Characterization of Antioxidant Peptides of Soybean Protein Hydrolysate
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.
<p>[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.</p>
<p>[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.</p>
@article{"International Journal of Biological, Life and Agricultural Sciences:61808", author = "Ferial M. Abu-Salem and Marwa H. Mahmoud and M. H. El-Kalyoub and A. Y. Gibriel and Azza Abou-Arab", title = "Characterization of Antioxidant Peptides of Soybean Protein Hydrolysate", abstract = "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.", volume = "7", number = "7", pages = "699-5", }
