Wist u dat overgevoeligheidsreacties een sterk opkomend probleem is in de westerse gemeenschap? Gluten, afkomstig uit granen, is één van de veertien officieel erkende allergenen door de Europese wetgeving. Om deze redenen wordt er actief onderzoek gedaan naar minder gekende graansoorten zoals Eragrostis tef ter vervanging van de frequent gebruikte glutenbevattende graansoorten zoals tarwe. Tijdens dit onderzoek werd een eiwitkarakterisering uitgevoerd op zeven verschillende tef variëteiten. Dit werk bevat tal van nieuwe gegevens die samen een beeld scheppen over de glutenvrije eigenschappen van tef.
1. Wat zijn gluten en wat kunnen ze veroorzaken?
Gluten zijn in de westerse wereld goed gekend omwille van hun negatieve effecten bij gluten-gevoelige personen. We kennen allemaal wel iemand die hier dagdagelijks rekening mee moet houden. Maar wat zijn gluten nu eigenlijk? Gluten zijn eiwitten die voornamelijk aanwezig zijn in veelvuldig gebruikte graansoorten in de voedingsindustrie zoals tarwe, gerst en rogge (Spaenij-Dekking et al., 2005). Graaneiwitten werden door Osborn reeds in 1924 onderverdeel in vier groepen. De twee niet-gluten eiwitten zijn albumine en globuline, terwijl de gluteneiwitten de prolamines en de glutelines omvatten (Zilic et al., 2011 & Singh et al., 2001). Gluteneiwitten zijn echter van het belang voor de fysische eigenschappen van het eindproduct in de bakkerij-industrie. Tijdens de fermentatiestap in de broodbereiding produceert gist koolstofdioxide, dit is een gas dat door het glutennetwerk wordt vastgehouden wat resulteert in een gerezen deeg (The National Academies, 1996). Niet tegenstaande van deze positief functionele eigenschappen van gluten wordt toch actief onderzoek gedaan naar minder gekende graansoorten. Deze granen kunnen omwille van gezondheidsaspecten dienen ter vervanging van de gluten bevattende graansoorten. Gluten kunnen immers drie verschillende ongewenste reacties veroorzaken in het lichaam zoals allergie, intolerantie en coeliakie, een glutengevoelige auto-immuunziekte van de dunne darm (Spaenij-Dekking et al., 2005).
2. Eragrostis tef
Eén van de graansoorten waar een groeiende interesse voor bestaat, is Eragrostis tef (Fig. 1), een graan afkomstig uit Ethiopië. Tef is één van de kleinste graansoorten ter wereld. De massa van één graan is slechts 0,6-0,8% van de massa van tarwe. Omwille van deze redenen, wordt tef gemaald tot volkorenbloem waarbij de buitenste lagen mee vermalen worden (Gebremariam et al., 2014). In Ethiopië wordt tef voornamelijk gebruikt voor de bereiding van injera, een zacht, rond en gefermenteerd brood dat deel uitmaakt van het traditioneel dieet in Ethiopië. De interesse in tef is gegroeid in de afgelopen jaren doordat het hoge gehaltes bevat aan essentiële aminozuren, mineralen en vitaminen, maar voornamelijk omdat tef beschouwd wordt als een glutenvrij graan, hoewel dit nooit officieel met cijfers is bewezen (Zhang et al., 2016).
3. Eiwitkarakterisering van tef
Granen zijn opgebouwd uit vijf hoofdcomponenten, namelijk koolhydraten, eiwitten, vet, vezels en as. In dit werk werd dieper ingegaan op de eiwitten aanwezig in tef. Voor de eiwitkarakterisering van zeven verschillende tef variëteiten werd allereerst het ruw eiwit gehalte in de bloem bepaald. Er werd een gehalte gevonden dat overeenkomstig was met het eiwitgehalte in tarwe wat dus zeer positief was.
Vervolgens werden de vier eiwitfracties gescheiden op basis van de Osborn techniek. Hiervoor werden resultaten bekomen die afnamen in de volgorde van globuline > albumine > prolamine > gluteline (Fig. 2). Uit deze resultaten kon al reeds afgeleid worden dat de niet-gluteneiwitten in grotere hoeveelheden aanwezig zijn in tef dan de gluteneiwitten. Uit de resultaten van tarwe, werd een duidelijk veel hoger gehalte aan gluteneiwitten teruggevonden.
Daarnaast werd ook ‘in vitro’-eiwitverteerbaarheid (IVPD) getest op zowel de bloem als op de injera. Dit was informatie die tot nu toch nog ongekend was voor tef. Door middel van een literatuurstudie konden onze resultaten vergeleken worden met deze van andere graansoorten. Hieruit bleek dat de IVPD van tef hoger was dan van gerst, mais en haver terwijl de IVPD van tarwe en rogge hoger waren dan van tef. Wel bleek dat na bereiding van de bloem tot injera, het gehalte aan IVPD lichtjes positief was toegenomen (Fig. 3).
