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Jantwal, Chetna
- A Review on Identified Major Food Allergens:Characteristics and Role in Food Allergy
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1 Department of Home science, D.S.B Campus, Kumaun University, Nainital, Uttarakhand, IN
1 Department of Home science, D.S.B Campus, Kumaun University, Nainital, Uttarakhand, IN
Source
The Indian Journal of Nutrition and Dietetics, Vol 54, No 3 (2017), Pagination: 346-365Abstract
Food allergens are the substances present in food that cause food allergy. Human body reactions to food allergens range from mild to severe life threatening anaphylactic shock. At least seventy different foods have been reported to cause allergic reactions and several other foods have been identified which have the potential to provoke allergic reactions. Majority of the identified food allergens are proteins. The Food Allergen Labeling and Consumer Protection Act (FALCPA) identifies eight major food groups i.e. milk, eggs, fish, crustacean shellfish, tree nuts, peanuts, wheat, and soybeans as major allergy causing foods. These eight foods are believed to account for 90 per cent of food allergies and are responsible for most serious reactions to foods. Several studies have been done which identify the major allergens in various foods. The present paper attempts to review the major allergens present in various food.Keywords
Allergens, Allergic Reactions, Cross Reactivity.
References
- Bjorksten, B., Crevel, R., Hschenhuber, C., Lovik, M., Samuls, F., Strobll, S., Taylor, S.L., Wal, J.M. and Ward, R. Criteria for identifying allergenic foods of public health importance. Regul. Toxic. Pharmacil., 2008, 51, 42–52.
- Ricci, G., Patrizi, A., Baldi, E., Menna, G., Tabanelli, M. and Masi, M. Long-term follow up of atopic dermatitis: retrospective analysis of related risk factors and association with concomitant allergic diseases. J. Am. Acad. Dermatol., 2006, 55, 765–771.
- Anet, J., Back, J.F., Baker, R.S., Barnett, D., Burley, R.W. and Howden, M.E. Allergens in the white and yolk of hen’s egg. A study of IgE binding by egg proteins. Int. Arch. Allergy Appl. Immunol., 1985, 77, 364–371.
- Bonds, R.S., Midoro-Horiuti, T. and Goldblum, R. A structural basis for food allergy: the role of cross-reactivity. Curr. Opin. Allergy Clin. Immunol., 2008, 8, 82–86.
- Hansen, K.S., Ballmer, W.B.K., Luttkopf, D., Skov, P.S., Wuthrich, B., Bindslev, J.C., Vieths, S. and Poulsen, L.K. Roasted hazelnut: allergrnic activity evaluated by double blind, placebo controlled food challenge. Allergy Copenhagen., 2003, 58, 132–138.
- Sampson, H.A. Peanut allergy. N. Engl. J. Med., 2002, 346, 1294–1299.
- Taylor, S.L., Hefle, S.L. and Munoz-Furlong, A. Food allergies and avoidance diets. Nutr. To day. 1999, 34, 15–22.
- Hefle, S.L., Nordlee, J.A. and Taylor, S.L. Allergenic foods. Crit. Rev. Fd. Sci. Nutr., 1996, 36, 69–89.
- Pestka, J.J. Food, diet and gastrointestinal immune function. Adv. Fd. Nutr. Res., 1993, 37, 1–53.
- Tong-Jen, F., Upasana, R, Abbott and Catherine, H. J. Agric., Fd. Chem., 2002, 50, 7154–7160.
- Besler, M., Steinhart, H. and Paschke, A. Stability of food allergens and allergenicity of processed foods. J. Chromatogr. B. Biomed. Sci. Appl., 2001, 756, 207–228.
- Poms, R.E., Klein, C.L. and Anklam, E. Methods for food allergen analysis in food: a review. Fd. Addit. Contam., 2004, 21, 1–31.
- Bonds, R.S., Midoro-Horiuti, T. and Goldblum, R. A structural basis for food allergy: the role of cross-reactivity. Curr. Opin. Allergy Clin. Immunol., 2008, 8, 82–86.
- Garcia, orozco. K.D., Aisspuro, H.E., YPG, Calderon-de-la-barca AM, Sotelo MRR.2008.
- Bousquet, J., Bjorksten, B., Bruijnzeel-Koomen. C.A.F.M., Huggett, A., Ortolani, C., Warner, J.O. and Smith, M. Scientific criteria and the selection of allergenic foods for product labeling. Allergy. 1998, 53, 3–21.
- Hefle, S.L., Nordlee, J.A. and Taylor, S.L. Allergenic foods. Crit. Rev. Fd. Sci. Nutr., 1996, 36, 69–89.
- Scott H. Sicherer and hugh A. Sampson. Food allergy: Recent Advances in pathophysiology and treatment. Annu. Rev. Med., 2009, 60, 261–277.
- Jonathan, B. Roses. Food allergen law and the food allergen labeling and consumer protection act of 2004: Falling short of true protection for allergy sufferers. Fd. Drug Law J., 2011, 66, 225–242.
- Furuta, G.T. Cow milk protein allergy. Encyclopedia of gastroenterol., Elsevier USA. 2004, 506–508.
- Du, T.G., Meyer, R., Shah, N., Heine, R.G., Thomson, M.A., Lack, G. and Fox, A.T. Identifying and managing cow’s milk protein allergy. Arch. Dis. Child Educ. Pract. Ed. 2010, 95, 134–144.
- Host, A. and Samuelsson, E.G. Allergic reactions to raw, pasteurized and homogenized/pasteurized cow milk: A comparison. A double-blind placebo-controlled study in milk allergic children. Allergy. 1988, 43, 113–118.
