Effect of Ribose on Mature/Immature Raw Peanut Proteins and Their Allergenic Properties

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DOI: 10.4236/fns.2011.24042   PDF   HTML   XML   5,504 Downloads   8,816 Views   Citations

Abstract

Mature and immature roasted peanuts are reportedly different in the level of Maillard reaction adducts (MRA) and IgE binding (i.e., allergenic capacity). Heating and sugar-protein interaction are the cause for the difference. The objective of this study was to determine if mature and immature raw peanuts (not roasted) are also different through treatment with a reducing sugar such as ribose, glucose or fructose at a mild temperature. Extracts from mature and immature raw peanuts were treated with individual sugars at 37?C and 50?C, respectively, for 0 - 10 days, and then assayed for MRA with nitroblue tetrazolium (NBT) in a time-course manner for 60 min. IgE binding was determined in an enzyme- linked immunosorbent assay (ELISA), using a pooled plasma from peanut-allergic individuals. Of the sugars tested, only ribose produced a big difference or a unique curve pattern in MRA between treated mature and immature peanuts. The unique curve pattern was more pronounced at 50?C (day 5 - 10) than at 37?C. IgE binding under this condition increased, but only with the ribose-treated mature raw peanut. It was concluded that mature and immature raw peanuts were different in MRA and IgE binding when treated with ribose only, and that under such a condition, mature and immature raw peanuts could be identified.

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S. Chung, "Effect of Ribose on Mature/Immature Raw Peanut Proteins and Their Allergenic Properties," Food and Nutrition Sciences, Vol. 2 No. 4, 2011, pp. 294-300. doi: 10.4236/fns.2011.24042.

Conflicts of Interest

The authors declare no conflicts of interest.