Zoals eerder vermeld werd nooit eerder het gehalte aan gluten in tef bepaald. Een casestudie in Nederland waarbij bij coeliakiepatiënten na het consumeren van tef, de reacties geëvalueerd werden, is het enige wat tot nu toe gekend is over gluten in tef. In dit werk werd door middel van een sandwich-enzym linked immunosorbent assay (ELISA) het gehalte aan gluten in de tef bloem bepaald. Volgens de Europese commissie mogen voedingsmiddelen als glutenvrij gelabeld worden als het glutengehalte lager is dan 20 mg/kg. Zoals te zien is in figuur 4 liggen de waarden voor alle zeven de tef variëteiten onder deze drempel waardoor tef als glutenvrij kan beschouwd worden.
Tenslotte werd ook via sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) de aanwezigheid van potentieel andere allergische eiwitten aanwezig in tef bepaald. In de literatuur zijn nog geen allergenen officieel gedetecteerd in tef terwijl er voor tarwe 51 officieel gekend zijn. Uit ons onderzoek bleek wel dat ongeveer 42 allergische eiwitten mogelijks kunnen voorkomen in tef. Belangrijk is hierbij te vermelden dat heel wat van deze allergische eiwitten na voedselbereiding waren verdwenen. Hierdoor werden nog slechts 17 allergische eiwitten teruggevonden die mogelijks kunnen voorkomen in injera.
4. Conclusie
Gluten is een vaak gekend probleem in de westerse maatschappij waardoor men actief op zoek is naar nieuwe granen die als glutenvrij kunnen beschouwd worden. Uit ons onderzoek bleek tef een veelbelovende vervangende graansoort. Onderzoek is nog steeds lopende, aangezien het gebruik van glutenvrij graan ook invloed heeft op de fysische eigenschappen van bakkerijproducten zoals brood. Ook de aanwezigheid van andere allergische componenten moet nog verder onderzocht worden, maar uit eerste resultaten blijken ook deze al veelbelovend te zijn.
Bronnen
Gebremariam, M. M., Zarnkow, M., & Becker, T. (2014). Teff (Eragrostis tef) as a raw material for malting, brewing and manufacturing of gluten-free foods and beverages: a review. Journal of Food Science and Technology, 51(11), 2881-2895. doi: 10.1007/s13197-012-0745-5
Zhang, W., Xu, J., Bennetzen, J. L., & Messing, J. (2016). Teff, an orphan cereal in the Chloridoideae, provides insights into the evolution of storage proteins in grasses. Genome Biology and Evolution, 8(6), 1712-1721. doi: 10.1093/gbe/evw117
Zilic, S., Barac, M., Pesic, M., Dodig, D., & Ignjatovic-Micic, D. (2011). Characterization of proteins from grain of different bread and durum wheat genotypes. International journal of molecular sciences, 12, 5878-5894. doi: 10.3390/ijms12095878
Singh, J., Blundell, M., Tanner, G., & Skerritt, J. H. (2001). Albumin and globulin proteins of wheat flour: Immunological and N-terminal sequence characterization. Journal of Cereal Science, 34, 85-103. doi: 10.1006/jcrs.2001.0380
Spaenij-Dekking, L., Kooy-Winkelaar, Y., & Koning, F. (2005). The Ethiopian cereal tef in celiac disease. The New England Journal of Medicine, 353(16), 1748-1749. doi: 10.1056/NEJMc051492
The National Academies. (1996). Eragrostis tef. In: Lost crops of Africa (1st edition, pp. 215-236). (ISBN 978-0-309-04990-0) Downloaded on December 1, 2016. Retrieved from
http://www.nap.edu/catalog/2305.html
Abdel-Aal, E.-S. M., & Hucl, P. (2002). Amino acid composition and in vitro protein digestibility of selected ancient wheats and their end products. Journal of Food Composition and Analysis, 15, 737-747. doi: 10.1006/jfca.2002.1094
Adebowale, A.-R. A., Emmambux, M. N., Beukes, M., & Taylor, J. R. N. (2011). Fractionation and characterization of teff proteins. Journal of Cereal Science, 54, 380-385. doi: 10.1016/j.jcs.2011.08.002
Ahmed, Z. S., Abd El- Moniem, G. M., & Yassen, A. A. E. (1996). Comperative studies on protein fractions and amino acid composition from sorghum and pearl millet. Molecular Nutrition Food Research, 40(6), 305-309. doi: 10.1002/food.19960400603
Allergome: The platform for Allergen Knowledge (2015). Accessed at December 29, 2016. Retrieved
from http://www.allergome.org/script/search_step2.php
Alvarez-Jubete, L., Arendt, E. K., & Gallagher, E. (2010). Nutritive value of pseudocereals and their increasing use as functional gluten-free ingredients. Trends in Food Science & Technology, 21, 106-113. doi: 10.1016/j.tifs.2009.10.014
