalapathy, U. (1997). Solubility and emulsifying properties of soy protein isolates modified by pancreatin. J. Food Sci. 62:1110–1115.
   Web of Science ®Google Scholar
• Rahman, S. (1995). Food Properties Handbook. CRC Press, Boca Raton, FL.
   Google Scholar
• Reese, G., Ayuso, R., Carle, T. and Lehrer, S. B. (1999). IgE-binding epitopes of shrimp tropomyosin, the major allergen Pen a 1. Int. Arch. Allerg. Immunol. 118:300–301.
   PubMed Web of Science ®Google Scholar
• Richardson, P. (2001). Thermal Technologies in Food Processing. CRC Press; Woodhead Pub., Boca Raton, Fla.; Cambridge, England.
   Google Scholar
• Rivalain, N., Roquain, J. and Demazeau, G. (2010). Development of high hydrostatic pressure in biosciences: Pressure effect on biological structures and potential applications in Biotechnologies. Biotechnol. Adv. 28:659–672.
   PubMed Web of Science ®Google Scholar
• Roudaut, G., Dacremont, C. and Meste, M. L. (1998). Influence of water on the crispness of cereal-based foods: Acoustic, mechanical, and sensory studies. J. Texture Stud. 29:199–213.
   Web of Science ®Google Scholar
• Sablani, S., Marcotte, M., Baik, O. and Castaigne, F. (1998). Modeling of simultaneous heat and water transport in the baking process. LWT-Food Sci. Technol. 31:201–209.
   Web of Science ®Google Scholar
• Salminen, S., Ouwehand, A. C. and Isolauri, E. (1998). Clinical applications of probiotic bacteria. Int. Dairy J. 8:563–572.
   Web of Science ®Google Scholar
• Sampson, H. A. (2004). Update on food allergy. Journal of Allergy and Clinical Immunology. 113:805–819.
   Google Scholar
• Sanger, F. (1952). The arrangement of amino acids in proteins. Adv. Protein Chem. 7:1.
   PubMedGoogle Scholar
• Sathe, S. K., Teuber, S. S. and Roux, K. H. (2005). Effects of food processing on the stability of food allergens. Biotechnol. Adv. 23:423–429.
   PubMed Web of Science ®Google Scholar
• Schmitt, D. A., Cheng, H., Maleki, S. J. and Burks, A. W. (2004). Competitive inhibition ELISA for quantification of Ara h 1 and Ara h 2, the major allergens of peanuts. Journal of AOAC International. 87:1492–1497.
   Google Scholar
• Schubert, H. R. M. (2005). The Microwave Processing of Foods. Woodhead, Cambridge.
   Google Scholar
• Scott, W. (1957). Water relations of food spoilage microorganisms. Adv. Food Res. 7:168.
   Google Scholar
• Sen, M., Kopper, R., Pons, L., Abraham, E. C., Burks, A. W. and Bannon, G. A. (2002). Protein structure plays a critical role in peanut allergen stability and may determine immunodominant IgE-binding epitopes. J. Immunol. 169:882–887.
   PubMed Web of Science ®Google Scholar
• Seo, J.-H., Kim, J.-H., Lee, J.-W., Yoo, Y.-C., Kim, M. R., Park, K.-S. and Byun, M.-W. (2007). Ovalbumin modified by gamma irradiation alters its immunological functions and allergic responses. Int. Immunopharmacol. 7:464–472.
   PubMed Web of Science ®Google Scholar
• Seo, J.-H., Lee, J.-W., Lee, Y.-S., Lee, S.-Y., Kim, M.-R., Yook, H.-S. and Byun, M.-W. (2004). Change of an egg allergen in a white layer cake containing gamma-irradiated egg white. J. Food Protect.®. 67:1725–1730.
   PubMed Web of Science ®Google Scholar
• Shreffler, W. G., Castro, R. R., Kucuk, Z. Y., Charlop-Powers, Z., Grishina, G., Yoo, S., Burks, A. W., Sampson, H. A. (2006). The major glycoprotein allergen from Arachis hypogaea, Ara h 1, is a ligand of dendritic cell-specific ICAM-grabbing nonintegrin and acts as a Th2 adjuvant in vitro. J. Immunol. 177(6):3677–3685.
   PubMed Web of Science ®Google Scholar
• Shriver, S., Yang, W., Chung, S.-Y. and Percival, S. (2011). Pulsed ultraviolet light reduces immunoglobulin E binding to Atlantic white shrimp (Litopenaeus setiferus) extract. Int. J. Environ. Res. Public Health 8:2569–2583.
   PubMed Web of Science ®Google Scholar
• Shriver, S. K. and Yang, W. W. (2011). Thermal and nonthermal methods for food allergen control. Food Eng. Rev. 3:26–43.
   Web of Science ®Google Scholar
• Sicherer, S. H. and Sampson, H. A. (2007). Peanut allergy: Emerging concepts and approaches for an apparent epidemic. Journal of Allergy and Clinical Immunology. 120:491–503.
