메뉴 건너뛰기




Volumn 49, Issue 9, 2014, Pages 1562-1569

Purification and evaluation of a novel antioxidant peptide from corn protein hydrolysate

Author keywords

Antioxidant activity; Corn protein; Hexapeptide; Hydrolysate

Indexed keywords

AMINO ACIDS; ANTIOXIDANTS; ENZYMATIC HYDROLYSIS; FREE RADICALS; MOLECULAR WEIGHT; PROTEOLYSIS; PURIFICATION;

EID: 84906783586     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.procbio.2014.05.014     Document Type: Article
Times cited : (83)

References (38)
  • 1
    • 0031826591 scopus 로고    scopus 로고
    • Effect of hydrophilic plasticizers on thermo-mechanical properties of corn gluten meal
    • L.D. Gioia, B. Cuq, and S. Guilbert Effect of hydrophilic plasticizers on thermo-mechanical properties of corn gluten meal Cereal Chem 75 1998 514 519
    • (1998) Cereal Chem , vol.75 , pp. 514-519
    • Gioia, L.D.1    Cuq, B.2    Guilbert, S.3
  • 2
    • 0037093739 scopus 로고    scopus 로고
    • Effect of diet on cancer development: Is oxidative DNA damage a biomarker
    • B. Halliwell Effect of diet on cancer development: is oxidative DNA damage a biomarker Free Radic Biol Med 32 2002 968 974
    • (2002) Free Radic Biol Med , vol.32 , pp. 968-974
    • Halliwell, B.1
  • 3
    • 33750710080 scopus 로고    scopus 로고
    • Protein oxidation and aging
    • E.R. Stadtman Protein oxidation and aging Free Radic Res 40 2006 1250 1258
    • (2006) Free Radic Res , vol.40 , pp. 1250-1258
    • Stadtman, E.R.1
  • 6
    • 84871462783 scopus 로고    scopus 로고
    • Production of antioxidant soy protein hydrolysates by sequential ultrafiltration and nanofiltration
    • S. Ranamukhaarachchi, L. Meissner, and C. Moresoli Production of antioxidant soy protein hydrolysates by sequential ultrafiltration and nanofiltration J Membr Sci 429 2013 81 87
    • (2013) J Membr Sci , vol.429 , pp. 81-87
    • Ranamukhaarachchi, S.1    Meissner, L.2    Moresoli, C.3
  • 7
    • 84873257881 scopus 로고    scopus 로고
    • Antioxidant activities of enzymatic rapeseed protein hydrolysates and the membrane ultrafiltration fractions
    • R. He, A.T. Girgih, S.A. Malomo, X.R. Ju, and R.E. Aluko Antioxidant activities of enzymatic rapeseed protein hydrolysates and the membrane ultrafiltration fractions J Funct Foods 5 2013 219 227
    • (2013) J Funct Foods , vol.5 , pp. 219-227
    • He, R.1    Girgih, A.T.2    Malomo, S.A.3    Ju, X.R.4    Aluko, R.E.5
  • 8
    • 80051545037 scopus 로고    scopus 로고
    • Antioxidant activities of rapeseed protein hydrolysates
    • M. Pan, T.S. Jiang, and J.L. Pan Antioxidant activities of rapeseed protein hydrolysates Food Bioprocess Technol 4 2011 1144 1152
    • (2011) Food Bioprocess Technol , vol.4 , pp. 1144-1152
    • Pan, M.1    Jiang, T.S.2    Pan, J.L.3
  • 9
    • 70349916047 scopus 로고    scopus 로고
    • Antioxidant activities of the rice endosperm protein hydrolysate: Identification of the active peptide
    • J.H. Zhang, H. Zhang, L. Wang, X.N. Guo, X.G. Wang, and H.Y. Yao Antioxidant activities of the rice endosperm protein hydrolysate: identification of the active peptide Eur Food Res Technol 229 2009 709 719
    • (2009) Eur Food Res Technol , vol.229 , pp. 709-719
    • Zhang, J.H.1    Zhang, H.2    Wang, L.3    Guo, X.N.4    Wang, X.G.5    Yao, H.Y.6
  • 10
    • 84867844723 scopus 로고    scopus 로고
    • Purification and identification of antioxidant peptides from chickpea (Cicer arietinum L.) albumin hydrolysates
    • X.H. Kou, J. Gao, Z.H. Xue, Z.J. Zhang, H. Wang, and X. Wang Purification and identification of antioxidant peptides from chickpea (Cicer arietinum L.) albumin hydrolysates LWT - Food Sci Technol 50 2013 591 598