References

[1] Y. Hellsten, L. Skadhauge and J. Bangsbo, “Effect of Ribose Supplementation on Resynthesis of Adenine Nucleotides after Intermittent Training in Humans,” American Journal of Physiology-Regulatory Integrative and Comparative Physiology, Vol. 286, No. 1, 2004, pp. R182-R188. doi:10.1152/ajpregu.00286.2003
[2] M. Friedman, “Food Browning and Its Prevention. An Overview,” Journal of Agricultural and Food Chemistry, Vol. 44, No. 3, 1996, pp. 631-653. doi:10.1021/jf950394r
[3] H. Jing and D. D. Kitts, “Comparison of the Antioxidative and Cytoxic Properties of Glucose-Lysine and Fructose-Lysine Maillard Reaction Products,” Food Research International, Vol. 33, No. 6, 2000, pp. 509-516. doi:10.1016/S0963-9969(00)00076-4
[4] J. M. Chobert, J. C. Gaudin, M. Dalalarrondo and T. Ha- ertle, “Impact of Maillard Type Glycation on Properties of Beta-Lactoglobulin,” Biotechnology Advance, Vol. 24, No. 6, 2006, pp. 629-632. doi:10.1016/j.biotechadv.2006.07.004
[5] L. Graham, “A Comprehensive Survey of the Acid-Stable Fluorescent Cross-Links Formed by Ribose with Basic Amino Acids, and Partial Characterization of a Novel Maillard Cross-Link,” Biochim Biosphysic Acta, Vol. 1297, No. 1, 1996, pp. 9-16. doi:10.1016/0167-4838(96)00082-9
[6] S. B. M. Yasir, K. H. Sutton, M. P. Newberry, N. R. Andrews and J. A. Gerrard, “The Impact of Transglutaminase on Soy Proteins and Tofu Texture,” Food Chemistry, Vol. 104, No. 4, 2007, pp. 1491-1501. doi:10.1016/j.foodchem.2007.02.026
[7] S. Y. Chung, C. Butts, S. J. Maleki and E. T. Champagne, “Linking Peanut Allergenicity to the Processes of Maturation, Curing and Roasting,” Journal of Agricultural and Food Chemistry, Vol. 51, No. 15, 2003, pp. 4273-4277. doi:10.1021/jf021212d
[8] T. H. Sanders, J. R. Vercellotti, P. D. Blankenship, K. L. Crippen and G. V. Civille, “Interaction of Maturity and Curing Temperature on Descriptive Flavor of Peanuts,” Journal of Food Science, Vol. 54, No. 4, 1989, pp. 1066-1069. doi:10.1111/j.1365-2621.1989.tb07944.x
[9] T. H. Sanders, “Maturity Distribution in Commercially Sized Florunner Peanuts,” Peanut Science, Vol. 16, No. 2, 1989, pp. 91-95. doi:10.3146/i0095-3679-16-2-8
[10] E. L. Williams and J. S. Drexler, “A Non-Destructive Method for Determining Peanut Pod Maturity,” Peanut Science, Vol. 8, No. 2, 1981, pp. 134-141. doi:10.3146/i0095-3679-8-2-15
[11] S. Y. Chung and E. T. Champagne, “Allergenicity of Maillard Reaction Products from Peanut Proteins,” Journal of Agricultural and Food Chemistry, Vol. 47, No. 12, 1999, pp. 5227-5231. doi:10.1021/jf9904416
[12] S. Y. Chung and E. T. Champagne, “Association of End- product Adducts with Increased IgE Binding of Roasted Peanuts,” Journal of Agricultural and Food Chemistry, Vol. 49, No. 8, 2001, pp. 3911-3916. doi:10.1021/jf001186o
[13] P. Gruber, W. M. Becker and T. Hofmann, “Influence of the Maillard Reaction on the Allergenicity of rAra h 2, a Recombinant Major Allergen from Peanut (Arachis Hypogaea), Its Major Epitopes, and Peanut Agglutinin,” Journal of Agricultural and Food Chemistry, Vol. 53, No. 6, 2005, pp. 2289-2296. doi:10.1021/jf048398w
[14] A. Ilchmann, S. Burgdorf, S. Scheurer, Z. Waibler, R. Nagai, A. Wellner, Y. Yamamoto, H. Yamamoto, T. Henle, C. Kurts, U. Kalinke, S. Vieths and M. Toda, “Glycation of a Food Allergen by the Maillard Reaction Enhances Its T-Cell Immunogenicity: Role of Macrophage Scavenger Receptor Class A Type I and II,” Journal of Allergy and Clinical Immunology, Vol. 125, No. 1, 2010, pp. 175-183. doi:10.1016/j.jaci.2009.08.013
[15] S. M. M. Basha, J. P. Cherry and C. T. Young, “Free and Total Amino Acid Composition of Maturing Seed from Six Peanut (Arachis Hypogaea L.) Cultivars,” Peanut Science, Vol. 7, No. 1, 1980, pp. 32-37. doi:10.3146/i0095-3679-7-1-8
[16] S. H. Ashoor and J. B. Zent, “Maillard Browning in Common Amino Acids and Sugars,” Journal of Food Science, Vol. 49, No. 4, 1984, pp. 1206-1207. doi:10.1111/j.1365-2621.1984.tb10432.x
[17] S. T. Talcott, S. Passeretti, C. E. Duncan and D. W. Gorbet, “Polyphenolic Content and Sensory Properties of Normal and High Oleic Acid Peanuts,” Food Chemistry, Vol. 90, No. 3, 2005, pp. 379-388. doi:10.1016/j.foodchem.2004.04.011
[18] A. Nakamura, K. Watanabe, T. Ojima, D. H. Ahn and H. Saeki, “Effect of Maillard Reaction on Allergenicity of Scallop Tropomyosin,” Journal of Agricultural and Food Chemistry, Vol. 53, No. 19, 2005, pp. 7559-7564. doi:10.1021/jf0502045
[19] A. Taheri-Kafrani, J. C. Gaudin, H. Rabesona, C. Nioi, D. Agarwal, M. Drouet, J. M. Chobert, A. K. Bordbar and T. Haertle, “Effects of Heating and Glycation of β-Lactoglobulin on Its Recognition by IgE of Sera From Cow Milk Allergy Patients,” Journal of Agricultural and Food Chemistry, Vol. 57, No. 11, 2009, pp. 4974-4982. doi:10.1021/jf804038t
[20] S. Nakamura, Y. Suzuki, E. Ishikawa, T. Yakushi, H. Jing, T. Miyamoto and K. Hashizume, “Reduction of in Vitro Allergenicity of Buckwheat Fag e 1 through the Maillard-Type Glycosylation with Polysaccharides,” Food Chemistry, Vol. 109, No. 3, 2008, pp. 538-545. doi:10.1016/j.foodchem.2007.12.075
[21] L. Mondoulet, E. Paty, M. F. Drumare, S. Ah-Leung, P. Scheinmann, R. M. Willemot, J. M. Wal and H. Bernard, “Influence of Thermal Processing on the Allergenicity of Peanut Proteins,” Journal of Agricultural and Food Che- mistry, Vol. 53, No. 11, 2005, pp. 4547-4553. doi:10.1021/jf050091p

  
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