메뉴 건너뛰기




Volumn 71, Issue 2, 2016, Pages 174-182

Antithrombotic and Antioxidant Activity of Amaranth Hydrolysate Obtained by Activation of an Endogenous Protease

Author keywords

Amaranth proteins; Antithrombotic and antioxidant activity; Bioactive peptides; Endogenous aspartic protease

Indexed keywords

ANTIOXIDANT; ASPARTIC PROTEINASE; FIBRINOLYTIC AGENT; PEPTIDE; PLANT PROTEIN;

EID: 84962231891     PISSN: 09219668     EISSN: 15739104     Source Type: Journal    
DOI: 10.1007/s11130-016-0540-y     Document Type: Article
Times cited : (34)

References (35)
  • 3
    • 77949290825 scopus 로고    scopus 로고
    • Invited review: physiological properties of bioactive peptides obtained from whey proteins
    • COI: 1:CAS:528:DC%2BC3cXht1CjtrY%3D
    • Madureira AR, Tavares T, Gomes AMP, Pintado ME, Malcata FX (2010) Invited review: physiological properties of bioactive peptides obtained from whey proteins. J Dairy Sci 93:437–455
    • (2010) J Dairy Sci , vol.93 , pp. 437-455
    • Madureira, A.R.1    Tavares, T.2    Gomes, A.M.P.3    Pintado, M.E.4    Malcata, F.X.5
  • 4
    • 77349090649 scopus 로고    scopus 로고
    • Development and biological activities of marine-derived bioactive peptides: a review
    • COI: 1:CAS:528:DC%2BC3cXhsF2gurfK
    • Kim SK, Wijesekara I (2010) Development and biological activities of marine-derived bioactive peptides: a review. J Funct Foods 2:1–9
    • (2010) J Funct Foods , vol.2 , pp. 1-9
    • Kim, S.K.1    Wijesekara, I.2
  • 5
    • 84856032752 scopus 로고    scopus 로고
    • Food protein-derived bioactive peptides: production, processing, and potential health benefits
    • Udenigwe CC, Aluko RE (2012) Food protein-derived bioactive peptides: production, processing, and potential health benefits. J Food Sci 77:11–24
    • (2012) J Food Sci , vol.77 , pp. 11-24
    • Udenigwe, C.C.1    Aluko, R.E.2
  • 7
    • 84887891337 scopus 로고    scopus 로고
    • Biochemical and molecular study of the influence of Amaranthus hypochondriacus flour on serum and liver lipids in rats treated with ethanol
    • López VRL, Razzeto GS, Escudero NL, Giménez MS (2013) Biochemical and molecular study of the influence of Amaranthus hypochondriacus flour on serum and liver lipids in rats treated with ethanol. Plant Foods Hum Nutr 68:396–402
    • (2013) Plant Foods Hum Nutr , vol.68 , pp. 396-402
    • López, V.R.L.1    Razzeto, G.S.2    Escudero, N.L.3    Giménez, M.S.4
  • 8
    • 72149105882 scopus 로고    scopus 로고
    • Amaranth as a source of antioxidant peptides: effect of proteolysis
    • COI: 1:CAS:528:DC%2BD1MXhs1WgsLnK
    • Tironi V, Añón MC (2010) Amaranth as a source of antioxidant peptides: effect of proteolysis. Food Res Int 43:315–322
    • (2010) Food Res Int , vol.43 , pp. 315-322
    • Tironi, V.1    Añón, M.C.2
  • 9
    • 84922017124 scopus 로고    scopus 로고
    • Potential antithrombotic activity detected in amaranth proteins and its hydrolysates
    • COI: 1:CAS:528:DC%2BC2cXhtlKmtbzP
    • Sabbione AC, Scilingo A, Añón MC (2015) Potential antithrombotic activity detected in amaranth proteins and its hydrolysates. LWT-Food Sci Technol 60:171–177
    • (2015) LWT-Food Sci Technol , vol.60 , pp. 171-177
    • Sabbione, A.C.1    Scilingo, A.2    Añón, M.C.3
  • 10
