Commenced in January 2007
Frequency: Monthly
Edition: International
Paper Count: 31824
Characterization of Antioxidant Peptides of Soybean Protein Hydrolysate

Authors: Ferial M. Abu-Salem, Marwa H. Mahmoud, M. H. El-Kalyoub, A. Y. Gibriel, Azza Abou-Arab


In order to characterize the soy protein hydrolysate obtained in this study, gel chromatography on Sephadex G-25 was used to perform the separation of the peptide mixture and electrophoresis in SDS-polyacrylamide gel has been employed. Protein hydrolysate gave high antioxidant activities, but didn't give any antimicrobial activities. The antioxidant activities of protein hydrolysate was in the same trend of peptide content which gave high antioxidant activities and high peptide content between fractions 15 to 50. With increasing peptide concentrations, the scavenging effect on DPPH radical increased until about 70%, thereafter reaching a plateau. In compare to different concentrations of BHA, which exhibited higher activity (90%), soybean protein hydrolysate exhibited high antioxidant activities (70%) at a concentration of 1.45 mg/ml at fraction 25. Electrophoresis analysis indicated that, low- MW hydrolysate fractions (F1) appeared, on average, to have higher DPPH scavenging activities than high-MW fractions. These results revealed that soybean peptides probably contain substances that were proton donors and could react with free radicals to convert them to stable diamagnetic molecules. 

Keywords: Antioxidant peptides, hydrolysis, protein hydrolysate, peptide fractions.

Digital Object Identifier (DOI):

Procedia APA BibTeX Chicago EndNote Harvard JSON MLA RIS XML ISO 690 PDF Downloads 4564


