Effects of transglutaminase catalysis on the functional and immunoglobulin binding properties of peanut flour dispersions containing casein

Journal of Agricultural and Food Chemistry

Volumn 56, Issue 22, 2008, Pages 10913-10921

  Clare, Debra A ^a   Gharst, Greg ^a   Maleki, Sohelia J ^b   Sanders, Timothy H ^c  

^a NORTH CAROLINA STATE UNIVERSITY   (United States)

^b SOUTHERN REGIONAL RESEARCH CENTER   (United States)

^c NORTH CAROLINA STATE UNIVERSITY   (United States)

Author keywords

Antibody reactivity; Casein; IgE binding; Peanut flour; Peanut proteins; Rheology; Transglutaminase

Indexed keywords

ALLERGEN; ALLERGEN ARA H3; ANTISERUM; ARA H 1 PROTEIN, ARACHIS HYPOGAEA; ARA H 2 ALLERGEN, ARACHIS HYPOGAEA; CASEIN; GLYCOPROTEIN; IMMUNOGLOBULIN; IMMUNOGLOBULIN E; PLANT ANTIGEN; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE; SEED STORAGE PROTEIN; VEGETABLE PROTEIN;

ARTICLE; CHEMISTRY; IMMUNOLOGY; METABOLISM; PEANUT; PROTEIN INTAKE; WESTERN BLOTTING;

ALLERGENS; ANTIGENS, PLANT; ARACHIS HYPOGAEA; BLOTTING, WESTERN; CASEINS; DIETARY PROTEINS; GLYCOPROTEINS; IMMUNE SERA; IMMUNOGLOBULIN E; IMMUNOGLOBULINS; PLANT PROTEINS; SEED STORAGE PROTEINS; TRANSGLUTAMINASES;

ARA; ARACHIS HYPOGAEA;

EID: 57849128508     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf801641d     Document Type: Article

References (38)