- Ricci, G., Patrizi, A., Baldi, E., Menna, G., Tabanelli, M. and Masi, M. Long-term followup of atopic dermatitis: retrospective analysis of related risk factors and association with concomitant allergic diseases. J. Am. Acad. Dermatol., 2006, 55, 765–771.
- Takaoka, Y., Futamura, M., Sakamoto, T. and Ito, K. Analysis of the risk factors to persistent milk allergy. Arerugi, 2010, 59.
- Wal, J.M. Bovine milk allergenicity. Ann. Allergy Asthma Immunol., 2004, 93, 2–11.
- Restani, P., Ballabio, C., Di Lorenzo, C., Tripodi, S. and Fiocchi. A: Molecular aspects of milk allergens and their role in clinical events. Anal. Bioanal. Chem., 2009, 395, 47–56.
- Shek, L.P., Bardina, L., Castro, R., Sampson, H.A. and Beyer, K. Humoral and cellular responses to cow milk proteins in patients with milk-induced IgE mediated and non-IgE-mediated disorders. Allergy. 2005, 60, 912–919.
- Francesco, B., Barbara, B., Luigi, C., Miris, M., Pamela, P., Caffarelli et al. Cow’s milk protein allergy in children: a practical guide. Italian J. Pediat., 2010, 36, 5. http://www.ijponline.net/content/36/1/5.
- Restani, P., Beretta, B., Fiocchi, A., Ballabio, C. and Galli, C.L. Cross reactivity between mammalian proteins. Ann. Allergy Asthama Immunol., 2002, 89, 11–15.
- Nowak, W.A., Bloom, K.A. and Sichere, S.H. Tolerance to extensively healed milk in children with cow’s milk allergy. J. Allergy Clin. Immunol., 2008, 122, 342–347.
- Kim, J.S., Nowak, W.A., Sichere, S.H., Noone, S., Moshie, E.L. and Sampson, H.A. dietary baked milk accelerates the resolution of cow’s milk allergy in children. J. Allergy Clin. Immunol., 2011, 128, 125–131.
- Host, A. and Samuelsson, E.G. Allergic reactions to raw, pasteurized, and homogenized/pasteurized cow milk: A comparison. A double-blind placebo-controlled study in milk allergic children. Allergy, 1988, 43, 113–118.
- Norgaard, A., Bindslev-Jensen, C. and Poulsen, L.K. IgE binding to egg white and yolk are due to common and distinct allergens. Allergy Clin. Immunol. News. 1994, 56, 445.
- Sampson, H.A., Bernhisel-Broadbent, J., Yang, E. and Scanlon, S.M. Safety of casein hydrolysate formula in children with cow milk allergy. J. Pediat., 1991, 118, 520–525.
- Saylor, J.D. and Bahna, S.L. Anaphylaxis to casein hydrolysate formula. J. Pediat., 1991, 118, 71–74.
- Maleki, S.J. Food processing: effects on allergenicity. Curr. Opin. Allergy Clin. Immunol., 2004, 4, 241–245.
- Hill, D.J., Hosking, C.S. and De Benedictis, F.M. confirmation of the association between high levels of immunoglobulin E food sensitization and eczema in infancy: an international study. Clin. Exp. Allergy. 2008, 38, 161–168.
- Heine, R.G., Laske, N. and Hill, D.J. The diagnosis and management of egg allergy. Curr. Allergy Asthma Rep., 2006, 6, 145–52.
- Miller, H. and Campbell, D.H. Skin test reactions to various chemical fractions of egg white and their possible clinical significance. J. Allergy, 1950, 21, 522–524.
- Bleumink, E. and Young, E. Studies on the atopic allergen in hen’s egg. II. Further characterization of the skin-reactive fraction in egg-white; immuno-electrophoretic studies. Int. Arch. Allergy Appl. Immunol., 1971, 40, 72–88.
- Cooke, S.K. and Sampson, H.A. Allergenic properties of ovomucoid in man. J. Immunol., 1997, 159, 2026–2032.
- Seo, J.H., Lee, J.W., Lee, Y.S., Lee, S.Y., Kim, M.R., Yook, H.S. and Byun, M.W. J. Fd. Prot., 2004, 67, 1725–1730.
- Besler, M., Steinhart, H. and Paschke, A. Stability of food allergens and allergenicity of processed foods. J. Chromatogr. B. Biomed. Sci. Appl., 2001, 756, 207–228.
- Anet, J., Back, J.F., Baker, R.S., Barnett, D., Burley, R.W. and Howden, M.E. Allergens in the white and yolk of hen’s egg. A study of IgE binding by egg proteins. Int. Arch. Allergy Appl. Immunol., 1985, 77, 364–371.
- Urisu, A., Ando, H., Morita, Y., Wada, E., Yasaki, T., Yamada, K., Komada, K., Torii, S., Goto, M. and Wakamatsu, T. Allergenic activity of heated and ovomucoid-depleted egg white. J. Allergy Clin. Immunol., 1997, 100, 171–176.
- Sampson, H.A., Mendelson, L. and Rosen, J.P. fatal and near fatal anaphylactic reactions in children and adolescents. N. Engl. J. Med., 1992, 327, 380-384.
- Langeland, T. A clinical and immunological study of allergy to hen’s egg white. VI. Occurrence of proteins cross-reacting with allergens in hen’s egg white as studied in egg white from turkey, duck, goose, seagull and in hen egg yolk and hen and chicken sera and flesh. Allergy. 1983, 38, 399–412.