    • (2013) LWT - Food Sci Technol , vol.50 , pp. 591-598
    • Kou, X.H.1    Gao, J.2    Xue, Z.H.3    Zhang, Z.J.4    Wang, H.5    Wang, X.6
  • 11
    • 84861097104 scopus 로고    scopus 로고
    • Fractionation and characterization of antioxidant peptides derived from barley glutelin by enzymatic hydrolysis
    • Y.C. Xia, F. Bamdad, M. Gänzle, and L.Y. Chen Fractionation and characterization of antioxidant peptides derived from barley glutelin by enzymatic hydrolysis Food Chem 134 2012 1509 1518
    • (2012) Food Chem , vol.134 , pp. 1509-1518
    • Xia, Y.C.1    Bamdad, F.2    Gänzle, M.3    Chen, L.Y.4
  • 12
    • 75749122983 scopus 로고    scopus 로고
    • Influence of degree of hydrolysis on functional properties, antioxidant activity and ACE inhibitory activity of peanut protein hydrolysate
    • S.N. Jamdar, V. Rajalakshmi, M.D. Pednekar, F. Juan, V. Yardi, and A. Sharma Influence of degree of hydrolysis on functional properties, antioxidant activity and ACE inhibitory activity of peanut protein hydrolysate Food Chem 121 2010 178 184
    • (2010) Food Chem , vol.121 , pp. 178-184
    • Jamdar, S.N.1    Rajalakshmi, V.2    Pednekar, M.D.3    Juan, F.4    Yardi, V.5    Sharma, A.6
  • 13
    • 2542545209 scopus 로고    scopus 로고
    • Antioxidant activity of designed peptides based on the antioxidative peptide isolated from digests of a soybean protein
    • 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 Agric Food Chem 44 1996 2619 2623
    • (1996) J Agric Food Chem , vol.44 , pp. 2619-2623
    • Chen, H.M.1    Muramoto, K.2    Yamauchi, F.3    Nokihara, K.4
  • 14
    • 0035358387 scopus 로고    scopus 로고
    • Purification and characterization of antioxidative peptides from protein hydrolysate of lecithin-free egg yolk
    • P.J. Park, W.K. Jung, K.S. Nam, F. Shahidi, and S.K. Kim Purification and characterization of antioxidative peptides from protein hydrolysate of lecithin-free egg yolk J Am Oil Chem Soc 78 2001 651 656
    • (2001) J Am Oil Chem Soc , vol.78 , pp. 651-656
    • Park, P.J.1    Jung, W.K.2    Nam, K.S.3    Shahidi, F.4    Kim, S.K.5
  • 15
    • 33751513849 scopus 로고    scopus 로고
    • Production of hydrolysate with antioxidative activity by enzymatic hydrolysis of extruded corn gluten
    • X.Q. Zheng, L.T. Li, X.L. Liu, X.J. Wang, J. Lin, and D. Li Production of hydrolysate with antioxidative activity by enzymatic hydrolysis of extruded corn gluten Appl Microbiol Biotechnol 73 2006 763 770
    • (2006) Appl Microbiol Biotechnol , vol.73 , pp. 763-770
    • Zheng, X.Q.1    Li, L.T.2    Liu, X.L.3    Wang, X.J.4    Lin, J.5    Li, D.6
  • 16
    • 43649092437 scopus 로고    scopus 로고
    • Reducing, radical scavenging, and chelation properties of in vitro digests of Alcalase-treated zein hydrolysate
    • L.J. Zhu, J. Chen, X.Y. Tang, and Y. Xiong Reducing, radical scavenging, and chelation properties of in vitro digests of Alcalase-treated zein hydrolysate J Agric Food Chem 56 2008 2714 2721
    • (2008) J Agric Food Chem , vol.56 , pp. 2714-2721
    • Zhu, L.J.1    Chen, J.2    Tang, X.Y.3    Xiong, Y.4
  • 17
    • 84865779303 scopus 로고    scopus 로고
    • Production and functional characterisation of antioxidative hydrolysates from corn protein via enzymatic hydrolysis and ultrafiltration
    • K.Q. Zhou, S. Sun, and C. Canning Production and functional characterisation of antioxidative hydrolysates from corn protein via enzymatic hydrolysis and ultrafiltration Food Chem 135 2012 1192 1197