    • 84860562490 scopus 로고    scopus 로고
    • Effect of acid treatment on structural and foaming properties of soy amaranth protein mixtures
    • COI: 1:CAS:528:DC%2BC38XnslSnur0%3D
    • Ventureira JL, Martínez EN, Añón MC (2012) Effect of acid treatment on structural and foaming properties of soy amaranth protein mixtures. Food Hydrocoll 29:272–279
    • (2012) Food Hydrocoll , vol.29 , pp. 272-279
    • Ventureira, J.L.1    Martínez, E.N.2    Añón, M.C.3
  • 11
    • 18644368723 scopus 로고    scopus 로고
    • Changes in the metabolism of protein during germination of sesame (Sesamum indicum L.) seeds
    • Hemalatha KPJ, Siva Prasad D (2003) Changes in the metabolism of protein during germination of sesame (Sesamum indicum L.) seeds. Plant Foods Hum Nutr 58:1–10
    • (2003) Plant Foods Hum Nutr , vol.58 , pp. 1-10
    • Hemalatha, K.P.J.1    Siva Prasad, D.2
  • 12
    • 11844252119 scopus 로고    scopus 로고
    • A cut above the rest: the regulatory function of plant proteases
    • COI: 1:CAS:528:DC%2BD2cXhtVensrfK
    • Schaller A (2004) A cut above the rest: the regulatory function of plant proteases. Planta 220:183–197
    • (2004) Planta , vol.220 , pp. 183-197
    • Schaller, A.1
  • 13
    • 2542574202 scopus 로고    scopus 로고
    • Composition and structural characterization of amaranth proteins isolates. An electrophoretic and calorimetric study
    • Martínez EN, Añón MC (1996) Composition and structural characterization of amaranth proteins isolates. An electrophoretic and calorimetric study. J Agric Food Chem 44:2523–2530
    • (1996) J Agric Food Chem , vol.44 , pp. 2523-2530
    • Martínez, E.N.1    Añón, M.C.2
  • 15
  • 16
    • 34248679167 scopus 로고    scopus 로고
    • Tricine-SDS-PAGE
    • Schägger H (2006) Tricine-SDS-PAGE. Nat Protoc 1:16–22
    • (2006) Nat Protoc , vol.1 , pp. 16-22
    • Schägger, H.1
  • 17
    • 0034879009 scopus 로고    scopus 로고
    • Improved method for determining food protein degree of hydrolysis
    • COI: 1:CAS:528:DC%2BD3MXmtVCqurs%3D
    • Nielsen PM, Petersen D, Dambmann C (2001) Improved method for determining food protein degree of hydrolysis. J Food Sci 66:642–646
    • (2001) J Food Sci , vol.66 , pp. 642-646
    • Nielsen, P.M.1    Petersen, D.2    Dambmann, C.3
  • 18
    • 71849104860 scopus 로고
    • Protein measurement with the folin phenol reagent
    • COI: 1:CAS:528:DyaG38XhsVyrsw%3D%3D
    • Lowry OH, Rosebrough NJ, Farr AL, Randall RJ (1951) Protein measurement with the folin phenol reagent. J Biol Chem 193:265–275
    • (1951) J Biol Chem , vol.193 , pp. 265-275
    • Lowry, O.H.1    Rosebrough, N.J.2    Farr, A.L.3    Randall, R.J.4
  • 19
    • 33947581389 scopus 로고    scopus 로고
    • A new method for determination of antithrombotic activity of egg white protein hydrolysate by microplate reader
    • COI: 1:CAS:528:DC%2BD2sXlvFGjsbw%3D
    • Yang WG, Wang Z, Xu SY (2007) A new method for determination of antithrombotic activity of egg white protein hydrolysate by microplate reader. Chin Chem Lett 18:449–451
    • (2007) Chin Chem Lett , vol.18 , pp. 449-451
    • Yang, W.G.1    Wang, Z.2    Xu, S.Y.3
  • 20
    • 43449124979 scopus 로고    scopus 로고
    • Antioxidant and antithrombotic activities of rapeseed peptides
    • COI: 1:CAS:528:DC%2BD1cXlvVChuro%3D