1. Suknark, K.; Phillips, R. D.; Chinnan, M. S. Physical properties of directly expanded extradates formulated from partially defatted peanut flour and different types of starch. Food Res. Int. 1997, 30, 575-583.
2. Basha, S. M. M.; Cherry, J. P.; Young, C. T. Changes in free amino-acids, carbohydrates, and proteins of maturing seeds from various peanut (Arachis-Hypogaea L. cultivars). Cereal Chem. 1976, 53, 586-597.
3. Steffe J. F. Rheological methods in food process engineering, 2nd Ed.; Freeman Press: East Lansing, MI, 1996.
4. Daubert, C. R.; Foegeding E. A. Rheological Principles for Food Analysis. In Chemical Analysis of Foods; Nielsen, S. S., Ed., Jones and Bartlett: Boston, Massachusetts, 1998.
5. Davis, J. P.; Gharst, G.; Sanders, T. H. Rheological Properties of Aqueous Peanut Flour Dispersions. J. Texture Stud. 2007, 38, 253-272.
6. Tang, C. H.; Wu, H.; Chen, Z.; Yang, X. Q. Formation of properties of glycinin-rich and β-conglycinin-rich soy protein isolate gels induced by microbial transglutaminase. Food Res. Int. 2006, 39, 87-97.
7. Truong, V. D.; Clare, D. A.; Catignani, G. L.; Swaisgood, H. E. Cross-linking and rheological changes of whey proteins treated with microbial transglutaminase. J. Agric. Food Chem. 2004, 52, 1170-1176.
8. Schorsch, C.; Carrie, H.; Clark, A. H.; Norton, I. T. Cross-linking casein micelles by a microbial transglutaminase conditions for formation of transglutaminase-induced gels. Int. Dairy J. 2000, 10, 519-528.
9. Folk, J. E.; Chung, S. I. Transglutaminases. Methods Enzymol. 1985, 113, 358-375.
10. Clare, D. A.; Gharst, G.; Sanders, T. H. Transglutaminase Polymerization of Peanut Proteins. J. Agric. Food Chem. 2007, 55, 432-438.
11. Zhu, Y.;Rinzema,A.;Tramper,J.;Bol,J.Mcrobial transglutaminase - A review of its production and application in food processing. Appl. Microbiol. Biotechnol. 1995, 44, 277-282.
12. Gharst, G.; Clare, D. A.; Davis, J. P.; Sanders, T. H. The effect of transglutaminase cross-linking on the rheological characteristics of peanut flour dispersions. J. Food Sci. 2007, 72, C369-C375.
13. Smithers, G. W.; Bradford, R. S.; Regester, G. O.; Pearce, R. J. New casein protein products for the food-industry - Physical, chemical and enzymatic manipulation of milk. Food Aust. 1991, 43, 252-254.
14. Lee, H. A.; Choi, S. J.; Moon, T. W. Characteristics of sodium caseinate-and soy protein isolate-stabilized emulsions-gels formed by microbial transglutaminase. J. Food Sci. 2006, 71, C352-C357.
15. SDAP: Structural database of allergenic proteins; Available at http://fermi.utmb.edu/SDAP/sdapf_src.html.
16. Lewis, S. A.; Grimshaw, K. E.; Warner, J. O.; Hourihane, J. O. The promiscuity of immunoglobulin E binding to peanut allergens, as determined by Western blotting, correlates with the severity of clinical symptoms. Clin. Exp. Allergy 2005, 35, 767-73.
17. van Wijk, F.; Hartgring, S.; Koppelman, S. J.; Pieters, R.; Knippels, L. M. Mixed antibody and T cell responses to peanut and the peanut allergens Ara h 1, Ara h 2, Ara h 3 and Ara h 6 in an oral sensitization model. Clin. Exp. Allergy 2004, 34, 1422-1428.
18. Koppelman, S. J.; Wensing, M.; Ertmann, M.; Knulst, A. C.; Knol, E. F. Relevance of Ara h 1, Ara h 2 and Ara h 3 in peanut-allergic patients, as determined by immunoglobulin E Western blotting, basophil-histamine release and intracutaneous testing: Ara h 2 is the most important peanut allergen. Clin. Exp. Allergy 2004, 34, 583-90.
19. Maleki, S. J.; Chung, S. Y.; Champagne, E. T.; Raufman, J. P. The effects of roasting on the allergenic properties of peanut proteins. J. Allergy Clin. Immun. 2000, 106, 763-768.
20. Maleki, S. J.; Chung, S. Y.; Champagne, E. T.; Khalifah, R. G. Allergic and biophysical properties of peanut proteins before and after roasting. Food Allergy Intolerance 2001, 2, 211-221, a journal for the World Food Industry.
21. Wilcox, C. P.; Swaisgood, H. E. Modification of the rheological properties of whey protein isolate through the use of an immobilized microbial transglutaminase. J. Agric. Food Chem. 2002, 50, 5546-5551.
22. Fleming, S. A.; Sosulski, F. W.; Kilara, A.; Humbert, E. S. Viscosity and water absorption characteristics of slurries of sunflower and soybean flours, concentrate and isolates. J. Food Sci. 1974, 39, 188-191.
23. Resch, J. J.; Daubert, C. R.; Foegeding, E. A. The effects of acidulant type on the rheological properties of beta-lactoglobulin gels and powders derived from these gels. Food Hydrocolloids 2005, 19, 851-860.
24. Wichers, H. J.; De Beijer, T.; Savelkoul, H. F. J.; Van Amerongen, A. The major peanut allergen Ara h 1 and its cleaved-off n-terminal peptide; possible implications for peanut allergen detection. J. Agric. Food Chem. 2004, 52, 4903-4907.
25. Koppleman, S. J.; Vlooswijk, R. A. A.; Knipples, L. M. J.; Hessing, M.; Knoll, E. F.; van Reijsen, F. C.; Bruijnzeel-Koomen, C. A. F. M. Quantification of major peanut allergens Ara h 1 and Ara h 2 in the peanut varieties Runner, Spanish, Virginia, and Valencia, bred in different parts of the world. Allergy 2001, 56, 132-137.
26. Koppleman, S. J.; Knol, E. F.; Vlooswijk, R. A. A.; Wensing, M.; Knulst, A. C.; Hefle, S. L.; Gruppen, H.; Piersma, S. Peanut allergen Ara h 3: Isolation from peanuts and biochemical characterization. Allergy 2003, 58, 1144-51.
27. Eissa, A. S.; Kahn, S. A. Modulation of hydrophobic interactions in denatured whey proteins by transglutaminase enzyme. Food Hydrocolloids 2006, 20, 543-547.
28. Eissa, A. S.; Puhl, C.; Kadla, J. F.; Khan, S. A. Enzymatic cross-linking of β-lactoglobulin: Conformational properties using FTR spectroscopy. Biomacromolecules 2006, 7, 1707-1713.
29. Bonisch, M. P.; Lauber, S.; Kulozik, U. Effect of ultra-high temperature treatment on the enzymatic cross-linking of micellar casein and sodium caseinate by transglutaminase. J. Food Sci. 2004, 69, 398-404.
30. Sen, M.; Kopper, R.; Pons, L.; Abraham, E. C.; Burks, A. W.; Bannon, G. A. Protein structure plays a critical role in peanut allergen stability and may determine immunodominant IgE-binding epitopes. J. Immunol. 2002, 882-887.
31. www.ajinomoto-usa.com
32. Steffe, J. F.; Daubert, C. R. Rheological properties of biological fluids. In Bioprocessing Pipelines: Rheology and Analysis; Freeman Press: East Lansing, MI, 2006; p 5.
33. Idris, W. H.; Babiker, E. E.; El Tinay, A. H. Fractionation, solubility and functional properties of wheat bran proteins as influenced by pH and/or salt concentration. Nahrung/Food 2003, 47, 425-429.
34. Khalid, E. K.; Babiker, E. E.; El Tinay, A. H. Solubility and functional properties of sesame seed proteins as influenced by pH and/or salt concentration. Food Chem. 2003, 82, 361-366.
35. Ragab, D. M.; Babiker, E. E.; El Tinay, A. H. Fractionation, solubility and functional properties of cowpea (Vigna unguiculata) proteins as affected by pH and/or salt concentration. Food Chem. 2004, 84, 207-212.
36. Anon, M. C.; Sorgentini, D. A.; Wagner, J. R. Relationships between different hydration properties of commercial and laboratory soybean isolates. J. Agric. Food Chem. 2001, 49, 4852-4858.
37. Chung, S. Y.; Maleki, S. J.; Champagne, E. T. Allergenic properties of roasted peanut allergens may be reduced by peroxidase. J. Agric. Food Chem. 2004, 52, 4541-4545.
38. Watanabe, M.; Suzuki, T.; Ikenzawa, Z.; Arai, S. Controlled enzymatic treatment of wheat proteins for production of hypoallergenic flour. Biosci., Biotechnol., Biochem. 1994, 58, 388-390.