Aman, P., Hesseman, K., & Tilly, A. (1985). The variation in chemical composition of Swedish barleys. Journal of Cereal Science, 3, 73-77. doi: https://doi.org/10.1016/S0733-5210(85)80035-7
Andini, R., Yoshida, S., & Ohsawa, R. (2013). Variation in protein content and amino acids in the leaves of grain, vegetable and weedy types of amaranths. Agronomy, 3, 391-403. doi:
10.3390/agronomy3020391
Antony, U., & Chandra, T. S. (1998). Antinutrient reduction and enhancement in protein, starch, and mineral availability in fermented flour of finger millet (Eleusine coracana). Journal of Agricultural and Food chemistry, 46, 2578-2582. doi: 10.1021/jf9706639
Aura, A.-M., Harkonen, H., Fabritius, M., & Poutanen, K. (1999). Development of an in vitro enzymic digestion method for removal of starch and protein and assessment of its performance using rye and wheat breads. Journal of Cereal Science, 29, 139-152. doi: 10.1006/jcrs.1998.0229
Ayalew, A., Fehrmann, H., Lepschy, J., Beck, R., & Abate, D. (2006). Natural occurrence of mycotoxins in staple cereals from Ethiopia. Mycopathologia, 162, 57-63. doi: 10.1007/s11046-006-0027-8
Ballabio, C., Uberti, F., Vacca, E., Boggini, G., Redaelli, R., Catassi, C., Lionetti, E., Penas, E., & Restani, P. (2011). Molecular characterization of 36 oat varieties and in vitro assessment of their suitability for coeliacs’ diet. Journal of Cereal Science, 54, 110-115. doi: 10.1016/j.jcs.2011.04.004
Bejosano, F. P., & Corke, H. (1998). Protein quality evaluation of amaranthus wholemeal flours and protein concentrates. Journal of the Science of Food and Agriculture, 76, 100-106. doi: 10.1002/(SICI)1097-0010(199801)76:1<100::AID-JSFA931>3.0.CO;2-
Belay, G., Zemede, A., Assefa, K. Metaferia, G. & Tefera, H. (2009). Seed size effect on grain weight and agronomic performance of tef (Eragrostis tef). African Journal of Agricultural Research, 4(9), 836-839. doi: 10.3389/fpls.2015.00177
Berhe, T. (2009). Recent developments in teff, Ethiopia’s most important cereal and gift to the world. Accessed at September 9, 2016. Retrieved from http://www.slideshare.net/guest49ae4883/0940-recentdevelopments-
in-teff-ethiopias-most-important-cereal-and-gift-to-the-world
Bonafaccia, G., Marocchini, M., & Kreft, I. (2003). Composition and technological properties of the flour and bran from common and tartary buckwheat. Food Chemistry, 80(1), 9-15. doi: 10.1016/S0308-8146(02)00228-5
Breiteneder, H., & Radauer, C. (2004). A classification of plant food allergens. Journal of Allergy and Clinical Immunology, 113(5), 821-830. doi: http://dx.doi.org/10.1016/j.jaci.2004.01.779
Bullerman, L. B., & Bianchini, A. (2007). Stability of mycotoxins during food processing. International Journal of Food Microbiology, 119, 140-146. doi: 10.1016/j.ijfoodmicro.2007.07.035
Cannarozzi, G., Plaza-Wuthrich, S., Esfeld, E., Larti, S., Wilson, Y. S., Girma, D., Castro, E., Chanyalew, S., Blosch, R., Farinelli, L., Lyons, E., Schneider, M., Falquet, L., Kuhlemeier, C., Asssefa,
K., & Tadele, Z. (2014). Genome and transcriptome sequencing identifies breeding targets in the orphan crop tef (Eragrostis tef). BMC Genomics, 15, 581. doi: 10.1186/1471-2164-15-581
Central Statistical Agency. (2015/2016). Report on area and production of major crops. The federal democratic republic of Ethiopia, 1, 1-118. Accessed at February 9, 2017. Retrieved from from http://www.csa.gov.et/
Chowdhury, S., & Punia, D. (2006). Nutrient and antinutrient composition of pearl millet grains as affected by milling and baking. Nahrung, 41(2), 105-107. doi: 10.1002/food.19970410210
Colgrave, M. L., Goswami, H., Blundell, M., Howitt, C. A., & Tanner, G. J. (2014). Using mass spectrometry to detect hydrolysed gluten in beer that is responsible for false negatives by ELISA. Journal of Chromatography A, 1370, 105-114. doi: http://dx.doi.org/10.1016/j.chroma.2014.10.033
Dahlin, K., & Lorenz, K. (1993). Protein digestibility of extruded cereal grains. Food Chemistry, 48, 13-18. doi: 10.1016/0308-8146(93)90214-Z
Dobzhansky, T. (2013). Chemical and molecular foundations. In: Molecular Cell biology (7th edition).