    • Zhang S, Wang Z, Xu SY (2008) Antioxidant and antithrombotic activities of rapeseed peptides. JAOCS 85:521–527
    • (2008) JAOCS , vol.85 , pp. 521-527
    • Zhang, S.1    Wang, Z.2    Xu, S.Y.3
  • 21
    • 84923848851 scopus 로고    scopus 로고
    • Amaranth peptides from simulated gastrointestinal digestion: antioxidant activity against reactive species
    • Orsini Delgado MC, Galleano M, Añón MC, Tironi VA (2015) Amaranth peptides from simulated gastrointestinal digestion: antioxidant activity against reactive species. Plant Foods Hum Nutr 70:27–34
    • (2015) Plant Foods Hum Nutr , vol.70 , pp. 27-34
    • Orsini Delgado, M.C.1    Galleano, M.2    Añón, M.C.3    Tironi, V.A.4
  • 22
    • 33646499887 scopus 로고    scopus 로고
    • The antioxidant activity and free radical-scavenging capacity of phenolics of raw and dry heated moth bean (Vigna aconitifolia) (jacq.) marechal seed extracts
    • COI: 1:CAS:528:DC%2BD28XjslygsLw%3D
    • Siddhuraju P (2006) The antioxidant activity and free radical-scavenging capacity of phenolics of raw and dry heated moth bean (Vigna aconitifolia) (jacq.) marechal seed extracts. Food Chem 99:149–157
    • (2006) Food Chem , vol.99 , pp. 149-157
    • Siddhuraju, P.1
  • 23
    • 62549165125 scopus 로고    scopus 로고
    • Synthetic and natural peptides as antithrombotic agents. A view on the current development
    • COI: 1:CAS:528:DC%2BD1MXkt1ems7c%3D
    • Atanassov A, Tchorbanov B (2009) Synthetic and natural peptides as antithrombotic agents. A view on the current development. Biotechnol Biotechnol Equip 23:1109–1114
    • (2009) Biotechnol Biotechnol Equip , vol.23 , pp. 1109-1114
    • Atanassov, A.1    Tchorbanov, B.2
  • 24
    • 77957596321 scopus 로고    scopus 로고
    • Influence of pH on structure and function of amaranth (A. hypochondriacus) protein isolates
    • COI: 1:CAS:528:DC%2BC3cXht1WmsLbL
    • Abugoch LE, Martínez EN, Añón MC (2010) Influence of pH on structure and function of amaranth (A. hypochondriacus) protein isolates. Cereal Chem 87:448–453
    • (2010) Cereal Chem , vol.87 , pp. 448-453
    • Abugoch, L.E.1    Martínez, E.N.2    Añón, M.C.3
  • 25
    • 71749110914 scopus 로고    scopus 로고
    • A method to describe enzyme-catalyzed reactions by combining steady state and time course enzyme kinetic parameters
    • COI: 1:CAS:528:DC%2BD1MXhsV2lur%2FF
    • Walsh R, Martin E, Darvesh S (2010) A method to describe enzyme-catalyzed reactions by combining steady state and time course enzyme kinetic parameters. Biochim Biophys Acta 1800:1–5
    • (2010) Biochim Biophys Acta , vol.1800 , pp. 1-5
    • Walsh, R.1    Martin, E.2    Darvesh, S.3
  • 27
    • 0043265957 scopus 로고    scopus 로고
    • A comparative study of functional properties of amaranth and soybean globulins isolates
    • COI: 1:CAS:528:DC%2BD3cXhtVWls7w%3D
    • Marcone MF, Kakuda Y (1999) A comparative study of functional properties of amaranth and soybean globulins isolates. Nahrung 43:368–373
    • (1999) Nahrung , vol.43 , pp. 368-373
    • Marcone, M.F.1    Kakuda, Y.2
  • 29
    • 0000946077 scopus 로고
    • Synthetic peptide derivatives that bind to fibrinogen and prevent the polymerization of fibrin monomers
    • COI: 1:CAS:528:DyaE1cXlsFyqurY%3D