- Sharp, M.F. and Lapata, A.L. 2013. Fish allergy: In review. Clin. Rev. Allergy Immunol., 2013.10.1007/s12016-013-83363-1.
- Solensky, R. Resolution of fish Allergy: A case report. Ann. Allergy Asthama Immunol., 2003, 91, 411–412.
- Hamada, Y., Nagashimaa, Y. and Shiomi, K. Reactivity of IgE in fish allergic patients to fish muscle collagen. Allergol. Int., 2003, 52, 139–147.
- Untersmayr, E., Szalai, K., Riemer, A.B., Hemmer, W., Swoboda, I., Hantusch, B, et.al. Mimotopes identify conformational epitopes on parvalbumin, the major fish allergen. Mol. Immunol., 2006, 43, 1454–1461.
- Aas, K. and Elsayed, S.M. Characterization of a major allergen (cod). Effect of enzymic hydrolysis on the allergenic activity. J. Allergy. 1969, 44, 333–343.
- Elsayed, S. and Aas, K. Characterization of a major allergen (cod). Observations on effect of denaturation on the allergenic activity. J. Allergy.1971, 47, 283–291.
- Elsayed, S. and Apold, J. Immunochemical analysis of cod fish allergen M: locations of the immunoglobulin binding sites as demonstrated by the native and synthetic peptides. Allergy. 1983, 38, 449–459.
- Filimonov, V.V., Pfeil, W., Tsalkova, T.N. and Privalov, P.L. Thermodynamic investigations of proteins. IV. Calcium binding protein parvalbumin. Biophys. Chem., 1978, 8, 117–122.
- Takaoka, Y., Futamura, M., Sakamoto, T. and Ito, K. Analysis of the risk factors to persistent milk allergy. Arerugi., 2010, 59, 1562-1571.
- Elham, H., Zeinab, E. and Ayan, R. 2010. Sea food allergyreview article. Egypt J. pediat. Allergy Immunol., 2010, 8, 49–54.
- Kobayashi, A., Tanaka, H., Hamada, Y., Ishizaki, S., Nagashima, Y. and Shiomi, K. Comparison of allergenicity and allergens between fish white and dark muscles. Allergy, 2006, 61, 357–363.
- Pascual, C.R., Reche, M., Fiandor, A., Valbuena, T., Cuevas, T. and Esteban, M.M. Fish allergy in childhood. Pediat. Allergy Immunol., 2008, 19, 573–579.
- Sicherer, S.H. Clinical implications of cross-reactive food allergens. J. Allergy Clin. Immunol., 2001, 108, 881–890.
- Pascua, l.C., Martín Esteban, M. and Crespo, J.F. Fish allergy: evaluation of the importance of cross-reactivity. J. Pediat., 1992, 121, 29–34.
- Torres, B.J., Martínez Cuevas, J.F. and Tejero García, J. Cross reactivity between fish and shellfish. Allergol. Immunopathol(Madr)., 2003, 31, 146–51.
- Bernhisel-Broadbent, J., Strause, D. and Sampson, H.A. Fish hypersensitivity. II: Clinical relevance of altered fish allergenicity caused by various preparation methods. J. Allergy Clin. Immunol., 1992, 90, 622–629.
- Mata, E., Favier, C., Moneret-Vautrin, D., Nicolas, J., Ching, L. and Gueant, J. Surimi and native codfish contain a common allergen identified as a 63-kDa protein. Allergy. 1994, 49, 442–447.
- Eliot, H. Soyabean allerginicity and suppression of the immunodominant allergen. Crop Sci., 2005, 45, 462–467.
- Ricki, M.H.A., Wesley, B. and Eliot, H. Hypoallergenic foods- soya bean and peanuts, ISB news report.1-3, 2002.
- Ogawa, T., Bando, N., Tsuji, H., Nishikawa, K. and Kitamura, K. Alpha subunit of beta conglycinin, an allergic protein recognized by Ige antibodies of soya bean sensitive patients with atopic dermatitis. Biosci. Biotech. Biochem., 1995, 59, 831–833.
- Maroz, L.A. and Yang, W.H. kunitz soyabean trypsin inhibitor: A specific allergen in food anaphylaxis. New Engl. J. Med., 1980, 15, 1126–1128.
- Burks, A.W., Williams, L.W., Thresher, W., Cannaughton, C., Cockrell, G. and Helm, R.M. Allergenicity of peanut and soyabean extracts altered by chemical or thermal denaturation in patients with atopic dermatitis and positive challenges. J. Allergy Clin. Immunol., 1992, 90, 889-897.
- Gu, X., Beardslee, T., Zeece, M., Sarath, G. and Markwell, J. Identification of IgE-binding proteins in soy lecithin. Int. Arch. Allergy Immunol., 2001, 126, 218–225.
- Porras, O., Carlsson, B., Fallstrom, S.P. and Hanson, L.A. Detection of soy protein in soy lecithin, margarine and occaisionally, soy oil. Int. Arch. Aller. Appl. Immunol., 1985, 78, 30–32.
- Renaud, C., Cardiet, C. and Dupont, C. Allergy to soy lecithin in a child. J. Pediat. Gastroenterol. Nutr., 1996, 22, 328–329.
- Palm, M., Moneret-Vautrin, D.A., Kanny, G., Denery-Papini, S. and Fremont, S. Food allergy to egg and soy lecithins. Allergy. 1999, 54, 1116–1117.