Lodish, H., Kaiser, C. A., Bretscher, A., Amon, A., Berk, A., Krieger, M., Ploegh, H., & Scott, M. P. (Eds.). W. H. Freeman and Company, New York, pp. 1-58. (ISBN 978-0716776017)
Dogra, D., & Awasthi, C. P. (2015). Comparative nutritional evaluation of common buckwheat genotypes with major cereal and pseudocereals crops. Agricultural Science Digest, 35(1), 36-40. doi: 10.5958/0976-0547.2015.00007.5
Duodu, K. G., Nunes, A., Delgadillo, I., Parker, M. L., Mills, E. N. C., Belton, P. S., & Taylor, J. R. N. (2002). Effect of grain structure and cooking on sorghum and maize in vitro protein digestibility. Journal of Cereal Science, 35, 161-174. doi: 10.1006/jcrs.2001.0411
Dykes, L., & Rooney, L. W. (2007). Phenolic compounds in cereal grains and their health benefits. Cereal Foods World, 52(3), 105-111. doi: 10.1094/CFW-52-3-0105
Elsohaimy, S. A., Refaay, T. M., & Zaytoun, M. A. M. (2015). Physicochemical and functional properties of quinoa protein isolate. Annals of Agriccultural Science, 60(2), 297-305. doi:
10.1021/jf703689u
Enyisi, S. I., Umoh, V. J., Whong, C. M. Z., Abdullahi, I. O., & Alabi, O. (2014). Chemical and nutritional value of maize and maize products obtained from selected markets in Kaduna State, Nigeria.
African Journal of Food Science and Technology, 5(4), 100-104. doi: http:/dx.doi.org/10.14303/ajfst.2014.029
European Food Safety Authority. (2014). Scientific Opinion on the evaluation of allergenic foods and food ingredients for labelling purposes. Downloaded on October 16, 2016. Retrieved from https://www.efsa.europa.eu/sites/default/files/consultation/140523.pdf
FAVV. (2016). Een voedselallergie? Lees het etiket of vraag info!. Accessed at August 21, 2016. Retrieved from http://www.favv.be/dagelijksleven/allergieen/leesetiket/
Freeman, P. L., & Palmer, H. (1984). The structure of the pericarp and testa of barley. Journal of the Institute of Brewing, 90(2), 88-94. doi: 10.1002/j.2050-0416.1984.tb04244.x
Friedman, M. (1989). Alternative measurements of amino acid availability in vitro. In: Absorption and utilization of amino acids. Friedman, M. (Eds.). CRC Press, United states, pp. 134-137. (ISBN 9780849360084)
Gänzle, M. G., Loponen, J., & Gobbetti, M. (2008). Proteolysis in sourdough fermentations: mechanisms and potential for improved bread quality. Trends in Food Science & Technology, 19(10), 513-521. doi: 10.1016/j.tifs.2008.04.002
Gebremariam, M. M., Zarnkow, M., & Becker, T. (2014). Teff (Eragrostis tef) as a raw material for malting, brewing and manufacturing of gluten-free foods and beverages: a review. Journal of Food Science and Technology, 51(11), 2881-2895. doi: 10.1007/s13197-012-0745-5
Gellrich, C., Schieberle, P., & Wieser, H. (2003). Biochemical characterization and quantification of the storage protein (secalin) types in rye flour. Cereal Chemistry, 80(1), 102-109. doi: 10.1094/CCHEM.2003.80.1.102
Giuberti, G., Gallo, A., Fiorentini, L., Fortunati, P., & Masoero, F. (2016). In vitro starch digestibility and quality attributes of gluten free ‘tagliatelle’ prepared with teff flour and increasing levels of a new developed bean cultivar. Starch, 68, 374-378. doi: 10.1002/star.201500007
Gobbetti, M., & Ganzle, M. (2013). Chemistry of cereal grains. In: Handbook on sourdough biotechnology. Gobbetti, M., &
Ganzle, M. (Eds.). Springer, New York, pp. 11-45. (ISBN 978-1-4614-5425-0)
Golde, D. W., McGinniss, M. G., & Holland, P. V. (1970). Serum Agglutinins to Commercially Prepared Albumin. American Journal of Clinical Pathology, 55, 655-658. doi:
https://doi.org/10.1093/ajcp/55.6.655
Gujral, N., Freeman, H. J., & Thomson, A. B. R. (2012). Celiac disease: Prevalence, diagnosis, pathogenesis and treatment. World Journal of Gastroenterology, 18(42), 6036-6059. doi:
10.3748/wjg.v18.i42.6036
Guo, X., & Yao, H. (2006). Fractionation and characterization of tartary buckwheat flour proteins. Food Chemistry, 98, 90-94. doi: 10.1016/j.foodchem.2005.05.055
Gupta, R. B., Masci, S., Lafiandra, D., Bariana, H. S., & MacRitchie, F. (1996). Accumulation of protein subunits and their polymers in developing grains of hexaploid wheats. Journal of Experimental Botany, 47(302), 1377-1385. doi: https://doi.org/10.1093/jxb/47.9.1377.