    • (2012) Food Chem , vol.135 , pp. 1192-1197
    • Zhou, K.Q.1    Sun, S.2    Canning, C.3
  • 18
    • 84888439264 scopus 로고    scopus 로고
    • Purification and identification of antioxidant peptides from corn gluten meal
    • H. Zhuang, N. Tang, and Y. Yuan Purification and identification of antioxidant peptides from corn gluten meal J Funct Foods 5 2013 1810 1821
    • (2013) J Funct Foods , vol.5 , pp. 1810-1821
    • Zhuang, H.1    Tang, N.2    Yuan, Y.3
  • 21
    • 0016272750 scopus 로고
    • Involvement of the superoxide anion radical in the autoxidation of pyrogallol and a convenient assay for superoxide dismutase
    • S. Marklund, and G. Marklund Involvement of the superoxide anion radical in the autoxidation of pyrogallol and a convenient assay for superoxide dismutase Eur J Biochem 47 1974 469 474
    • (1974) Eur J Biochem , vol.47 , pp. 469-474
    • Marklund, S.1    Marklund, G.2
  • 22
    • 69049094874 scopus 로고    scopus 로고
    • Antioxidant activities form the aerial parts of Platycodon grandiflorum
    • C.H. Jeong, G.N. Choi, J.H. Kim, J.H. Kwaka, D.O. Kimb, and Y.J. Kimc et al. Antioxidant activities form the aerial parts of Platycodon grandiflorum Food Chem 118 2010 278 282
    • (2010) Food Chem , vol.118 , pp. 278-282
    • Jeong, C.H.1    Choi, G.N.2    Kim, J.H.3    Kwaka, J.H.4    Kimb, D.O.5    Kimc, Y.J.6
  • 23
    • 33847297952 scopus 로고    scopus 로고
    • Hydroxyl radical scavenging activity of a new ophthalmic viscosurgical device
    • F. Maugeri, A. Maltese, K.W. Ward, and C. Bucolo Hydroxyl radical scavenging activity of a new ophthalmic viscosurgical device Curr Eye Res 32 2007 105 111
    • (2007) Curr Eye Res , vol.32 , pp. 105-111
    • Maugeri, F.1    Maltese, A.2    Ward, K.W.3    Bucolo, C.4
  • 24
    • 0000626067 scopus 로고
    • Antioxidative activities of browning products of glucosamine fractionated by organic solvent and thin-layer chromatography
    • M. Oyaizu Antioxidative activities of browning products of glucosamine fractionated by organic solvent and thin-layer chromatography J Jpn Soc Food Sci Technol 35 1988 771 775
    • (1988) J Jpn Soc Food Sci Technol , vol.35 , pp. 771-775
    • Oyaizu, M.1
  • 25
    • 33748431810 scopus 로고    scopus 로고
    • Antioxidant activity of zein hydrolysates in a liposome system and the possible mode of action
    • B.H. Kong, and Y.L.L. Xiong Antioxidant activity of zein hydrolysates in a liposome system and the possible mode of action Food Chem 54 2006 6059 6068
    • (2006) Food Chem , vol.54 , pp. 6059-6068
    • Kong, B.H.1    Xiong, Y.L.L.2
  • 27
    • 46049116527 scopus 로고    scopus 로고
    • In vitro antioxidant activity of protein hydrolysates prepared from corn gluten meal
    • X.X. Li, L.J. Han, and L.J. Chen In vitro antioxidant activity of protein hydrolysates prepared from corn gluten meal J Sci Food Agric 88 2008 1660 1666
    • (2008) J Sci Food Agric , vol.88 , pp. 1660-1666
    • Li, X.X.1    Han, L.J.2    Chen, L.J.3
  • 28
    • 1942424985 scopus 로고    scopus 로고
    • Preparation of corn gluten hydrolysate with angiotensin i converting enzyme inhibitory activity and its solubility and moisture sorption
    • J.M. Kim, J.H. Whang, K.M. Kim, J.H. Koh, and H.J. Suh Preparation of corn gluten hydrolysate with angiotensin I converting enzyme inhibitory activity and its solubility and moisture sorption Process Biochem 39 2004 989 994
    • (2004) Process Biochem , vol.39 , pp. 989-994
    • Kim, J.M.1    Whang, J.H.2    Kim, K.M.3    Koh, J.H.4    Suh, H.J.5
  • 29