- Paschke, A., Zunker, K., Wigotzki, M. and Steinhart, H. Determination of the IgE-binding activity of soy lecithin and refined and non-refined soybean oils. J. Chromatogr. B. Biomed. Sci. Appl., 2001, 756, 249–254.
- Awazuhara, H., Kawai, H., Baba, M., Matsui, T. and Komiyama, A. Antigenicity of the proteins in soy lecithin and soy oil in soybean allergy. Clin. Exp. Allergy, 1998, 28, 1559–1564.
- Errahali, Y., Morisset, M., Moneret-Vautrin, D.A., Kanny, G., Metche, M., Nicolas, J.P. and Fremont, S. Allergen in soy oils. Allergy, 2002, 57, 648–649.
- Shanti, K.N., Martin, B.M., Nagpal, S., Metcalfe, D.D. and Rao, P.V. Identification of tropomyosin as the major shrimp allergen and characterization of its IgE-binding epitopes. J. Immunol., 1993, 151, 5354–5363.
- Lopata, A.L., O’Hehir, R.E. and Lehrer, S.B. Shellfish allergy. Clin. Exp. Allergy, 2010, 40, 850–858.
- Garcia orozco, K.D., Aisspuro Hernandez, E., Yepiz-plascencia, G., Calderon-de-la-barca, A.M. and Sotelo-Mundo, R.R. Molecular characterization of arginine kinase, an allergen from the shrimp Liptopenaeus vannemei. Int. Arch. Allergy Immunol., 2007, 144, 23–28.
- Hoffman, D.R., Day, E.D. Jr and Miller, J.S. The major heat stable allergen of shrimp. Ann. Allergy, 1981, 47, 17–22.
- Daul, C.B., Morgan, J.E., Hughes, J. and Lehrer, S.B. Provocation-challenge studies in shrimp-sensitive individuals. J. Allergy Clin. Immunol., 1988, 81, 1180–1186.
- Leung, P.S., Chow, W.K., Duffey, S., Kwan, H.S., Gershwin, M.E. and Chu, K.H. 1996. IgE reactivity against a cross reactive allergen in crustacea and mollusca: evidence for tropomyosin as the common allergen. J. Allergy Clin. Iimmunol., 1996, 98, 954–961.
- Reese, G., Ayuso, R. and Lehrer, S.B. Tropomyosin: an invertebrate panallergen. Int. Arch. Allergy Immunol., 1999, 119, 247–258.
- Pascual, C.Y., Crespo, J.F., San Martín, S., Ornia, N., Ortega, N., Caballero, T., MuñozPereira, M. and Martín-Esteban, M. Crossreactivity between IgE-binding proteins from Anisakis, German cockroach and chironomids. Allergy, 1997, 52, 514–520.
- Carrillo, T., Castillo, R., Caminero, J., Cuevas, M., Rodríguez, J.C., Acosta, O. and Rodríguez de Castro, F. Squid hypersensitivity: a clinical and immunologic study. Ann. Allergy, 1992, 68, 483–487.
- Battais, F., Pineau, F., Popineau, Y., Aparicio, C., Kanny, G., Guerin, L., Moneret, V. and Denery, P. Clin. Exp. Allergy, 2003, 33, 962–970.
- Moneret-Vautrin, D.A. and Kanny, G. Update on threshold doses of food allergens: implications for patients and the food industry. Curr. Opin. Allergy Clin. Immunol., 2004, 4, 215–219.
- Simonato, B., Pasini, G., Giannattasio, M., Peruffo, A., DeLazzari, F. and Curioni, A. Food allergy to wheat products: the effect of bread baking and in vitro digestion on wheat allergenic proteins. A study with bread dough, crumb, and crust. J. Agric. Fd. Chem., 2001, 49, 5668–5673.
- Pomes, A., Helm, R.M., Bannom, G.A., Burks, A.W.A., Tsay, A. and Chapman, M.D. Monitoring peanut allergy in food products by measuring Ara h 1. J. Allergy Clin. Immunol., 2003, 111, 640–645.
- Dodo, H.W., Viquez, O.M., Maleki, S.J. and Konan, K.N. cDNA clone of a putative peanut (Arachis hypogaea L.) trypsin inhibitor has homology with peanut allergens Ara h 3 and Ara h 4. J. Agr. Fd. Chem., 2004, 52, 1404–1409.
- Mari, A., Scala, E., Palazzo, P., Ridolfi, S., Zennaro, D and Carabella, G.Bioinformatics applied to allergy: allergen databases, from collecting sequence information to data integration. The allergome platform as a model. Cellular Immunology.2006, 44, 97–100.
- Cabanos,C., Urabe, H., Tandanq-Silvas, M.R., Utsumi, S., Mikami., B and Maruyama, N. Crystal structure of the major peanut allergen Ara h 1. Molecular Immunology. 2011, 49, 115–123.
- Maleki, S.J. Food processing: effects on allergenicity. Curr. Opin. Allergy Clin. Immunol., 2004, 4, 241–245.
- Kappelman, S.J., Knal, E.F., Vlooswijik, R.A.A. et al. Peanut allergen Ara h3: isolation from peanuts and biochemical characterization. Allergy. 2003, 58, 1144–1151.
- Jin, T.C., Guo, A.F., Chen, Y.W., Howard, A. and Zhang, Y. Crystal structure of Ara h 3, a major allergen in peanut. Molecu. Immunol., 2009, 46, 1796–1804.
- Suzanne, S.T. and Shridhar, K.S. Tree nut allergens. Int. Arch. Allergy Immunol., 2003, 131, 234–244.