[1] P. Kehrer, “Free radicals as mediators of tissue injury and disease." Critical Rev in Toxic., vol. 23, pp. 21–48, 1993.
[2] N. Baydar, G. O¨ zkan, and S. Yasar, “Evaluation of the antiradical and antioxidant potential of grape extracts," Food Control, vol.18, pp. 1131– 1136, 2007.
[3] N. Rajapakse, E. Mendis, W. K. Jung, J. Y. Je, and S.K. Kim, “Purification of a radical scavenging peptide from fermented mussel sauce and its antioxidant properties,” Food Research International, vol. 38, pp.175–182, 2005.
[4] R. Marcuse, “Antioxidative effect of amino acids,” Nature, vol.186, pp.886-887, 1960.
[5] A. Saiga, S. Tanabe, and T. Nishimura, “Antioxidant activity of peptides obtained from porcine myofibrilar proteins by proteasetreatment,” J. Agriculture Food Chemistry, vol.51, no. 12, pp.3661–3667, 2003.
[6] S. Morimura, H. Nagata, Y. Uemura, A. Fahmi, T. Shigematsu and K. Kida, “Development of an effective process for utilization of collagen from livestock and fish waste,” Process Biochemistry, vol.37, no. 12, pp. 1403–1412, 2002.
[7] S. Sakanaka, Y. Tachibana, N. Ishihara, and LR. Juneja, “Antioxidant activity of egg-yolk protein hydrolyzates in a linoleic acid oxidation system,” Food Chemistry, vol. 86, no. 1,pp. 99–103, 2004.
[8] F. Shahidi, and R. Amarowicz, “Antioxidant activity of protein hydrolyzates from aquatic species,” J. American Oil Chemistry Society, vol.73, no. 9, pp. 1197–1199, 1996.
[9] Y. Je, P.Y. Park, and S.K. Kim, “Antioxidant activity of a peptide isolated from Alaska Pollack (Theragra chalcogramma) frame protein hydrolysate,” Food Res Int , vol.38, pp .45–50, 2005.
[10] R. E. Aluko, and E. Monu, “Functional and bioactive properties of quinoa seed protein hydrolyzates,” J. of Food Science, vol. 68, no. 4, pp. 1254–1258, 2003.
[11] B.F. Gibbs, A. Zougman, R. Masse, and C. Mulligan, "Production and characterization of bioactive peptides from soy hydrolysate and soyfermented food,” Food Research International, vol. 37, no. 2, pp. 123– 131, 2004.
[12] H.M. Chen, K. Muramoto, F. Yamauchi, and K. Nokihara, “Antioxidant activity of designed peptides based on the antioxidative peptide isolated from digests of a soybean protein,” J. Agriculture Food Chemistry, vol. 44, no. 9, pp.2126–2130, 1996.
[13] H.M. Chen, K. Muramoto, F. Yamauchi, K. Fujimoto, and K. Nokihara, “Antioxidative properties of histidine-containing peptides designed from peptide fragments found in the digests of a soybean protein,” J. Agriculture Food Chemistry, vol. 46, no. 1, pp. 49–53, 1998.
[14] W.D. Chiang, C.J. Shih, and Y.H. Chu, “Functional properties of soy protein hydrolysate produced from a continuous membrane reactor system,” Food Chemistry, vol. 65, no. 2, pp. 189–194, 1999.
[15] E.N. Frankel and A. Meyer, “The problems of using one-dimensional methods to evaluate multifunctional food and biological antioxidants,” J. Science Food Agriculture, vol. 23, 80, no. 13, pp. 1925–1941, 2000.
[16] C. Sa´nchez-Moreno, “Methods used to evaluate the free radical scavenging activity in foods and biological systems,” Food Science Technology International, vol. 8, no. 3, pp. 121–137, 2002.
[17] E.A. Pen˜a-Ramos, and Y.L. Xiong, “Antioxidant activity of soy protein hydrolyzates in a liposomial system,” J. of Food Science, vol. 6, no. 8, pp. 2952–2956, 2002.
[18] A. Arnoldi, A. D’Agostina, G. Boschin, M.R. Lovati, C. Manzoni, and C.R. Sirtori, “Soy protein components active in the regulation of cholesterol homeostasis. In: Biologically active phytochemicals in food,” Royal Society of Chemistry, vol. 269, pp. 103–106, 2001.
[19] J.R. Chen, S.C. Yang, K. Suetsuna, and J.C.J. Chao, “Soybean proteinderived hydrolysate affects blood pressure in spontaneously hypertensive rats,” J. Food Biochemistry, vol. 28, no. 1, pp. 61–73, 2004.
[20] H.M. Chen, K. Muramoto, and F. Yamauchi, “Structural analysis of antioxidative peptides from soybean b-conglycinin,” Agriculture Food Chemistry, vol. 43, no. 3, pp. 574–578, 1995.
[21] W.C. Hou, H.J. Chen, and Y.H. Lin, Antioxidant peptides with angiotensin converting enzyme inhibitory activities and applications for angiotensin converting enzyme purification,”.J. Agriculture Food Chemistry, vol. 51, pp. 1706-1709, 2003.
[22] Y.P. Zhu, J.F. Fan, Y.Q. Cheng, and L.T. Li, "Improvement of the antioxidant activity of Chinese traditional fermented okara (Meitauza) using Bacillus subtilis B2, "Food Control, vol. 19, pp.654-661, 2008.
[23] C. Wang, Q. Ma, S. Pagadala, M.S. Sherrard, and P.G. Krishnan, "Changes of Isoflavones during Processing of Soy Protein Isolates,” J. American Oil Chemistry Society, vol. 75, no. 3, pp. 337-341, 1998.
[24] J. Adler-Nissen, “Determination of degree of hydrolysis of food protein hydrolysates by trinitrobenzenesulfonic acid,” J. Agriculture. Food Chemistry, vol. 27, pp. 1256-1262, 1979.
[25] F.M. Netto, and M.A.M. Galeazzi, “Production and characterization of enzymatic hydrolysate from soy protein isolate,” Lebensm.-wiss. U.- Technol, vol. 31, pp. 624-631, 1998.
[26] K.A. Lee and S.H. Kim, “SSGE and DEE, new peptides isolated from a soy protein hydrolysate that inhibit platelet aggregation,” Food Chemistry, vol. 90, pp. 389-393, 2005.
[27] C. Marı´a, S. Conde, A. Adriana, and C. An˜o´n, “Characterization of amaranth proteins modified by trypsin proteolysis. Structural and functional changes,” LWT - Food Science and Technology, vol. 42, pp. 963–970, 2009.
[28] SAS. “SAS User's Guide: Statistics,” SAS Inc., Cary, NC, 1982.
[29] W. R. Waller and D.B. Duncan, “A Bayes rule for the symmetric multiple comparison problems," J. of the American Statistical Association, vol. 64, pp. 1481-1503, 1969.
[30] S.B. Zhang, Z. Wang, and S.Y. Xu, “Antioxidant and Antithrombotic Activities of Rapeseed Peptides,” J. American Oil Chemistry Society, vol. 85, pp. 521–527, 2008.
[31] Y. Yoshie Starka, Y. Wadab, M. Schottb, and A. Wasche, “Functional and bioactive properties of rapeseed protein concentrates and sensory analysis of food application with rapeseed protein concentrates,” LWT, vol. 39, pp. 503–512, 2006.
[32] K. Saito, D.H. Jin, T. Ogawa, K. Muramoto, E. Hatakeyama, and T. Yasuhara, “Antioxidative properties of tripeptide libraries prepared by the combinatorial chemistry,” J. Agriculture Food Chemistry, vol. 51, no. 12, pp. 3668-3674, 2003.