نوع مقاله : مقاله پژوهشی

نویسندگان

1 دانشگاه شیراز-دانشکده کشاورزی

2 دانشگاه شیراز

چکیده

کانژوگه‌های پروتئین‌های سویای رسوب‌یافته با اسید و مالتودکسترین تحت شرایط کنترل‌شده واکنش مایلارد آماده شدند. (دمای 60 درجه سانتی‌گراد، 8 :pH، رطوبت نسبی 79٪ و زمان‌های 1، 3، 5 و 7 روز). تشکیل کانژوگه‌های پروتئین-پلی‌ساکارید با الکتروفورز SDS-PAGE تائید شد و کروماتوگرافی ژل فیلتراسیون نشان داد واکنش مایلارد بین پروتئین‌های سویا و مالتودکسترین رخ داده است. مطابق نتایج آنالیز گرماسنجی افتراقی (DSC)، پایداری حرارتی پروتئین‌های سویا به‌طور چشمگیری توسط کانژوگه شدن با مالتودکسترین افزایش یافت و بیشترین دمای دناتوراسیون بعد از 7 روز گرم‌خانه‌گذاری مشاهده شد. در مقایسه با نمونه شاهد، خصوصیات حلالیت، کف‌کنندگی و امولسیفایری به‌طور قابل توجه‌ای با افزایش زمان گرم‌خانه‌گذاری بهبود یافت. نتایج نشان داد که خصوصیات فیزیکوشیمیایی و عملکردی پروتئین‌های سویا از طریق کانژوگه شدن با مالتودکسترین تغییر و بهبود می‌یابد.