- Ewan, P.W. Clinical study of peanut and nut allergy in 62 consecutive patients: New features and associations. BMJ. 1996, 312, 1074–1078.
- Crespo, J.F. and Rodriguez, J. food allergy in adulthood. 1996. Allergy. 2003, 58, 98–113.
- Kenneth, H.R., Suzzane, S.T. and Shridhar, K.S. Tree nur allergens. Int. Arch. Allergy Immunol., 2003, 131, 234–244.
- Hansen, K.S., Ballmer, W.B.K., Luttkopf, D., Skov, P.S., Wuthrich, B., Bindslev, J.C., Vieths, S. and Poulsen, L.K. Roasted hazelnut: allergrnic activity evaluated by double blind, placebo controlled food challenge. Allergy Copenhagen., 2003, 58, 132–138.
- Schocker, frauk. Luettkopf dirk, scheurer Stephan, Petersen arnd, cistero bahima ann, Enrique Ernesto, san Miguel moncin mar, akkerdaas jaap, van ree Ronald, vieths Stefan, becker wolf meinhard.. Recombinant lipid transfer protein Coe an 8 from hazelnut: a new tool for in vitro diagnosis of potentially severe hazelnut allergy. J. Allergy Clin. Immunol., 2004, 113, 141–147.
- Beyer, K., Grishina, G., Bardina, L., Grishin, A. and Sampson, H.A. Identification of an 11S globulin as a major hazelnut food allergen in hazelnut induced systemic reactions. J. Allergy Clin. Immunol., 2002, 110, 517–523.
- Hansen, K.S., Ballmer, W.B.K., Luttkopf, D., Skov, P.S., Wuthrich, B., Bindslev, J.C., Vieths, S. and Poulsen, L.K. Roasted hazelnut: allergrnic activity evaluated by double blind, placebo controlled food challenge. Allergy Copenhagen., 2003, 58, 132–138.
- Wigotzki, M., Steinhart, H. and Paschke, A. Determination of the allergenicity of various hazelnut products by immunoblotting and enzyme allergosorbent test inhibition. J. Chromatogr. B. Biomed. Sci. Appl., 2001, 756, 239–248.
- Venkatachalam, M., Teuber, S.S., Roux, K.H. and Sathe, S.K. Effects of roasting, blanching, autoclaving, and microwave heating on antigenicity of almond (Prunus dulcis L.) proteins. J. Agric. Fd. Chem., 2002, 50, 3544–3548.
- Ballmer-Weber, B., Besler, M., Hoffmann-Sommergruber, K., Veiths, S. and Wuthrich, B. Allergen data collection: Celery. Internet Sym. Fd. Allergens, 2000, 2, 145–167.
- Vieths, S., Luttkopf, D., Reindl, J., Anliker, B., Wuthrich, B. and Ballmer-Weber, B.K. 105 Allergens in celery and zucchini. Allergy. 2002, 57, 100–105.
- Besler, M., Hefle Sue, L. and Jarolim Jensen, E. Allergen data collection: sesame seed (sesamum indicum). Internet Sym. Fd. Allergens, 2001, 3, 93–102.
- Izumi, H., Sugiyama, M., Matsuda, T. and Nakamura, R. Structural characterization of the 16-kDa allergen, RA17, in rice seeds. Prediction of the secondary structure and identification of intra molecular disulfide bridges. Biosci. Biotechnol. Biochem., 1999, 63, 2059-2063.
- Usui, Y., Nakase, M., Hotta, H., Urisu, A., Aoki, N. and Kitajima, K. et al. A 33-kDa allergen from rice (Oryza sativa L. Japonica). cDNA cloning, expression, and identification as a novel glyoxalase I. J. Biol. Chem., 2001, 276, 11376–11381.
- Kumar, R., Srivastava, P., Kumari, D., Fakhr, H., Sridhara, S. and Arora, N. et al. Rice (Oryza sativa) allergy in rhinitis and asthma patients: a clinico-immunological study. Immunobiol., 2007, 212, 141–147.
- Arai, T., Takaya, T., Ito, Y., Hayakawa, K., Toshima, S and Shibuya, C. et al. Bronchial asthma induced by rice. Intern. Med., 1998, 37, 98–101.
- Radauer, C. and Breiteneder, H. Evolutionary biology of plant food allergens. J. Allergy Clin. Immunol., 2007, 120, 518–25.
- Asero, R., Amato, S., Alfieri, B., Folloni, S. and Mistrello, G. Rice: another potential cause of food allergy in patients sensitized to lipid transfer protein. Int. Arch. Allergy Immunol., 2007, 143, 69–74.
- Cheng, H.C., Cheng, P.T., Peng, P., Lyu, P.C. and Sun, Y.J. Lipid binding in rice nonspecific lipid transfer protein-1 complexes from Oryza sativa. Protein Sci., 2004, 13, 2304–2315.
- Pastorello, E.A., Farioli, L., Pravettoni, V., Ispano, M., Scibola, E. and Trambaioli, C. The maize major allergen, which is responsible for food-induced allergic reactions, is a lipid transfer protein. J. Allergy Clin. Immunol., 2000, 106, 744–751.
- Watanabe, M., Miyakawa, J., Ikezawa, Z., Suzuki, Y., Hirao, T., Yoshizawa, T. and Arai, S. Production of hypoallergenic rice by enzymatic decomposition of constituent proteins. J. Fd. Sci., 1990, 55, 781–783.
