메뉴 건너뛰기




Volumn 135, Issue 3, 2012, Pages 1789-1795

Antioxidant and metal chelating activities of peptide fractions from phaseolin and bean protein hydrolysates

Author keywords

Antioxidant activity; Chelating activity; Phaseolin; Phaseolus vulgaris; Protein isolate

Indexed keywords

ANTIOXIDANT ACTIVITIES; CHELATING ACTIVITY; PHASEOLIN; PHASEOLUS VULGARIS; PROTEIN ISOLATES;

EID: 84865790385     PISSN: 03088146     EISSN: 18737072     Source Type: Journal    
DOI: 10.1016/j.foodchem.2012.06.016     Document Type: Article
Times cited : (211)

References (34)
  • 1
    • 0018536145 scopus 로고
    • Determination of the degree of hydrolysis of food protein hydrolysates by trinitrobenzensulfonic acid
    • J. Adler-Nissen Determination of the degree of hydrolysis of food protein hydrolysates by trinitrobenzensulfonic acid Journal of Agricultural and Food Chemistry 27 1979 1256 1262
    • (1979) Journal of Agricultural and Food Chemistry , vol.27 , pp. 1256-1262
    • Adler-Nissen, J.1
  • 2
    • 84986513721 scopus 로고
    • Antioxidant activity and total phenolics in different genotypes of potato (Solanum tuberosum L.)
    • M.S. Al-Saikhan, L.R. Howard, and J.C. Miller Antioxidant activity and total phenolics in different genotypes of potato (Solanum tuberosum L.) Journal of Food Science 60 2 1995 341 343
    • (1995) Journal of Food Science , vol.60 , Issue.2 , pp. 341-343
    • Al-Saikhan, M.S.1    Howard, L.R.2    Miller, J.C.3
  • 3
    • 0026569401 scopus 로고
    • Amino acid analysis by high-performance liquid chromatography after derivatization with diethyl ethoxymethylenemalonate
    • M. Alaiz, J.L. Navarro, J. Girón, and E. Vioque Amino acid analysis by high-performance liquid chromatography after derivatization with diethyl ethoxymethylenemalonate Journal of Chromatography A 591 1-2 1992 181 186
    • (1992) Journal of Chromatography A , vol.591 , Issue.12 , pp. 181-186
    • Alaiz, M.1    Navarro, J.L.2    Girón, J.3    Vioque, E.4
  • 4
    • 70349952477 scopus 로고    scopus 로고
    • Anti-oxidative capacity of enzymatically released peptides from soybean protein isolate
    • C. Beermann, M. Euler, J. Herzberg, and B. Stahl Anti-oxidative capacity of enzymatically released peptides from soybean protein isolate European Food Research and Technology 229 4 2009 637 644
    • (2009) European Food Research and Technology , vol.229 , Issue.4 , pp. 637-644
    • Beermann, C.1    Euler, M.2    Herzberg, J.3    Stahl, B.4
  • 5
    • 75449086814 scopus 로고    scopus 로고
    • Minor components of pulses and their potential impact on human health
    • R. Campos-Vega, G. Loarca-Piña, and B.D. Oomah Minor components of pulses and their potential impact on human health Food Research International 43 2 2010 461 482
    • (2010) Food Research International , vol.43 , Issue.2 , pp. 461-482
    • Campos-Vega, R.1    Loarca-Piña, G.2    Oomah, B.D.3
  • 7
    • 0015040637 scopus 로고
    • Spectrophotometric determination of serum iron at the submicrogram level with a new reagent (ferrozine)
    • P. Carter Spectrophotometric determination of serum iron at the submicrogram level with a new reagent (ferrozine) Analytical Biochemistry 40 2 1971 450 458
    • (1971) Analytical Biochemistry , vol.40 , Issue.2 , pp. 450-458
    • Carter, P.1
  • 9
