Yerfıstığı Alerjisi ve İlgili Proteinler

Yıl 2025, Cilt: 8 Sayı: 1, 18 - 33, 31.12.2025

Deniz Sevilmiş , Yaşar Ahu Ağan

Öz

Morfolojik olarak değişken olmasına rağmen kültürü yapılan yerfıstıklarının genetik tabanı çok dardır. Dünya çapında 300'den fazla ticari çeşidi yetiştirilmektedir. Yerfıstığı, besleyiciliği, tadı ve uygun fiyatı nedeniyle dünya çapında en çok tüketilen baklagillerden biridir. Yerfıstığı protein ve enerji açısından zengindir. Yerfıstığı çiğ, haşlanmış veya kavrulmuş olarak yenebilir ve çeşitli paketlenmiş gıdaların (fıstık ezmesi, şekerlemeler, şekerlemeler ve atıştırmalık ürünler) hazırlanmasında yaygın olarak ve gelişmekte olan ülkelerde protein genişletici olarak kullanılmaktadır. Günümüzde ek olarak, lezzetini değiştirmeden hayvan sütünü sulandırıcı olarak yerfıstığı sütü veya yerfıstığı proteini izolatlarının kullanılmasına, daha çekici fermente ürünler geliştirmeye ve “tofu” adı verilen bir lor elde etmek ve peynir analogları üretmek için sütten proteinleri çökeltmeyi de kapsar şekilde bir yönelim söz konusudur.
Geçmiş yıllarda yerfıstığı yüksek yağ içeriği nedeniyle sağlıksız bir gıda olarak algılanıyordu ancak mevcut araştırma çalışmaları, yerfıstığının diyete dahil edilmesinin kalp hastalıklarının azalmasıyla ve kilo yönetiminin iyileştirilmesiyle bağlantılı olduğunu göstermiştir. Ancak aflatoksin ve alerjenler yerfıstığında sağlık açısından önemli caydırıcı faktörlerdir ve aflatoksin ve alerjen içermeyen yerfıstığı geliştirmek için daha fazla araştırma çabasına ihtiyaç vardır.