Hampshire County Council. (2016). Allergens. Accessed at August 21, 2016. Retrieved from http://www3.hants.gov.uk/hc3s/hc3s-secondary/allergens.htm
Hanin, M., Brini, F., Ebel, C., Toda, Y., Takeda, S. & Masmoudi, K. (2011). Plant dehydrins and stress tolerance. Plant Signal Behavior, 6(10), 1503-1509. doi: 10.4161/psb.6.10.17088
Hoge gezondheidsraad. (2009). Publicatie van de hoge gezondheidsraad nr. 8513: Voedselallergieën en pseudoallergieën. Downloaded on February 7, 2017. Retrieved from http://www.health.belgium.be/sites/default/files/uploads/fields/fpsheal…
elallergie%C3%ABn%20en%20pseudoallergie%C3%ABn%20(augustus%202009)%20(HGR%20851
3).pdf
Hopman, E., Dekking, L., Blokland, M.-L., Wuisman, M., Zuijderduin, W., Koning, F., & Schweizer, J. (2008). Tef in the diet of celiac patients in The Netherlands. Scandinavian Journal of Gastorenterology, 43, 277-282. doi: 10.1080/00365520701714871
Hsu, H. W., Vavak, D. L., Satterlee, L. D., & Miller, G. A. (1977). A multi-enzyme technique for estimating protein digestibility. Journal of Food Science, 42, 1269-1273. doi: 10.1111/j.1365-
2621.1977.tb14476.x
Huby, R. D. J., Dearman, R. J., & Kimber, I. (2000). Why are some proteins allergens?. Toxicological sciences, 55(2), 235-246. doi: 10.1093/toxsci/55.2.235.
Hurkman, W. J., Vensel, W. H., Tanaka, C. K., Whitehand, L., & Altenbach, S. B. (2009). Effect of high temperature on albumin and globulin accumulation in the endosperm proteome of the developing wheat grain. Journal of Cereal Science, 49, 12-13. doi: 10.1016/j.jcs.2008.06.014
International Organization for Standardization. (1978). ISO 937:1978 Meat and meat products-Determination of nitrogen content (Reference method). Accessed at September 9, 2016. Retrieved from http://www.iso.org/iso/catalogue_detail.htm?csnumber=5356
Janssen, F., Pauly, A., Rombouts, I., Jansens, K. J. A., Deleu, L. J., & Delcour, J. A. (2016). Proteins of amaranth (amaranthus spp.), buckwheat (fagopyrum spp.), and quinoa (chenopodium spp.): A food science and technology perspective. Institute of Food Technologists, 0, 1-20. doi: 10.1111/1541-4337.12240
Kaleab Baye. (2014). Teff: nutrient composition and health benefits. Accessed at March 15, 2017. Retrieved from https://www.researchgate.net/profile/Kaleab_Baye2/publication/266316373…
Kasera, R., Niphadkar, P. V., Saran, A., Mathur, C., & Singh, A. B. (2013). First case report of anaphylaxis caused by Rajgira seed floru (Amaranthus paniculatus) from India: A clinic-immunologic evaluation. Asian Pacific Journal of Allergy and Immunology, 31, 79-83. Downloaded from http://apjaijournal.
org/wp-content/uploads/2016/10/12FirstcasereportVol31No1March20 13P79.pdf
Kieffer, R., Wieser, H., Henderson, M. H., & Graveland, A. (1996). Correlations of the breadmaking performance of wheat flour with rheological measurements on a micro-scale. Journal of Cereal Sciene, 27, 53-60. doi: 10.1006/jcrs.1997.0136
Klose, C., & Arendt, E., (2012). Proteins in oats: their synthesis and changes during germination: a review. Critical Reviews in Food Science and Nutrition, 52(7), 629-639. doi:
10.1080/10408398.2010.504902
Kohajdova, Z., & Karovicova, J. (2007). Fermentation of cereals for specific purpose. Journal of Food and Nutrition Research, 46, 2, 51-57. doi: 10.12691/jfnr-5-1-7
Kumagai, H. (2010). Wheat proteins and peptides. In: Bioactive proteins and peptides as functional foods and nutraceuticals. Y. Mine, E. Li-Chan, & B. Jiang (Eds.). Iowa State University Press, Arnes, pp. 1980-1983. (ISBN 9780813811048)
Kumar, S., Dwivedi, P. D., Das, M., & Tripathi, A. (2013). Macrophages in food allergy: An enigma. Molecular Immunology, 56, 612-618. doi: 10.1016/j.molimm.2013.06.009
Li, Q., & Xu, J.-G. (2015). Changes in nutritive value and in vitro digestibility of proteins form naked oats during germination. European Journal of Food Science and Technology, 3(2), 49-57. Retrieved from http://www.eajournals.org/wp-content/uploads/Changes-in-Nutritive-Value…-
Digestibility-of-Proteins-from-Naked-Oats-during-Germination.pdf
Lim, T. K. (2015). Poaceae. In: Medicinal and non-medicinal plants. Springer, London, pp. 417-418. (ISBN 978-94-017-9511-1)
Lin, Y., Mouratidou, T., Vereecken, C., Kersting, M., Bolca, S., Moraes, A. C., & Huybrechts, I. (2015). Dietary animal and plant protein intakes and their associations with obesity and cardio-metabolic indicators in European adolescents: the HELENA cross-sectional study. Nutrition Journal, 14(10), 1-11. doi: 10.1186/1475-2891-14-10
Mahmood, T., & Yang, P.-C. (2012). Western Blot: Technique, theory, and trouble shooting. North American Journal of Medical Sciences, 4(9), 429-243. doi: 10.4103/1947-2714.100998
Malik, A. H. (2009). Nutrient uptake, transport and translocation in cereals: Influences of environment and farming conditions. Swedish University of Agricultural Sciences, Alnarp, pp. 8-13.