    • 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 Journal of Agricultural and Food Chemistry 44 9 1996 2619 2623 (Pubitemid 126453550)
    • (1996) Journal of Agricultural and Food Chemistry , vol.44 , Issue.9 , pp. 2619-2623
    • Chen, H.-M.1    Muramoto, K.2    Yamauchi, F.3    Nokihara, K.4
  • 10
    • 76149092811 scopus 로고    scopus 로고
    • Health-promoting activities of ultra-filtered okara protein hydrolysates released by in vitro gastrointestinal digestion: Identification of active peptide from soybean lipoxygenase
    • A. Jiménez-Escrig, M. Alaiz, J. Vioque, and P. Rupérez Health-promoting activities of ultra-filtered okara protein hydrolysates released by in vitro gastrointestinal digestion: identification of active peptide from soybean lipoxygenase European Food Research and Technology 230 4 2010 655 663
    • (2010) European Food Research and Technology , vol.230 , Issue.4 , pp. 655-663
    • Jiménez-Escrig, A.1    Alaiz, M.2    Vioque, J.3    Rupérez, P.4
  • 12
    • 33748431810 scopus 로고    scopus 로고
    • Antioxidant activity of zein hydrolysates in a liposome system and the possible mode of action
    • DOI 10.1021/jf060632q
    • B. Kong, and Y.L. Xiong Antioxidant activity of zein hydrolysates in a liposome system and the possible mode of action Journal of Agricultural and Food Chemistry 54 16 2006 6059 6068 (Pubitemid 44342243)
    • (2006) Journal of Agricultural and Food Chemistry , vol.54 , Issue.16 , pp. 6059-6068
    • Kong, B.1    Xiong, Y.L.2
  • 13
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 5259 1970 680 685
    • (1970) Nature , vol.227 , Issue.5259 , pp. 680-685
    • Laemmli, U.K.1
  • 14
    • 0028361114 scopus 로고
    • Structure of phaseolin at 2·2 Å resolution: Implications for a common vicilin/legumin structure and the genetic engineering of seed storage proteins
    • M.C. Lawrence, T. Izard, M. Beuchat, R.J. Blagrove, and P.M. Colman Structure of phaseolin at 2·2 Å resolution: implications for a common vicilin/legumin structure and the genetic engineering of seed storage proteins Journal of Molecular Biology 238 5 1994 748 776
    • (1994) Journal of Molecular Biology , vol.238 , Issue.5 , pp. 748-776
    • Lawrence, M.C.1    Izard, T.2    Beuchat, M.3    Blagrove, R.J.4    Colman, P.M.5
  • 19
    • 75149120104 scopus 로고    scopus 로고
    • Phaseolin diversity as a possible strategy to improve the nutritional value of common beans (Phaseolus vulgaris)
    • C.A. Montoya, J.-P. Lallès, S. Beebe, and P. Leterme Phaseolin diversity as a possible strategy to improve the nutritional value of common beans (Phaseolus vulgaris) Food Research International 43 2 2010 443 449
    • (2010) Food Research International , vol.43 , Issue.2 , pp. 443-449
    • Montoya, C.A.1    Lallès, J.-P.2    Beebe, S.3    Leterme, P.4
  • 20
    • 32844458708 scopus 로고    scopus 로고
    • Influence of the Phaseolus vulgaris phaseolin level of incorporation, type and thermal treatment on gut characteristics in rats
    • DOI 10.1079/BJN20051613
    • C.A. Montoya, J.-P. Lallés, S. Beebe, L. Montagne, W.B. Souffrant, and P. Leterme Influence of the Phaseolus vulgaris phaseolin level of incorporation, type and thermal treatment on gut characteristics in rats British Journal of Nutrition 95 01 2006 116 123 (Pubitemid 43250717)