- Brenna, O.V., Pompei, C., Pravettoni, V., Farioli, L. and Pastorello, E.A. Production of Hypoallergenic foods from apricots. J. Fd. Sci. 2005, 70, 38–41.
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Authors
Affiliations
1 Department of Foods and Nutrition, College of Home Science, Govind Ballabh Pant University of Agriculture and Technology, Pantnagar-263145, U.S. Nagar, Uttarakhand, IN
2 Department of Entomology, College of Agriculture, Govind Ballabh Pant University of Agriculture and Technology, Pantnagar-263145, U.S. Nagar, Uttarakhand, IN
1 Department of Foods and Nutrition, College of Home Science, Govind Ballabh Pant University of Agriculture and Technology, Pantnagar-263145, U.S. Nagar, Uttarakhand, IN
2 Department of Entomology, College of Agriculture, Govind Ballabh Pant University of Agriculture and Technology, Pantnagar-263145, U.S. Nagar, Uttarakhand, IN
Source
The Indian Journal of Nutrition and Dietetics, Vol 55, No 2 (2018), Pagination: 142-155Abstract
The present study was undertaken to determine the proximate composition, vitamins, minerals, in vitro protein digestibility, in vitro iron bioavailability, antinutritional factors viz. oxalates, phytates, tannins and antioxidant activity viz. DPPH activity in leaves of six genotypes of mulberry. The results revealed that in fresh mulberry leaves, the proximate values ranged from 70.74 to 77.85% for moisture,1.82 to 2.47% for total ash, 6.32 to 8.44% for crude protein, 0.68 to 0.93% for crude fat, 1.94 to 2.88% for crude fibre, 11.15 to 15.55% for total carbohydrates and 77 to 101 Kcal/100 g for physiological energy. In dried mulberry leaves powder, moisture ranged from 5.68 to 7.36%, total ash 7.56 to 8.47%, crude protein 24.03 to 29.83%, crude fat 2.92 to 3.42%, crude fibre 8.76 to 10.90%, total carbohydrates 41.01 to 47.91% and physiological energy 310 to 324 Kcal/100 g. The vitamins ascorbic acid and beta carotene were found to range from 241.73 to 324.36 mg/100 g and 7.73 to 11.55 mg/100 g, respectively in fresh mulberry leaves and 106.04 to 163.90 mg/100 g and 18.06 to 40.31 mg/100 g, respectively in dried mulberry leaves powder. Among minerals, calcium and iron range from 192.11 to 425.23 mg/100 g and 2.95 to 5.44 mg/ 100 g, respectively for fresh mulberry leaves and 852 to 1806.67 mg/100 g and 13.34 to 19.06 mg/100 g, respectively for dried mulberry leaves powder. Among antinutrients oxalates, tannins and phytates ranged from 59.44 to 113.05 mg/100 g, 0.48 to 0.70mg/100 g and 0.20 to 1.05mg/100 g, respectively for fresh mulberry leaves and 254.40 to 386.40 mg/100 g, 1.82 to 2.65 mg/100 g and 0.9 to 3.70 mg/100 g respectively for dried mulberry leaves powder. In vitro protein digestibility and in vitro iron bioavailability ranged from 79.53 to 83.45% and 1.34 to 1.78% respectively for fresh mulberry leaves powder and 76.16 to 77.80% and 1.15 to 1.57%, respectively for dried mulberry leaves powder. The DPPH activity of fresh mulberry leaves ranged from 27.52 to 45.53% whereas in dried mulberry leaves powder it ranged from 30.41 to 50.7%.Keywords
Mulberry, Nutritional Quality, Antioxidant Activity, Proximate Composition, Anti Nutrients.References
- Anchez, M.D. Mulberry: an exceptional forages available almost worldwide. World Animal Rev., 2000, 93, 1-21.
- Dillard, C.J. and Bruce, J. Phytochemicals: Nutraceuticals and human health. J. Fd. Sci. Agr., 2000, 80, 1744-1756.
- Srivastava, S., Kapoor, R. and Srivastava, R.P. Delicious delicacies from nutritious mulberry. Ind. Silk. 1997, 36 (1), 39-40.
- Srivastava, S., Arya, C., Chaturvedu, R. and Srivastava, R.P. Mulberry leaf based soups: Nutritional aspect. Ind. Silk, 2009, 10-11.
- Rajkumari and Srivastava, S. Nutritional quality components of dried mulberry leaves from different genotypes. Asian Man, 2008, 2 (1), 89-98.
- Chang, L.W., Juang, L.J., Wang, B.S., Wang, M.Y., Ta, H.M., Hung, W.J., Chen, Y.J. and Huang, M.H. Antioxidant and anti tyrosinase activity of mulberry (Morus alba L.) twigs and ischolar_main bark. Fd. Chem. Toxicol., 2011, 49, 785-790.
- Soni, S., Sahu, R.K., Dewgan, S., Soni, Y. and Katre, S. Medicinal value of (Morus alba) mulberry plant. Int. Res. J., 2009, 2 (5), 449-450.
- Doi, K., Kojima, T. and Fujimoto, Y. Mulberry leaf extract inhibits the oxidative modification of rabbit and human low density lipoproteins. Biol. Pharm. Bull., 2000, 23 (9), 1066-1071.
- Che, O.K., Kim, D.O., Moon, H.Y., Kang, H.G. and Lee, C.Y. Contribution of individual polyphenolics to total antioxidant capacity of plums. J. Agr. Fd. Chem., 2003, 51, 7240-7245.