Mariotti, F., Tomé, D., & Mirand, P. P. (2008). Converting nitrogen into protein-beyond 6.25 and jones’ factors. Critical reviews in Food Science and Nutrition, 48, 177-184. doi: 10.1080/10408390701279749
McDonough, C. M., Rooney, L. W., Serna-Saldivar, S. O. (2000). Handbook of cereal science and technology. Millets. In Kulp, K., & Ponte, J. G. (Eds.), Basel, New York, pp. 183. (ISBN
9780824782948)
Mena, M. C., Lombardia, M., Hernando, A., Mendez, E., & Albar, J. P. (2012). Comprehensive analysis of gluten in processed foods using a new extraction method and a competitive ELISA based on the R5 antibody. Talanta, 91, 33-40. doi: 10.1016/j.talanta.2011.12.073
Mengistu, D. K., & Mekonnen, L. S. (2012). Integrated agronomic crop managements to improve tef productivity under terminal drought. Water stress, 235-254. doi: 10.5772/30662
M’Hir, S., Ziadi, M., Chammem, N., & Hamdi, M. (2012). Gluten proteolysis as alternative therapy for celiac patients: a mini-review. African Journal of Biotechnology, 11(29), 7323-7330. doi: 10.5897/AJB11.726
Moreno, F. J., & Clemente, A. (2008). 2S Albumin storage proteins: what makes them food allergens?. The Open Biochemistry Journal, 2, 16-28. doi: 10.2174/1874091X00802010016
Moyano, F. J., Saénz de Rodriganez, M. A., Diaz, M., & Tacon, A. G. J. (2015). Application of in vitro digestibility methods in aquaculture: constraints and perspectives. Reviews in Aquaculture, 7, 223-242. doi: 10.1111/raq.12065
Mulugeta, A. (1978). Floral morphogenesis, temperature effect on growth and devellopment and variation in nutritional composition and distribution among cultivars in Eragrostis tef (Zucc.) Trotter. USA: University of Wisconsin.
Munoz-Huerta, R. F., Guevara-gonzalez, R. G., Contreras-Medina, L. M., Torres-Pacheco, I., Prado-Olivarez, J., & Ocampo-Velazquez, R. V. (2013). A review of methods for sensing the nitrogen status in plants: advantages, disadvantages and recent advances. Sensors, 13, 10823-10843. doi: 10.3390/s130810823
Nambiar, V. S., Dhaduk, J. J., Sareen, N., Shahu, T., & Desai, R. (2011). Potential functional implications of pearl millet (Pennisetum glaucum) in health and disease. Journal of Applied Pharmaceutical Science, 1(10), 62-67. Retrieved from http://www.japsonline.com/admin/php/
uploads/299_pdf.pdf
Nguyen, G. T., Gidley, M. J., & Sopade, P. A. (2015). Dependence of in-vitro starch and protein digestions on particle size of field peas (Pisum sativum L.) LWT- Food Science and Technology, 63, 541-549. doi: 10.1016/j.lwt.2015.03.037
Nilsson, M., & Aman, P. (1997). Content of nutrients and lignans in roller milled fractions of rye. Journal of the Science of Food and Agriculture, 73(2), 143-148. doi: 10.1002/(SICI)1097-
0010(199702)73:2<143::AID-JSFA698>3.0.CO;2-H
Nowakowski, A. B., Wobig, W. J., & Petering, D. H. (2014). Native SDS-PAGE: High resolution electrophoretic separation of proteins with retention of native properties including bound metal ions. Metallomics, 6(5), 1068-1078. doi: 10.1039/c4mt00033a.
Oregon State University. (2004). High-energy feedstuffs. Accessed at September 27, 2016. Retrieved from https://courses.ecampus.oregonstate.edu/ans312/two/cereal.htm
Pastorello, E.A., Farioli, L., Pravettoni, V., Ispano, M., Scibola, E., Trambaioli, C., Giuffrida, M. G., Ansaloni, R., Godovac-Zimmermann, J., Conti, A., Fortunato, D., & Ortolani, C. (2000). The maize major allergen, which is responsible for food-induced allergic reactions, is a lipid transfer protein. The
journal of Allergy and Clinical Immunology, 106(4), 744-751. doi: http://dx.doi.org/10.1067/mai.2000.108712
Penas, E., Uberti, F., Lorenzo, C., Ballabio, C., Brandolini, A., & Restani, P. (2014). Biochemical and immunochemical evidences supporting the inclusion of quinoa (Chenopodium quinoa Willd.) as a gluten-free ingredient. Plant Foods for Human Nutrition, 69, 297-303. doi: 10.1007/s11130-014-0449-2
Petr, J., Michalik, I., Tlaskalova, H., Capouchova, I., Famera, O., Urminska, D., Tuckova, L., & Knblochova, H. (2003). Extention of the sprectra of plant products for the diet in coeliac disease. Czech Journal of Food Science, 21(2), 59-70. Retrieved from http://www.agriculturejournals.cz/publicFiles/50830.pdf
Poms, R. E., Klein, C. L., & Anklam, E. (2004). Methods for allergen analysis in food: a review. Food Additives and Contaminants, 21(1), 1-31. doi: 10.1080/02652030310001620423
Poutanen, K., Flander, L., & Katina, K. (2009). Sourdough and cereal fermentation in a nutritional perspective. Food Microbiology, 26, 693-699. doi: 10.1016/j.fm.2009.07.011
R-Biopharm, AG. (2012). Ridascreen® Gliadin: Enzymimmunoassay for the quantitative analysis of gliadins and corresponding prolamines. Accessed on October 15, 2016. Retrieved from https://www.azmax.co.jp/wp-content/uploads/2015/11/R7001-Gliadin-12-04-…
R-biopharm AG. (2016). Analytical test kits to ensure gluten-free food. Downloaded on September 9, 2016. Retrieved from http://www.r-biopharm.com/wp-content/uploads/1300/Gluten-free-foodbroch….