    • (2006) British Journal of Nutrition , vol.95 , Issue.1 , pp. 116-123
    • Montoya, C.A.1    Lalles, J.-P.2    Beebe, S.3    Montagne, L.4    Souffrant, W.B.5    Leterme, P.6
  • 21
    • 41849092668 scopus 로고    scopus 로고
    • Susceptibility of phaseolin to in vitro proteolysis is highly variable across common bean varieties (Phaseolus vulgaris)
    • DOI 10.1021/jf072576e
    • C.A. Montoya, P. Leterme, N.F. Victoria, O. Toro, W.B. Souffrant, S. Beebe, and J.-P. Lallès Susceptibility of phaseolin to in vitro proteolysis is highly variable across common bean varieties (Phaseolus vulgaris) Journal of Agricultural and Food Chemistry 56 6 2008 2183 2191 (Pubitemid 351497884)
    • (2008) Journal of Agricultural and Food Chemistry , vol.56 , Issue.6 , pp. 2183-2191
    • Montoya, C.A.1    Leterme, P.2    Victoria, N.F.3    Toro, O.4    Souffrant, W.B.5    Beebe, S.6    Lalles, J.-P.7
  • 22
    • 0000209774 scopus 로고
    • Studies on product browning reaction prepared from glucose amine
    • M. Oyaizu Studies on product browning reaction prepared from glucose amine Japanese Journal of Nutrition 44 1968 307 315
    • (1968) Japanese Journal of Nutrition , vol.44 , pp. 307-315
    • Oyaizu, M.1
  • 23
    • 76749131572 scopus 로고    scopus 로고
    • Reducing and radical-scavenging activities of whey protein hydrolysates prepared with Alcalase
    • X. Peng, B. Kong, X. Xia, and Q. Liu Reducing and radical-scavenging activities of whey protein hydrolysates prepared with Alcalase International Dairy Journal 20 5 2010 360 365
    • (2010) International Dairy Journal , vol.20 , Issue.5 , pp. 360-365
    • Peng, X.1    Kong, B.2    Xia, X.3    Liu, Q.4
  • 24
    • 52949091925 scopus 로고    scopus 로고
    • Antioxidant activity of peptide fractions from whey protein hydrolysates as measured by electron spin resonance
    • X. Peng, Y.L. Xiong, and B. Kong Antioxidant activity of peptide fractions from whey protein hydrolysates as measured by electron spin resonance Food Chemistry 113 1 2009 196 201
    • (2009) Food Chemistry , vol.113 , Issue.1 , pp. 196-201
    • Peng, X.1    Xiong, Y.L.2    Kong, B.3
  • 25
    • 0032982508 scopus 로고    scopus 로고
    • Antioxidant activity applying an improved ABTS radical cation decolorization assay
    • DOI 10.1016/S0891-5849(98)00315-3, PII S0891584998003153
    • R. Re, N. Pellegrini, A. Proteggente, A. Pannala, M. Yang, and C. Rice-Evans Antioxidant activity applying an improved ABTS radical cation decolorization assay Free Radical Biology and Medicine 26 9-10 1999 1231 1237 (Pubitemid 29262709)
    • (1999) Free Radical Biology and Medicine , vol.26 , Issue.9-10 , pp. 1231-1237
    • Re, R.1    Pellegrini, N.2    Proteggente, A.3    Pannala, A.4    Yang, M.5    Rice-Evans, C.6
  • 26
    • 80051560567 scopus 로고    scopus 로고
    • Comparative study of the composition and thermal properties of protein isolates prepared from nine Phaseolus vulgaris legume varieties
    • X. Rui, J.I. Boye, S. Ribereau, B.K. Simpson, and S.O. Prasher Comparative study of the composition and thermal properties of protein isolates prepared from nine Phaseolus vulgaris legume varieties Food Research International 44 8 2011 2497 2504
    • (2011) Food Research International , vol.44 , Issue.8 , pp. 2497-2504
    • Rui, X.1    Boye, J.I.2    Ribereau, S.3    Simpson, B.K.4    Prasher, S.O.5