کلیدواژه‌ها

1. Abtahi, S. and Aminlari, M. 1997. Effect of sodium sulfite, sodium bisulfite, cysteine, and pH on protein solubility and Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis of soybean milk base. Journal of Agricultural and Food Chemistry, 45: 4768-4772.
2. Aminlari, M. Ramezani, R. and Jadidi, F. 2005. Effect of Maillard-based conjugation with dextran on the functional properties of lysozyme and casein. Journal of the Science of Food and Agriculture, 85: 2617–2624.
3. Achouri, A. Boye, J. I. Yaylayan, V. A and Yeboah, F. K. 2005. Functional properties of glycated soy 11S glycinin. Journal of Food Science, 70: 269-274.
4. Al-hakkak, J. and Al-hakkak, F. 2010. Functional egg white–pectin conjugates prepared by controlled Maillard reaction. Journal of Food Engineering, 100: 152–159.
5. Babiker, E. Hiroyuki, A. Matsudomi, N. Iwata, H. Ogawa, T. Bando, N. and Kato, A. 1998. Effect of polysaccharide conjugation or transglutaminase treatment on the allergenicity and functional properties of soy protein. Journal of Agricultural and Food Chemistry, 46: 866-871.
6. Chrystel Loret, W. J. F. 2008. Influence of preparation conditions of maltodextrin gel on food texture. 3rd International Symposium on Food Rheology and Structure.
7. Chiu T. Chen, M. and Chang, H. 2009. Comparisons of emulsifying properties of maillard reaction products conjugated by green, red seaweeds and various commercial proteins. Food Hydrocolloids, 23: 2270–2277.
8. Damodaran, S. 1996. Amino Acids, Peptides and Proteins. In: Food Chemistry, 3rd ed.; Fennema, O. R., Ed.; Dekker: New York. 321-330.
9. Diftis, N. and Kiosseoglou, V. 2003. Improvement of emulsifying properties of soybean protein isolate by conjugation with carboxymethyl cellulose. Food Chemistry, 81: 1–6.
10. Endres, J. G. 2001. Soy protein products characteristics, nutritional aspects, and utilization. AOAC Press, Champaign IL. 16-30.
11. Fernandez, Q. A. and Macarulla, M. T. 1997. Composition and functional properties of protein isolates obtained from commercial legumes grown in northern Spain. Plant Foods for Human Nutrition 51: 331–342.
12. Gan, C.Y. Cheng, L.H. and Easa, A.M. 2008. Assessment of Maillard reaction and cross-linking in transglutaminase-cross-linked powdered soy protein isolate gel. Food Research International. Communicating.
13. Janson, J.C. 1998. Protein purification, principle of high resolution methods and application, New York, WILEY-LISS. Inc.
14. Iwabuchi, S. and Yamauchi, F. 1987. Determination of glycinin and β-conglycinin in soy protein by immunological methods. Journal of Agricultural and Food Chemistry, 35: 200–205.
15. Kilara, A. and Sharkasi, T.Y. 1986. Effect of temperature on food protein. Critical Reviews in Food Science and Nutrition, 23: 323-395.
16. Kato, A. 2002. Industrial applications of maillard-type protein- polysaccharide conjugates, Food Science and Technology Research, 8: 193-199.
17. Kato, A. Shimokawa, K. and Kobayashi, K. 1991. Improvement of the functional properties of insoluble gluten by pronase digestion followed by dextran conjugation. Journal of Agricultural and Food Chemistry, 39: 1053-1058.
18. Kato, A. Mifuru, R. Matsudomi, N. and Kobayashi, K. 1992. Functional casein-polysaccharide conjugates prepared by controlled dry heating. Bioscience, Biotechnology, and Biochemistry, 56:567–571.
19. Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of head of bacteriophage T4. Nature, 227: 680-685.
20. Liu, Y. Zhao, G. Zhao, M. Ren, J. and Yang, B. 2012. Improvement of functional properties of peanut protein isolate by conjugation with dextran through Maillard reaction, Food Chemistry, 131: 901–906.
21. Nakamura, S. Ogawa, M. Nakai, S. Kato, A. and Kitts, D. 1998. Antioxidant activity of a maillard-type phosvitin-galactomannan conjugate with emulsifying properties and heat stability. Journal of Agricultural and Food Chemistry, 46: 3958-3963.
22. Oliver, C. M. Stanley, R. A. and Melton, L. D. 2006. Creating proteins with novel functionality through the maillard reaction. Critical Reviews in Food Science and Nutrition, 46: 337-350.
23. O′Regan, J. and Mulvihill, D. M. 2009. Preparation, characterisation and selected functional properties of sodium caseinate–maltodextrin conjugates. Food Chemistry, 115, 1257–1267.
24. Pearce, K. M. and Kinsella, J. E. 1978. Emulsifying properties of proteins: evaluation of a turbidimeric technique. Journal of Agricultural and Food Chemistry, 26: 716-723.
25. Qi, J. R. Yang, X. Q. and Liao, J. S. 2009. Improvement of functional properties of acid-precipitated soy protein by the attachment of dextran through Maillard reaction. International Journal of Food Science and Technology, 44, 2296–2302.
26. Tang, C. Choi, S. and Ma, C. 2007. Study of thermal properties and heat-induced denaturation and aggregation of soy proteins by modulated differential scanning calorimetry, International Journal of Biological Macromolecules, 40: 96–104.
27. Van de Lagemaat, J. Manuel Silvan, J. Javier Moreno, F. Olano, A. and Dolores del Castillo, M. 2007. In vitro glycation and antigenicity of soy proteins. Food Research International, 40: 153–160.
28. Van Boekel, M. A. J. S. 2001. Kinetic aspects of the Maillard reaction: A critical review. Nahrung, 45: 150-159.
29. Wang, Q. and Ismail, B. 2012. Effect of Maillard-induced glycosylation on the nutritional quality, solubility, thermal stability and molecular configuration of whey protein. International Dairy Journal, 25: 112-122.
30. Xu, C.H. Yang, X.Q. Yu, S.J. Qi, J.R. Guo, R. Sun, W.W. Yao, Y.J. and Zhao, M.M. 2010. The effect of glycosylation with dextran chains of differing lengths on the thermal aggregation of β-conglycinin and glycinin, Food Research International 43: 2270–2276.
31. Yadav, M.P. Parris, N. Johnston D.B. Onwulata, C.I and Hicks, K.B. 2010. Corn fiber gum and milk protein conjugates with improved emulsion stability, Carbohydrate Polymers, 81: 476–483.
CAPTCHA Image