pdf
Ranhotra, G. S., Gelroth, J. A., Glaser, B. K., Lorenz, K. J., & Johnson, D. L. (1993). Composition and protein nutritional quality of quinoa. American Association of Cereal Chemists, 70(3), 303-305. doi: 10.1007/BF02196067
Rombold, S., Ollert, M., Sbornik, M., Rakoski, J., Darsow, U., & Ring, J. (2008). Immediate-type respiratory allergy to millet-containing seed mixture of bird food. World allergy organization journal, 1(8), 135-137. doi: 10.1097/WOX.0b013e31817833ef
Rossel, C. M., Barro, F., Sousa, C., & Mena, M. C. (2014). Cereals for developing gluten-free products and analytical tools for gluten detection. Journal of Cereal Science, 59, 354-364. doi:
http://dx.doi.org/10.1016/j.jcs.2013.10.001
Rostami, K., Rostami-Nejad, M., & Dulaimi, D. (2015). Post gastroenteritis gluten intolerance. Gastroenterology and Hepatology from bed to bench, 8(1), 66-70. Retrieved from
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4285934/
Roy, A., Bera, S., Patra, S., Ray, S., & Ray, M. (2009). A novel D-glyderaldehyde-3-phosphate binding protein, a truncated albumin, with D-glyceraldehyde-3-phosphate dehydrogenase inhibitory property. IUBMB life, 61(10), 995-1000. doi: 10.1002/iub.238
Sher, M. G., Nadeem, M., Syed, Q., Abass, S., & Hassan, A. (2011). Study on protease from barley tempeh and in vitro protein digestibility. Jordan Journal of Biological Sciences, 4(4), 257-264. Retrieved from http://jjbs.hu.edu.jo/files/v4n4/Paper%20Number%2011.pdf
Shewry, P. R., & Halford, N. G. (2002). Cereal seed storage proteins: structures, properties and role in grain utilization. Journal of Experimental Botany, 53(370), 947-958. doi: 10.1093/jexbot/53.370.947
hewry, P. R., Napier, J. A., & Tatham, A. S. (1995). Seed storage proteins: Structures and biosynthesis. The plant Cell, 7, 945-956. doi: 10.1105/tpc.7.7.945
Shewry, P. R., & Tatham, A. S. (1990). The prolamin storage proteins of cereal seeds: structure and evolution. Biochemical journal, 267, 1-12. doi: 10.1042/bj2670001
Shin, M., Han, Y., & Ahn, K. (2012). The influence of the time and temperature of heat treatment on the allergenicity of egg white proteins. Allergy Asthma Immunologic Response, 5(2), 96-101. doi: 10.4168/aair.2013.5.2.96
Shumoy, H., Lauwens, S., Gabaza, M., Vandevelde, J., Vanhaecke, F., & Raes, K. (2017). Traditional fermentation of tef: Impact on in vitro iron and zinc dialysability. Submitted to journal agricultural and food chemistry.
Shutov, A. D., Bäumlein, H., Blattner, F. R., & Müntz, K. (2003). Storage and mobilization as antagonistic functional constraints on seed storage globulin evolution. Journal of Experimental Botany, 54(388), 1645-1654. doi: https://doi.org/10.1093/jxb/erg165
Sigma-Aldrich. (2017a). Trypsin from porcine pancreas. Accessed at November 26, 2016. Retrieved
from http://www.sigmaaldrich.com/catalog/substance/trypsinfromporcinepancrea…
Sigma-Aldrich. (2017b). α-Chymotrypsin from bovine pancreas. Accessed at November 26, 2016. Retrieved from http://www.sigmaaldrich.com/catalog/product/sigma/c4129?lang=en®ion=…
Sigma-Aldrich. (2017c). Protease from Streptmyces griseus. Accessed at November 26, 2016. Retrieved from http://www.sigmaaldrich.com/catalog/substance/proteasefromstreptomycesg…
Singh, J., Blundell, M., Tanner, G., & Skerritt, J. H. (2001). Albumin and globulin proteins of wheat flour: Immunological and N-terminal sequence characterization. Journal of Cereal Science, 34, 85-103. doi: 10.1006/jcrs.2001.0380
Sivam, A. S., Sun-Waterhouse, D., Quek, S. Y., & Perera, C. O. (2010). Properties of bread dough with added fibre polysaccharides and phenolic antioxidants: A review. Journal of Food Science, 75(8), 163-174. doi: 10.1111/j.1750-3841.2010.01815.x
Spaenij-Dekking, L., Kooy-Winkelaar, Y., & Koning, F. (2005). The Ethiopian cereal tef in celiac disease. The New England Journal of Medicine, 353(16), 1748-1749. doi: 10.1056/NEJMc051492
Sharma, G. M., Khuda, S. E., Parker, C. H., Eischeid, A. C., & Pereira, M. (2017). Detection of allergen markers in food: Analytical methods. In: Food Safety: Innovative analytical tools for safety assessment.