- Katsube, T., Imawaka, N., Kawano, Y., Yamazaki, Y., Shiwaku, K. and Yamane, Y. Antioxidant flavanol glycosides in mulberry (Morus alba L.) leaves isolated based on LDL antioxidant activity. Fd. Chem., 2006, 97, 25-31.
- Kim, Y.C., Kim, M., Takaya, Y., Niwa, M. and Chung, S. Phenolic antioxidants isolated from Mulberry leaves. J. Fd. Sc. Biol., 2007, 16, 854-857.
- Srivastava, S., Kapoor, R., Thathola, A. and Srivastava, R.P. Nutritional quality of leaves of some genotype of mulberry. Int. J. Fd. Sc. Nutr., 2006, 57 (5), 305-313.
- AOAC, Official Methods of Analysis of the Association of Official Analytical Chemist. Washington D.C: Association of Official Analytical Chemists, 1995.
- AOAC, Official Methods of Analysis of the Association of Official Analytical Chemist. Washington D.C: Association of Official Analytical Chemists, 1984.
- Ranganna, S. Handbook of Analysis and Quality Control for Fruit and Vegetable Products, 2nd Edn. New Delhi. 1986, 479-485.
- Akeson, W.A. and Stahman, M.A. A pepsin pancreatin digest index of protein quality evaluation. J. Nutr., 1964, 83, 257-261.
- Rao, B.S.N. and Prabhavati, T. An in vitro method for predicting the bioavailability of iron from foods. Am. J. Clin. Nutr., 1978, 31, 169-175.
- Baker, C.J.L. The determination of oxalate in fresh plant material. The Analyst, 1952, 77, 340-344.
- Wheeler, E.I. and Ferrel, R.E. A method for phytic acid determination in wheat and wheat fraction. Cereal Chem., 1971, 48, 317.
- AOAC, Ed. W Hornitz. Official Methods of Analysis of the Association of Official Analytical Chemist. Washington D.C: Association of Official Analytical Chemists,1970.
- Williams, B., Cuvelier, M.E. and Berset, C. Use of free radical method to evaluate antioxidant activity to evaluate antioxidant activity. Leb.-Wiss. U. Technol., 1995, 28 (1), 25-30.
- Snedecor, G.W. and Cochran, W.G. Statistical methods. Calcutta: Oxford and IBH Publishing, 1967.
- Gopalan, C., RamaSastri, B.V. and Balasubramanian, S.C. Nutritive Value of Indian Foods. National Institute of Nutrition. ICMR, 1989.
- Thakkar, P.S. and Jadhav, R. Biodiversity threat through exotic species monitoring and management using remotely sensed data and GIS techniques- A case study of Banni (Kachchh), Gujrat, India. http:wwws.gisdevelopment.net/application/environment 2007./overview/mi03/91 pt.htm.
- Rajkumari, Srivastava, S. and Srivastava, R.P. Nutritional evaluation of fresh leaves of mulberry genotypes. Agric. Sci. Digest., 2009, 29 (3), 198-201.
- Rafigue, S.M. and Bajjwa, B.A. Effects of different mulberry cultivation forms on economic characters of silkworm, Bombyx mori L. Pak. J. Forest., 2003, 53 (2), 117-126.
- Sesikeran, B. The changing scenario of micronutrient deficiencies in India. NFI Bull., 2013, 34 (2), 1-4.
- Gupta, B.K. and Gupta, Y.K. Amino acids and synthesis of silk. Ind. Silk, 1998, 37 (1), 14.
- Nair, M.K. and Iyengar, V.N. Iron content, bioavailability and factors affecting iron status of Indians. Ind. J. Med. Res., 2009, 130, 634-645.
- Rajkumari, Srivastava, S., Srivastava, R.P. et al. Preliminary studies on feeding deterrents in leaves of ten mulberry genotypes. Ind. J. Sericult., 2012, 51 (2), 177-179.
- Klein, B.P. Processing effects on the dietary antioxidants from plant foods. Horticult. Sci., 2000, 35 (2), 580-584.
- Andallu, B. and Varadacharyulu, N.C. Antioxidant role of mulberry (Morus indica L. cv. Anantha) in streptozotocin diabetic rats. Clin. Chim. Acta., 2003, 338, 3-10.
- Sharma, R., Sharma, A., Shona, T., Takasugi, M., Shirata, A., Fujimura, T., Machii, H. et al. Mulberry (Morus alba) maracins: Scavangers of UV stress- generated free radicals. J. Biosci. Biotechnol. Biochem., 2001, 65 (6), 1402-1405.
- Doi, K., Kojima, T., Harada, M., Hariguchi, Y., Fujimoto, Y. et al. Effect of various fractions extracted from mulberry leaves on lipid metabolism in rabbits fed a cholesterol diet. J. Jpn. Soc. Nutr. Fd. Sci., 1999, 52 (2), 85-90.
- Kojima, Y., Tonegowa, E., Taniguchi, E., Narasaki, R., Husuni, K. et al. Retardation of the development of diabetes mellitus in a murine model of type 1 diabetes fed Morus alba leaves. J. Jpn. Soc. Nutr. Fd. Sci., 2001, 54 (4), 361-364.
- Naowaratwattana, W., De-Eknamkul, D., De, Mejia., E.G. et al. Phenolic containing organic extracts of mulberry (Morus alba L.) leaves inhibit HepG2 hepatoma cells through G2/M phase arrest, induction of apoptosis and inhibition of topoisomerase II a activity. J. Med. Fd., 2010 13 (5), 1045-1056.