   Google Scholar
• Sikorski, Z. E. (2007). Chemical and Functional Properties of Food Components. CRC Press, Boca Raton, FL.
   Google Scholar
• Sinanoglou, V. J., Batrinou, A., Konteles, S. and Sflomos, K. (2007). Microbial population, physicochemical quality, and allergenicity of molluscs and shrimp treated with cobalt-60 gamma radiation. J. Food Protect. 70:958–966.
   PubMed Web of Science ®Google Scholar
• Singh, A., Munshi, S. and Raghavan, V. (2013a). Effect of external electric field stress on gliadin protein conformation. Proteomes. 1:25–39.
   PubMedGoogle Scholar
• Singh, A., Orsat, V. and Raghavan, V. (2013b). Soybean hydrophobic protein response to external electric field: a molecular modeling approach. Biomolecules. 3:168–179.
   PubMedGoogle Scholar
• Sivasankar, B. (2002). Food Processing and Preservation. PHI Learning Pvt. Ltd, New Delhi, India.
   Google Scholar
• Smeller, L. (2002). Pressure-temperature phase diagrams of biomolecules. Biochimica et Biophysica Acta—Protein Struct. Mol. Enzymol. 1595:11–29.
   PubMed Web of Science ®Google Scholar
• Smith, D. M. (1994). Protein Interactions in Gels: Protein-Protein Interactions. Marcel Dekker, New York.
   Google Scholar
• Smith, J. and Charter, E. (2011). Functional Food Product Development. Chichester-West Sussex-Ames, Iowa: Wiley-Blackwell.
   Google Scholar
• Soria, A. C. and Villamiel, M. (2010). Effect of ultrasound on the technological properties and bioactivity of food: A review. Trend. Food Sci. Technol. 21:323–331.
   Web of Science ®Google Scholar
• Spies, J. R. (1974). Allergens. J. Agric. Food Chem. 22:30–36.
   PubMed Web of Science ®Google Scholar
• Stanic-Vucinic, D., Stojadinovic, M., Atanaskovic-Markovic, M., Ognjenovic, J., Grönlund, H., van Hage, M., Lantto, R., Sancho, A. I. and Velickovic, T. C. (2012). Structural changes and allergenic properties of β-lactoglobulin upon exposure to high-intensity ultrasound. Mol. Nutr. Food Res. 56:1894–1905.
   PubMed Web of Science ®Google Scholar
• Su, M., Venkatachalam, M., Teuber, S. S., Roux, K. H. and Sathe, S. K. (2004). Impact of γ-irradiation and thermal processing on the antigenicity of almond, cashew nut and walnut proteins. J. Sci. Food Agric. 84:1119–1125.
   Web of Science ®Google Scholar
• Sun, D.-W. (2005). Emerging Technologies for Food Processing. Elsevier Academic Press, San Diego, Calif.
   Google Scholar
• Tammineedi, C. V. R. K., Choudhary, R., Perez-Alvarado, G. C. and Watson, D. G. (2013). Determining the effect of UV-C, high intensity ultrasound and nonthermal atmospheric plasma treatments on reducing the allergenicity of α-casein and whey proteins. LWT - Food Sci. Technol. 54:35–41.
   Web of Science ®Google Scholar
• Tanford, C. (1968). Protein denaturation. Adv. Protein Chem. 23:282.
   Google Scholar
• Tewari, G. J. V. K. (2007). Advances in Thermal and Non-Thermal Food Preservation. Blackwell Pub., Ames, Iowa.
   Google Scholar
• Thomas, K., Herouet-Guicheney, C., Ladics, G., Bannon, G., Cockburn, A., Crevel, R., Fitzpatrick, J., Mills, C., Privalle, L. 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.
   PubMed Web of Science ®Google Scholar
• Thorvaldsson, K. and Skjöldebrand, C. (1998). Water diffusion in bread during baking. LWT-Food Sci. Technol. 31:658–663.
   Web of Science ®Google Scholar
• Van Holde, K. (1977). Effects of amino acid composition and microenvironment on protein structure.
   Google Scholar
• Venkatachalam, M., Monaghan, E. K., Kshirsagar, H. H., Robotham, J. M., O'Donnell, S. E., Gerber, M. S., Roux, K. H. and Sathe, S. K. (2008). Effects of processing on immunoreactivity of cashew nut (Anacardium occidentale L.) seed flour proteins. J. Agric. Food Chem. 56:8998–9005.
   PubMed Web of Science ®Google Scholar
• Venkatachalam, M., Teuber, S. S., Roux, K. H. and Sathe, S. K. (2002). Effects of roasting, blanching, autoclaving, and microwave heating on antigenicity of almond (Prunus dulcis L.) proteins. J. Agric. Food Chem. 50:3544–3548.