Spizzirri, U. G., & Cirillo, G. (Eds.). Scrivener Publishing: United States, pp. 65-69. (ISBN 978-1-119-
16055-7)
Sramkova, Z., Gregova, E., & Sturdik, E. (2009). Chemical composition and nutritional quality of wheat grain. Acta Chimica Slovaca, 2(1), 115-138. Retrieved from http://www.acs.chtf.stuba.sk/papers/acs_0041.pdf
Srivastava, R., & Roy, B. K. (2011). Effect of varying pH on protein composition and yield of amaranth seed (Amaranthus blitum). Journal of Environ Biology, 32(5), 629-634. Retrieved from https://www.ncbi.nlm.nih.gov/pubmed/22319880
Steinman, H. (2012). ThermoScientific. Accessed on October 16, 2016. Retrieved from http://www.phadia.com/sv/Products/Produkter/ImmunoCAP-Allergens/Food-of…
Takumi, K., Udaka, J., Kimoto, M., Koga, T., & Tsuji, H. (2000). Structural and immunochemical homologies between foxtail millet glutelin 60 kDa and starch granule-bound starch synthase proteins from rice barley, corn and wheat grains. Journal of Nutritional Science and Vitaminology, 46(2), 109-
112. Retrieved from https://www.ncbi.nlm.nih.gov/pubmed/10885800
Tatham, A. S., Fido, R. J., Moore, C. M., Kasarda, D. D., Kuzmicky, D. D., Keen, J. N., & Shewry, P.R. (1996). Characterisation of the major prolamins of tef (Eragrostis tef) and finger millet (Eleusine Coracana). Journal of Cereal Science, 24, 65-71. doi: 0733–5210/96/040065
Tatham, A. S., & Shewry, P. R. (2008). Allergens in wheat and related cereals. Clinical and Experimental Allergy, 38, 1712-1726. doi: 10.1111/j.1365-2222.2008.03101.x
The European Commission. (2009). Commission regulation (EC) No 41/2009: Concerning the composition and labelling of foodstuffs suitable for people intolerant to gluten. Official Journal of the European Union, 41(16), 3-5. Retrieved from http://eur-lex.europa.eu/LexUriServ/LexUriServ.
do?uri=OJ:L:2009:016:0003:0005:EN:PDF
The National Academies. (1996). Eragrostis tef. In: Lost crops of Africa (1st edition, pp. 215-236). (ISBN 978-0-309-04990-0) Downloaded on December 1, 2016. Retrieved from
http://www.nap.edu/catalog/2305.html
Tinus, T., Damour, M., Riel, V., & Sopade, P.A. (2012). Particle size-starch-protein digestibility relationships in cowpea (Vigna unguiculata). Journal of Food Engineering, 113, 254-264. doi:
10.1016/j.jfoodeng.2012.05.041
Ustunol, Z., (2015). Applied food protein chemistry (1st edition). Wiley Blackwell, Michigan, pp. 5-21. (ISBN 978-1-119-94449-2)
Vadivoo, A. S., Joseph, R., & Ganesan, N. M. (1998). Genetic variability and diversity for protein and calcium contents in finger millet (Eleusine coracana (L.) Gaertn) in relation to grain color. Plant Foods for Human Nutrition, 52, 353-364. doi: 10.1023/A:1008074002390
Verhoeckx, K. C. M., Vissers, Y. M., Baumert, J. L., Faludi, R., Feys, M., Flanagan, S., Herouet-Guicheney, C., Holzhauser, T., Shimojo, R., Bolt, N., Wichers, H., & Kimber, I. (2015). Food processing and allergenicity. Food and Chemical Toxicology, 80, 223-240. doi: 10.1016/j.fct.2015.03.005
Wallner, M., & Hofer, H. (2015). Adverse reactions triggered by amaranth allergens-what we know so far from a molecular perspective. Journal of Allergy & Therapy, 6, 108. doi: 10.4172/2155-6121.1000e108
Wampler, J. E. (2010). The 20 amino acids and their role in protein structures. Accessed on March 15, 2017. Retrieved from http://www.proteinstructures.com/Structure/Structure/amino-acids.html
WHO/IUIS Allergen Nomenclature Sub-Committee. (n.d.). Allergen nomenclature. Accessed on October 15, 2016. Retrieved from http://www.allergen.org/index.php