  • 27
    • 84874023015 scopus 로고    scopus 로고
    • Angiotensin I-converting enzyme inhibitory and antioxidant peptide fractions from hard-to-cook bean enzymatic hydrolysates
    • Ruiz-Ruiz, J., Dávila-Ortíz, G., Chel-Guerrero, L., & Betancur-Ancona, D. (2011). Angiotensin I-converting enzyme inhibitory and antioxidant peptide fractions from hard-to-cook bean enzymatic hydrolysates. Journal of Food Biochemistry.
    • (2011) Journal of Food Biochemistry
    • Ruiz-Ruiz, J.1    Dávila-Ortíz, G.2    Chel-Guerrero, L.3    Betancur-Ancona, D.4
  • 28
    • 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 Journal of Agricultural and Food Chemistry 51 12 2003 3661 3667
    • (2003) Journal of Agricultural and Food Chemistry , vol.51 , Issue.12 , pp. 3661-3667
    • Saiga, A.1    Tanabe, S.2    Nishimura, T.3
  • 29
    • 77956688199 scopus 로고    scopus 로고
    • Antioxidative peptides from food proteins: A review
    • B.H. Sarmadi, and A. Ismail Antioxidative peptides from food proteins: A review Peptides 31 10 2010 1949 1956
    • (2010) Peptides , vol.31 , Issue.10 , pp. 1949-1956
    • Sarmadi, B.H.1    Ismail, A.2
  • 30
    • 79959948783 scopus 로고    scopus 로고
    • Affinity purification and characterisation of chelating peptides from chickpea protein hydrolysates
    • C. Torres-Fuentes, M. Alaiz, and J. Vioque Affinity purification and characterisation of chelating peptides from chickpea protein hydrolysates Food Chemistry 129 2 2011 485 490
    • (2011) Food Chemistry , vol.129 , Issue.2 , pp. 485-490
    • Torres-Fuentes, C.1    Alaiz, M.2    Vioque, J.3
  • 32
    • 51749125669 scopus 로고    scopus 로고
    • Antioxidant activity of peptides isolated from alfalfa leaf protein hydrolysate
    • Z. Xie, J. Huang, X. Xu, and Z. Jin Antioxidant activity of peptides isolated from alfalfa leaf protein hydrolysate Food Chemistry 111 2 2008 370 376
    • (2008) Food Chemistry , vol.111 , Issue.2 , pp. 370-376
    • Xie, Z.1    Huang, J.2    Xu, X.3    Jin, Z.4
  • 33
    • 0346219390 scopus 로고    scopus 로고
    • Determination of tryptophan by high-performance liquid chromatography of alkaline hydrolysates with spectrophotometric detection
    • DOI 10.1016/j.foodchem.2003.07.026
    • M.M. Yust, J. Pedroche, J. Girón-Calle, J. Vioque, F. Millán, and M. Alaiz Determination of tryptophan by high-performance liquid chromatography of alkaline hydrolysates with spectrophotometric detection Food Chemistry 85 2 2004 317 320 (Pubitemid 37532707)
    • (2004) Food Chemistry , vol.85 , Issue.2 , pp. 317-320
    • Yust, M.M.1    Pedroche, J.2    Giron-Calle, J.3    Vioque, J.4    Millan, F.5    Alaiz, M.6
  • 34
    • 43649092437 scopus 로고    scopus 로고
    • Reducing, radical scavenging, and chelation properties of in vitro digests of alcalase-treated zein hydrolysate
    • DOI 10.1021/jf703697e
    • L. Zhu, J. Chen, X. Tang, and Y.L. Xiong Reducing, radical scavenging, and chelation properties of in vitro digests of alcalase-treated zein hydrolysate Journal of Agricultural and Food Chemistry 56 8 2008 2714 2721 (Pubitemid 351685216)
    • (2008) Journal of Agricultural and Food Chemistry , vol.56 , Issue.8 , pp. 2714-2721
    • Zhu, L.1    Jie, C.2    Tang, X.3    Xiong, Y.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.