Anahtar Kelimeler

Yerfıstığı , Arachis hypogaea , alerji , protein , alerjen

Kaynakça

• Chang, A. S., Sreedharan, A., & Schneider, K. R. (2013). Peanut and peanut products: A food safety perspective. Food Control, 32(1): 296-303.
• Chen, X., Wang, Q., El-Mezayen, R., Zhuang, Y., & Dreskin, S. C. (2013). Ara h 2 and Ara h 6 have similar allergenic activity and are substantially redundant. International archives of allergy and immunology, 160(3): 251-258.
• Chukwumah, Y., Walker, L. T., & Verghese, M. (2009). Peanut skin color: a biomarker for total polyphenolic content and antioxidative capacities of peanut cultivars. International Journal of Molecular Sciences, 10(11): 4941-4952.
• Di Stasio, L., Picariello, G., Mongiello, M., Nocerino, R., Canani, R. B., Bavaro, S., Monaci, L., Ferranti, P., & Mamone, G. (2017). Peanut digestome: Identification of digestion resistant IgE‑binding peptides. Food and Chemical Toxicology, 107: 88–98. https://doi.org/10.1016/j.fct.2017.06.029
• Diarra, K., Nong, Z. G., & Jie, C. (2005). Peanut milk and peanut milk based products production: a review. Critical reviews in food science and nutrition, 45(5): 405-423.
• Du Toit, G., Roberts, G., Sayre, P. H., Bahnson, H. T., Radulovic, S., Santos, A. F., ... & Lack, G. (2015). Randomized trial of peanut consumption in infants at risk for peanut allergy. New England Journal of Medicine, 372(9): 803-813.
• Du Toit, G., Sayre, P. H., Roberts, G., Sever, M. L., Lawson, K., Bahnson, H. T., ... & Lack, G. (2016). Effect of avoidance on peanut allergy after early peanut consumption. New England Journal of Medicine, 374(15): 1435-1443.
• Dunwell, J. M., Purvis, A., & Khuri, S. (2004). Cupins: the most functionally diverse protein superfamily?. Phytochemistry, 65(1): 7-17.
• Hathorn, C. S., & Sanders, T. H. (2012). Flavor and antioxidant capacity of peanut paste and peanut butter supplemented with peanut skins. Journal of Food Science, 77(11): S407-S411.
• Jolivet, P., Acevedo, F., Boulard, C., d'Andréa, S., Faure, J. D., Kohli, A., & Chardot, T. (2013). Crop seed oil bodies: from challenges in protein identification to an emerging picture of the oil body proteome. Proteomics, 13(12-13): 1836-1849.
• Jones, J. B., Provost, M., Keaver, L., Breen, C., Ludy, M. J., & Mattes, R. D. (2014). A randomized trial on the effects of flavorings on the health benefits of daily peanut consumption. The American journal of clinical nutrition, 99(3): 490-496.
• Koppelman, S. J., Knol, E. F., Vlooswijk, R. A. A., Wensing, M., Knulst, A. C., Hefle, S. L., & Piersma, S. (2003). Peanut allergen Ara h 3: isolation from peanuts and biochemical characterization. Allergy, 58(11): 1144-1151.
• Koppelman, S. J., Wensing, M., Ertmann, M., Knulst, A. C., & Knol, E. F. (2004). Relevance of Ara h1, Ara h2 and Ara h3 in peanut‐allergic patients, as determined by immunoglobulin E Western blotting, basophil–histamine release and intracutaneous testing: Ara h2 is the most important peanut allergen. Clinical & Experimental Allergy, 34(4): 583-590.
• Lauer, M. K., Sanders, Z. E., Smith, A. D., & Smith, R. C. (2021). Morphological and mechanical characterization of high-strength sulfur composites prepared with variably-sized lignocellulose particles. Materials Advances, 2(22): 7413-7422.
• Lehmann, K., Schweimer, K., Reese, G., Randow, S., Suhr, M., Becker, W. M., & Rösch, P. (2006). Structure and stability of 2S albumin-type peanut allergens: implications for the severity of peanut allergic reactions. Biochemical Journal, 395(3): 463-472.
• Lieberman, J. A., Gupta, R. S., Knibb, R. C., Haselkorn, T., Tilles, S., Mack, D. P., & Pouessel, G. (2021). The global burden of illness of peanut allergy: A comprehensive literature review. Allergy, 76(5): 1367–1384. Liu, F., Zhang, X., Lu, C., Zeng, X., Li, Y., Fu, D., & Wu, G. (2015). Non-specific lipid transfer proteins in plants: presenting new advances and an integrated functional analysis. Journal of experimental botany, 66(19): 5663-5681.
• Maleki, S. J., Viquez, O., Jacks, T., Dodo, H., Champagne, E. T., Chung, S. Y., & Landry, S. J. (2003). The major peanut allergen, Ara h 2, functions as a trypsin inhibitor, and roasting enhances this function. Journal of Allergy and Clinical Immunology, 112(1): 190-195. Mari, A., Scala, E., Palazzo, P., Ridolfi, S., Zennaro, D., & Carabella, G. (2006). Bioinformatics applied to allergy: allergen databases, from collecting sequence information to data integration. The Allergome platform as a model. Cellular immunology, 244(2): 97-100. McCurdy, D. W., Kovar, D. R., & Staiger, C. J. (2001). Actin and actin-binding proteins in higher plants. Protoplasma, 215: 89-104. Moreno, J. P., Johnston, C. A., El-Mubasher, A. A., Papaioannou, M. A., Tyler, C., Gee, M., & Foreyt, J. P. (2013). Peanut consumption in adolescents is associated with improved weight status. Nutrition Research, 33(7): 552-556.