    • Laudano AP, Doolittle RF (1978) Synthetic peptide derivatives that bind to fibrinogen and prevent the polymerization of fibrin monomers. Proc Natl Acad Sci USA 75:3085–3089
    • (1978) Proc Natl Acad Sci USA , vol.75 , pp. 3085-3089
    • Laudano, A.P.1    Doolittle, R.F.2
  • 30
    • 5444228406 scopus 로고    scopus 로고
    • SSGE and DEE, new peptides isolated from a soy protein hydrolysate that inhibit platelet aggregation
    • COI: 1:CAS:528:DC%2BD2cXosFSksLY%3D
    • Lee KA, Kim SH (2005) SSGE and DEE, new peptides isolated from a soy protein hydrolysate that inhibit platelet aggregation. Food Chem 90:389–394
    • (2005) Food Chem , vol.90 , pp. 389-394
    • Lee, K.A.1    Kim, S.H.2
  • 31
    • 33646786738 scopus 로고    scopus 로고
    • Isolation and characterization of a novel platelet aggregation inhibitory peptide from the medicinal mushroom, Inonotus obliquus
    • COI: 1:CAS:528:DC%2BD28XltFOgt7c%3D
    • Hyun KW, Jeong SC, Lee DH, Park JS, Lee JS (2006) Isolation and characterization of a novel platelet aggregation inhibitory peptide from the medicinal mushroom, Inonotus obliquus. Peptides 27:1173–1178
    • (2006) Peptides , vol.27 , pp. 1173-1178
    • Hyun, K.W.1    Jeong, S.C.2    Lee, D.H.3    Park, J.S.4    Lee, J.S.5
  • 32
    • 38049089877 scopus 로고    scopus 로고
    • Purification and characterization of a novel anticoagulant peptide from marine echiuroid worm Urechis unicinctus
    • COI: 1:CAS:528:DC%2BD1cXpt1Ogtg%3D%3D
    • Jo HY, Jung WK, Kim SK (2008) Purification and characterization of a novel anticoagulant peptide from marine echiuroid worm Urechis unicinctus. Process Biochem 43:179–184
    • (2008) Process Biochem , vol.43 , pp. 179-184
    • Jo, H.Y.1    Jung, W.K.2    Kim, S.K.3
  • 33
    • 0024206252 scopus 로고
    • Echistatin, a potent platelet aggregation inhibitor from venom of viper, Echis carinatus
    • COI: 1:CAS:528:DyaL1MXjsFSkuw%3D%3D
    • Gan ZR, Gould RJ, Jacobs JW, Freidman PA, Polokoff MA (1988) Echistatin, a potent platelet aggregation inhibitor from venom of viper, Echis carinatus. J Biol Chem 263:19827–19832
    • (1988) J Biol Chem , vol.263 , pp. 19827-19832
    • Gan, Z.R.1    Gould, R.J.2    Jacobs, J.W.3    Freidman, P.A.4    Polokoff, M.A.5
  • 34
    • 0032982508 scopus 로고    scopus 로고
    • Antioxidant activity applying an improved ABTS radical cation decolorization assay
    • COI: 1:CAS:528:DyaK1MXjvVakt7o%3D
    • Re R, Pellegrini A, Proteggente A, Pannala M, Yang C, Rice-Evans C (1999) Antioxidant activity applying an improved ABTS radical cation decolorization assay. Free Radic Biol Med 26:1231–1237
    • (1999) Free Radic Biol Med , vol.26 , pp. 1231-1237
    • Re, R.1    Pellegrini, A.2    Proteggente, A.3    Pannala, M.4    Yang, C.5    Rice-Evans, C.6
  • 35
    • 79956314937 scopus 로고    scopus 로고
    • Antioxidant activity of amaranth protein or their hydrolysates under simulated gastrointestinal digestion
    • COI: 1:CAS:528:DC%2BC3MXmslOktr4%3D
    • Orsini Delgado MC, Tironi VA, Añón MC (2011) Antioxidant activity of amaranth protein or their hydrolysates under simulated gastrointestinal digestion. LWT 44:1752–1760
    • (2011) LWT , vol.44 , pp. 1752-1760
    • Orsini Delgado, M.C.1    Tironi, V.A.2    Añón, M.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.