    • 0343263093 scopus 로고
    • Enzymatic hydrolysis of corn gluten meal
    • J.E. Hardwick, and C.E. Glatz Enzymatic hydrolysis of corn gluten meal J Agric Food Chem 37 1989 1188 1192
    • (1989) J Agric Food Chem , vol.37 , pp. 1188-1192
    • Hardwick, J.E.1    Glatz, C.E.2
  • 31
    • 84906779321 scopus 로고    scopus 로고
    • Enzymatic hydrolysis of corn gluten meal
    • L. Lin, and Y. Ma Enzymatic hydrolysis of corn gluten meal Food Ind 4 2003 38 39
    • (2003) Food Ind , vol.4 , pp. 38-39
    • Lin, L.1    Ma, Y.2
  • 32
    • 77951925904 scopus 로고    scopus 로고
    • The separation, purification and antioxidative activity of corn peptide
    • Y.F. Dai, Z.Y. He, J. Chen, G.J. Tao, and F. Qin The separation, purification and antioxidative activity of corn peptide Food Mach 24 2008 5 8
    • (2008) Food Mach , vol.24 , pp. 5-8
    • Dai, Y.F.1    He, Z.Y.2    Chen, J.3    Tao, G.J.4    Qin, F.5
  • 33
    • 0038012771 scopus 로고    scopus 로고
    • Antioxidant activity of peptides obtained from porcine myofibrillar proteins by protease treatment
    • A. Saiga, S. Tanabe, and T. Nishimura Antioxidant activity of peptides obtained from porcine myofibrillar proteins by protease treatment J Agric Food Chem 51 2003 3661 3667
    • (2003) J Agric Food Chem , vol.51 , pp. 3661-3667
    • Saiga, A.1    Tanabe, S.2    Nishimura, T.3
  • 34
    • 0038689280 scopus 로고    scopus 로고
    • Antioxidative properties of tripeptide libraries prepared by the combinatorial chemistry
    • K. Saito, D.H. Jin, T. Ogawa, K. Muramoto, E. Hatakeyama, and T. Yasuhara et al. Antioxidative properties of tripeptide libraries prepared by the combinatorial chemistry J Agric Food Chem 51 2003 3668 3674
    • (2003) J Agric Food Chem , vol.51 , pp. 3668-3674
    • Saito, K.1    Jin, D.H.2    Ogawa, T.3    Muramoto, K.4    Hatakeyama, E.5    Yasuhara, T.6
  • 35
    • 84878316004 scopus 로고    scopus 로고
    • Production and purification of antioxidant peptides from a mungbean meal hydrolysate by Virgibacillus sp. SK37 proteinase
    • N. Lapsongphon, and J. Yongsawatdigul Production and purification of antioxidant peptides from a mungbean meal hydrolysate by Virgibacillus sp. SK37 proteinase Food Chem 141 2013 992 999
    • (2013) Food Chem , vol.141 , pp. 992-999
    • Lapsongphon, N.1    Yongsawatdigul, J.2
  • 36
    • 23944469378 scopus 로고    scopus 로고
    • Purification and in vitro antioxidative effects of giant squid muscle peptides on free radical-mediated oxidative systems
    • N. Rajapakse, E. Mendis, H.G. Byun, and S.K. Kim Purification and in vitro antioxidative effects of giant squid muscle peptides on free radical-mediated oxidative systems J Nutr Biochem 16 2005 562 569
    • (2005) J Nutr Biochem , vol.16 , pp. 562-569
    • Rajapakse, N.1    Mendis, E.2    Byun, H.G.3    Kim, S.K.4
  • 37
    • 0017612704 scopus 로고
    • Protein absorption-then and now
    • D.M. Matthews Protein absorption-then and now Gastroenterology 73 1977 1267 1279
    • (1977) Gastroenterology , vol.73 , pp. 1267-1279
    • Matthews, D.M.1
  • 38
    • 84865258037 scopus 로고    scopus 로고
    • The primary structure identification of a corn peptide facilitating alcohol metabolism by HPLC-MS/MS
    • Z.L. Ma, W.J. Zhang, G.C. Yu, H. He, and Y. Zhang The primary structure identification of a corn peptide facilitating alcohol metabolism by HPLC-MS/MS Peptides 37 2012 138 143
    • (2012) Peptides , vol.37 , pp. 138-143
    • Ma, Z.L.1    Zhang, W.J.2    Yu, G.C.3    He, H.4    Zhang, Y.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.