• Mylne, J. S., Hara-Nishimura, I., & Rosengren, K. J. (2014). Seed storage albumins: biosynthesis, trafficking and structures. Functional plant biology, 41(7): 671-677.
• O’Rourke, E., Tang, H., Chin, A., Long, A., & Sindher, S. (2022). Current insights: a systemic review of therapeutic options for peanut allergy. Current Opinion in Allergy and Clinical Immunology, 22(3): 188–193. https://doi.org/10.1097/ACI.0000000000000824
• Palladino, C., & Breiteneder, H. (2018). Peanut allergens. Molecular immunology, 100: 58-70. Pele, M. (2010). Peanut allergens. Romanian Biotechnology Lett. 15(2):5205.
• Petersen, A., Becker, W. M., & Jappe, U. (2013). What makes peanuts so allergenic?. Journal of the Serbian Chemical Society, 78(3): 321-331.
• Petersen, A., Kull, S., Rennert, S., Becker, W. M., Krause, S., Ernst, M., & Jappe, U. (2015). Peanut defensins: Novel allergens isolated from lipophilic peanut extract. Journal of Allergy and Clinical Immunology, 136(5): 1295-1301.
• Petersen, A., Rennert, S., Kull, S., Becker, W. M., Notbohm, H., Goldmann, T., & Jappe, U. (2014). Roasting and lipid binding provide allergenic and proteolytic stability to the peanut allergen Ara h 8. Biological chemistry, 395(2): 239-250. Porterfield, H. S., Murray, K. S., Schlichting, D. G., Chen, X., Hansen, K. C., Duncan, M. W., & Dreskin, S. C. (2009). Effector activity of peanut allergens: a critical role for Ara h 2, Ara h 6, and their variants. Clinical & Experimental Allergy, 39(7): 1099-1108.
• Radauer, C., & Breiteneder, H. (2006). Pollen allergens are restricted to few protein families and show distinct patterns of species distribution. Journal of Allergy and Clinical Immunology, 117(1): 141-147.
• Radauer, C., Bublin, M., Wagner, S., Mari, A., & Breiteneder, H. (2008). Allergens are distributed into few protein families and possess a restricted number of biochemical functions. Journal of allergy and clinical immunology, 121(4): 847-852.
• Saiz, J., Montealegre, C., Marina, M. L., & García-Ruiz, C. (2013). Peanut allergens: an overview. Critical reviews in food science and nutrition, 53(7): 722-737.
• Santiago, H. D. C., Bennuru, S., Ribeiro, J. M., & Nutman, T. B. (2012). Structural differences between human proteins and aero-and microbial allergens define allergenicity. PloS one, 7(7): e40552.
• Seidler, M. J., Hoflehner, E., & Gadermaier, G. (2024). Allergenicity and conformational diversity of allergens. Biomolecules, 14(1): 1. https://doi.org/10.3390/biom14010001
• Settaluri, V. S., Kandala, C. V. K., Puppala, N., & Sundaram, J. (2012). Peanuts and their nutritional aspects—a review.
• Toomer, O. T. (2018). Nutritional chemistry of the peanut (Arachis hypogaea). Critical reviews in food science and nutrition, 58(17): 3042-3053.
• Variath, M. T., & Janila, P. (2017). Economic and academic importance of peanut. The peanut genome, 7-26.
• Vereda, A., van Hage, M., Ahlstedt, S., Ibañez, M. D., Cuesta-Herranz, J., van Odijk, J., & Sampson, H. A. (2011). Peanut allergy: clinical and immunologic differences among patients from 3 different geographic regions. Journal of Allergy and Clinical Immunology, 127(3): 603-607.
• Vriens, K., Cammue, B. P., & Thevissen, K. (2014). Antifungal plant defensins: mechanisms of action and production. Molecules, 19(8): 12280-12303.
• Wen, H. W., Borejsza‐Wysocki, W., DeCory, T. R., & Durst, R. A. (2007). Peanut allergy, peanut allergens, and methods for the detection of peanut contamination in food products. Comprehensive reviews in food science and food safety, 6(2): 47-58.
• WHO/IUIS Allergen Nomenclature Sub-Committee. (2017). www.allergen.org/search.php?allergensource%20=%20Arachis+hypogaea
• Yusnawan, E., Marquis, C. P., & Lee, N. A. (2012). Purification and characterization of Ara h1 and Ara h3 from four peanut market types revealed higher order oligomeric structures. Journal of agricultural and food chemistry, 60(41): 10352-10358.
• Zhao, X., Chen, J., & Du, F. (2012). Potential use of peanut by-products in food processing: a review. Journal of food science and technology, 49: 521-529.
• Zhou, X., Wang, H., Wang, R., Zhu, Y., Xu, H., Wang, J., & Chen, Z. (2024). The structure and potential allergenicity of peanut allergen monomers after roasting. Food & Function, 15(4): 1238–1250. https://doi.org/10.1039/D3FO05351B
• Zhuang, Y., & Dreskin, S. C. (2013). Redefining the major peanut allergens. Immunologic Research, 55: 125-134.