- Physical Growth and Nutritional Status Assessment of School Going Children Residing in Western and Eastern Uttar Pradesh, India
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Authors
Rita Singh Raghuvanshi
1,
Rashmi Singh
2,
Dashrath Bhati
1,
Raushan Khan
1,
Chetna Jantwal
1,
Pragati Shukla
2
Affiliations
1 Department of Foods and Nutrition, College of Home Science, G. B. Pant University of Agriculture and Technology, Pantnagar - 263 153, IN
2 Department of Foods and Nutrition, College of Home Science, CSA University of Agriculture and Technology, Kanpur - 208 002, IN
1 Department of Foods and Nutrition, College of Home Science, G. B. Pant University of Agriculture and Technology, Pantnagar - 263 153, IN
2 Department of Foods and Nutrition, College of Home Science, CSA University of Agriculture and Technology, Kanpur - 208 002, IN
Source
The Indian Journal of Nutrition and Dietetics, Vol 57, No 4 (2020), Pagination: 486-497Abstract
Uttar Pradesh is the largest state of India in population and fourth largest state in terms of area. On the basis of its large size, diverse geography, climate and topography, the state has been divided into 4 regions, namely Western, Central, Eastern and Bundelkhand. Present study was conducted with an objective to assess physical growth and nutritional status of school going children age 6-14 years, residing in western and eastern Uttar Pradesh (UP), India. Survey was conducted at Bulandshahr district in western region and Chandauli district in eastern UP. The multistage stratified random sampling was used for identification of schools. Data was collected from 38 schools (Western Uttar Pradesh 20 schools and Eastern Uttar Pradesh 18 schools). Selected children in Western Uttar Pradesh (WUP) were 413 (Male 186 and Female 227) and in Eastern Uttar Pradesh (EUP) total children were 340 (Male 167 and Female 173). The clinical signs and symptoms examination was carried out for prevalence of macro and micro nutrients deficiencies. Anthropometric measurements i.e. body weight, height and mid upper arm circumference were measured. Body Mass Index (BMI) was calculated as weight/ height2 to assess chronic energy deficiency. Physical growth of children was assessed by height for age (stunting) and BMI for age (under and over weight) by using z score suggested by WHO. Physical growth of the children was compared with WHO growth standards. Present study revealed that the overall mean height of children from both the regions were lower than the WHO standards however, height and weight measurements exhibit uniform increase with age in both the sexes. Prevalence of sever stunting was higher among boys and girls of WUP in comparison with EUP. The clinical signs and symptoms of protein deficiency were noticed tripe among girls than boys in both WUP and EUP. This indicates that overall girls were not receiving adequate protein in the diet. However symptoms of vitamin A and B complex deficiency were higher in boys of both the regions.Keywords
Clinical Signs, Malnutrition, Anthropometric Measurements, Macro and Micro Nutrients.References
- WHO-SEARO: adolescent nutrition: A review of the situation in selected South-East Asian Countries, New Delhi: WHO. 2006.
- Anurag, S., Syed, E.M. and Payal, M.S. Nutritional status of school-age children-A scenario of urban slums in India. Arch. Pub. Heal., 2012, 70, 8.
- World Health Organization: Research to improve implementation and effectiveness of school health programmes. WHO, Geneva: 1996, 1, 9-15.
- Shivaprakash, N.C. and Joseph, R.B. Nutritional status of rural school-going children (6-12 years) of Mandya District, Karnataka. Int. J Sci. Stud., 2014, 2, 39-43.
- Spear, B.A. Adolescent growth and development. J. Am. Diet. Assoc., 2002,102, 23-29.
- Eveleth, P.D. and Tanner, J.M. Worldwide variation in human growth, 2nd ed. Cambridge: Cambridge University Press; 1990.
- Vasulu, T.S. and Pal, M. Size and shape components of anthropometric differences among the Yanadis. Ann. Hum. Biol., 1989, 16, 449-462.
- Clinical Anthropometry Biochemistry fact sheet, Uttar Pradesh, 2014, Census of India, 2014. (Internet) Available from http://www.censusindia.gov.in/2011census/hh-series/HH2/Uttar%20Pradesh%20CAB%20 Factsheet%202014.pdf [Last accessed June 10, 2017]
- Charan, J. and Biswas, T. How to calculate sample size for different study designs in medical research? Ind. J. Psychol. Med., 2013, 35,121-126.
- Gibson, R.S. Principle of Nutritional assessment. New York. Oxford University Press. 1990, 691p.
- World Health Organization (WHO) Child Growth Standards. Geneva: WHO. 2007.
- Hussain, R. A. and Kahn, P. S. Comparative study of the nutritional and health status among adolescent students (boys and girls) in rural area, Chandragiri, Chittoor district. A.P. IOSR J. Dental. Med. Sci., 2015, 14, 30-37.
- Perween, R. Nutritional profile of school going children (10-12 years) belonging to trans yamuna area of Allahabad, India. Int. J. Curr. Microbiol. App. Sci., 2018, 7, 4728-4736.
- Handa, R., Faizan, A., Kesari, K. and Prasad, R. Assessment of nutritional status of 710 years school going children of Allahabad district: A review. MiddleEast J. Sci. Res., 2008, 3, 109115. https://pdfs.semanticscholar.org/0200/cc52a6f 535106280f7e1aad9cbce35 be3ccb.pdf
- Dey, A.K. and Nath, A.B. Nutritional status of school going children (6-15 years) in a semi-urban area of Cachar district, Assam. J. Evolution Med. Dent. Sci. 2017, 6, 4057-4062, DOI: 10.14260/Jemds/2017/877