   PubMed Web of Science ®Google Scholar
• Venkatesh, M. and Raghavan, G. (2004). An overview of microwave processing and dielectric properties of agri-food materials. Biosyst. Eng. 88:1–18.
   Web of Science ®Google Scholar
• Vieths, S., Zagon, J., Fischer, K., Dehne, L. and Bögl, K. (1995). Verarbeitungsbedingte Einfluesse auf das allergene Potential von Lebensmitteln. Die Sojaallergie als Modellbeispiel. Lebensmittelchemie. 49, Germany.
   Google Scholar
• Vignais, P., Barbu, E., Macheboeuf, M. and Basset, M. (1952). Antigenic and vaccinal power of bacteria killed by pressure. Pouvoir antigène et vaccinant de bactéries tuées par pression. 34:43–46.
   Google Scholar
• Vladisavljević, G., Vukosavljević, P. and Bukvić, B. (2003). Permeate flux and fouling resistance in ultrafiltration of depectinized apple juice using ceramic membranes. J. Food Eng. 60:241–247.
   Web of Science ®Google Scholar
• Watanabe, M., Miyakawa, J., Ikezawa, Z., Suzuki, Y., Hirao, T., Yoshizawa, T. and Arai, S. (1990). Production of hypoallergenic rice by enzymatic decomposition of constituent proteins. J. Food Sci. 55:781–783.
   Web of Science ®Google Scholar
• Whitford, D. (2005). Proteins: Structure and Function. J. Wiley & Sons, Hoboken, NJ.
   Google Scholar
• Wigotzki, M., Steinhart, H. and Paschke, A. (2000). Influence of varieties, storage and heat treatment on IgE-binding proteins in hazelnuts (Corylus avellana). Food Agric. Immunol. 12:217–229.
   Web of Science ®Google Scholar
• Wilson, S., Blaschek, K. and de Mejia, E. G. (2005). Allergenic proteins in soybean: processing and reduction of P34 allergenicity. Nutr. Rev. 63:47–58.
   PubMed Web of Science ®Google Scholar
• Winter, R., Dzwolak, W., Wolynes, P. G., Dobson, C. M. and Saykally, R. J. (2005). Exploring the temperature-pressure configurational landscape of biomolecules: From lipid membranes to proteins. Philosophic. Trans. R Soc. A. 363:537–563.
   PubMed Web of Science ®Google Scholar
• Wu, C. H., Nakai, S. and Powrie, W. D. (1976). Preparation and properties of acid-solubilized gluten. J. Agric. Food Chem. 24:504–510.
   PubMed Web of Science ®Google Scholar
• Yang, W., Mwakatage, N., Goodrich-Schneider, R., Krishnamurthy, K. and Rababah, T. (2012). Mitigation of major peanut allergens by pulsed ultraviolet light. Food Bioproc. Technol. 5:2728–2738.
   Web of Science ®Google Scholar
• Yang, W. W., Chung, S.-Y., Ajayi, O., Krishnamurthy, K., Konan, K. and Goodrich-Schneider, R. (2010). Use of pulsed ultraviolet light to reduce the allergenic potency of soybean extracts. Int. J. Food Eng. 6.
   Web of Science ®Google Scholar
• Zaks, A. and Klibanov, A. M. (1988). The effect of water on enzyme action in organic media. J. Biologic. Chem. 263:8017–8021.
   PubMed Web of Science ®Google Scholar
• Zeece, M., Huppertz, T. and Kelly, A. (2008). Effect of high-pressure treatment on in-vitro digestibility of β-lactoglobulin. Innovat. Food Sci. Emerg. Technol. 9:62–69.
   Web of Science ®Google Scholar
• Zhang, J. (1995). NMR study of the cold, heat, and pressure unfolding of ribonuclease A. Biochemistry®. 34:8631–8641.
   PubMed Web of Science ®Google Scholar
• Zhenxing, L., Caolimin, L. and Jamil, K. (2006). Reduction of allergenic properties of shrimp (Penaeus Vannamei) allergens by high intensity ultrasound. Eur. Food Res. Technol. 223:639–644.
   Web of Science ®Google Scholar
• Zhenxing, L., Hong, L., Limin, C. and Jamil, K. (2007a). Impact of irradiation and thermal processing on the immunoreactivity of shrimp (Penaeus vannamei) proteins. J. Sci. Food Agric. 87:951–956.
   Web of Science ®Google Scholar
• Zhenxing, L., Hong, L., Limin, C. and Jamil, K. (2007b). The influence of gamma irradiation on the allergenicity of shrimp (Penaeus vannamei). J. Food Eng. 79:945–949.
   Web of Science ®Google Scholar
• Zhong, J., Liu, C., Liu, W., Cai, X., Tu, Z. and Wan, J. (2011). Effect of dynamic high-pressure microfluidization at different temperatures on the antigenic response of bovine β-lactoglobulin. Eur. Food Res. Technol. 233:95–102.
   Web of Science ®Google Scholar