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Volumn 15, Issue 11, 2014, Pages 21120-21135

Bioactive peptides in cereals and legumes: Agronomical, biochemical and clinical aspects

Author keywords

Agronomical aspects; Bioactive peptides; Biological activities; Cereals; Clinical aspects; Legumes

Indexed keywords

CHYMOTRYPSIN; LECTIN; NUTRACEUTICAL; TRYPSIN; ANTIINFLAMMATORY AGENT; ANTINEOPLASTIC AGENT; ANTIOXIDANT; CARDIOVASCULAR AGENT; PEPTIDE;

EID: 84910123375     PISSN: 16616596     EISSN: 14220067     Source Type: Journal    
DOI: 10.3390/ijms151121120     Document Type: Review
Times cited : (150)

References (87)
  • 2
    • 84857098140 scopus 로고    scopus 로고
    • Selected lactic acid bacteria synthesize antioxidant peptides during sourdough fermentation of cereal flours. Appl. Environ
    • Coda, R.; Rizzello, C.G.; Pinto, D.; Gobbetti, M. Selected lactic acid bacteria synthesize antioxidant peptides during sourdough fermentation of cereal flours. Appl. Environ. Microbiol. 2012, 78, 1087-1096.
    • (2012) Microbiol , vol.78 , pp. 1087-1096
    • Coda, R.1    Rizzello, C.G.2    Pinto, D.3    Gobbetti, M.4
  • 4
    • 84889675077 scopus 로고    scopus 로고
    • Potential of bioactive proteins and peptides for prevention and treatment of mass non-communicable dieseases
    • Belovic, M.M.; Mastilović, J.S.; Torbica, A.L.; Tomić, J.M.; Stanić, D.R.; Džinić, N.R. Potential of bioactive proteins and peptides for prevention and treatment of mass non-communicable dieseases. Food Feed Res. 2011, 38, 51-61.
    • (2011) Food Feed Res , vol.38 , pp. 51-61
    • Belovic, M.M.1    Mastilović, J.S.2    Torbica, A.L.3    Tomić, J.M.4    Stanić, D.R.5    Džinić, N.R.6
  • 5
    • 84910044710 scopus 로고    scopus 로고
    • Preventive and therapeutic potential of peptides from cereals against cancer
    • Ortiz-Martinez, M.; Winkler, R.; Garcia-Lara, S. Preventive and therapeutic potential of peptides from cereals against cancer. J. Proteomics 2014, doi:10.1016/j.jprot.2014.03.044.
    • (2014) J. Proteomics
    • Ortiz-Martinez, M.1    Winkler, R.2    Garcia-Lara, S.3
  • 6
    • 78249282622 scopus 로고    scopus 로고
    • Lunasin is prevalent in barley and is bioavailable and bioactive in vivo and in vitro studies. Nutr
    • Jeong, H.J.; Jeong, J.B.; Hsieh, C.C.; Hernandez-Ledesma, B.; de Lumen, B.O. Lunasin is prevalent in barley and is bioavailable and bioactive in vivo and in vitro studies. Nutr. Cancer 2010, 62, 1113-1119.
    • (2010) Cancer , vol.62 , pp. 1113-1119
    • Jeong, H.J.1    Jeong, J.B.2    Hsieh, C.C.3    Hernandez-Ledesma, B.4    De Lumen, B.O.5
  • 8
    • 70449635964 scopus 로고    scopus 로고
    • The preventive seed peptide lunasin from rye is bioavailable and bioactive. Nutr
    • Jeong, H.J.; Lee, J.R.; Jeong, J.B.; Park J.H.; Cheong, Y.K.; de Lumen, B.O. The preventive seed peptide lunasin from rye is bioavailable and bioactive. Nutr. Cancer 2009, 61, 680-686.
    • (2009) Cancer , vol.61 , pp. 680-686
    • Jeong, H.J.1    Lee, J.R.2    Jeong, J.B.3    Park, J.H.4    Cheong, Y.K.5    De Lumen, B.O.6
  • 9
    • 27144441748 scopus 로고    scopus 로고
    • Contents and bioactivities of lunasin, bowman-birk inhibitor, and isoflavones in soybean seed
    • Park, J.H.; Jeong, H.J.; de Lumen, B.O. Contents and bioactivities of lunasin, bowman-birk inhibitor, and isoflavones in soybean seed. J. Agric. Food Chem. 2005, 53, 7686-7690.
    • (2005) J. Agric. Food Chem , vol.53 , pp. 7686-7690
    • Park, J.H.1    Jeong, H.J.2    De Lumen, B.O.3
  • 12
    • 4644354405 scopus 로고    scopus 로고
    • Lunasin concentration in different soybean genotypes, commercial soy protein, and isoflavone products
    • De Mejia, E.G.; Vásconez, M.; de Lumen, B.O.; Nelson, R. Lunasin concentration in different soybean genotypes, commercial soy protein, and isoflavone products. J. Agric. Food Chem. 2004, 52, 5882-5887.
    • (2004) J. Agric. Food Chem , vol.52 , pp. 5882-5887
    • De Mejia, E.G.1    Vásconez, M.2    De Lumen, B.O.3    Nelson, R.4
  • 13
    • 58149505705 scopus 로고    scopus 로고
    • Lunasin, a novel seed peptide for cancer prevention
    • Hernandez-Ledesma, B.; Hsieh, C.C.; de Lumen, B.O. Lunasin, a novel seed peptide for cancer prevention. Peptides 2009, 30, 426-430.
    • (2009) Peptides , vol.30 , pp. 426-430
    • Hernandez-Ledesma, B.1    Hsieh, C.C.2    De Lumen, B.O.3
  • 14
    • 84883001778 scopus 로고    scopus 로고
    • Brown Kidney Bean Bowman-Birk Trypsin Inhibitor is Heat and pH Stable and Exhibits Anti-Proliferative Activity
    • Chan, Y.S.; Zhang, Y.; Ng, T.B. Brown Kidney Bean Bowman-Birk Trypsin Inhibitor is Heat and pH Stable and Exhibits Anti-Proliferative Activity. Appl. Biochem. Biotechnol. 2013, 169, 1306-1314.
    • (2013) Appl. Biochem. Biotechnol , vol.169 , pp. 1306-1314
    • Chan, Y.S.1    Zhang, Y.2    Ng, T.B.3
  • 15
    • 77957604071 scopus 로고    scopus 로고
    • The role of nutraceutical proteins and peptides in apoptosis, angiogenesis, and metastasis of cancer cells
    • De Mejia, E.G.; Dia, V.P. The role of nutraceutical proteins and peptides in apoptosis, angiogenesis, and metastasis of cancer cells. Cancer Metastasis Rev. 2010, 29, 511-528.
    • (2010) Cancer Metastasis Rev , vol.29 , pp. 511-528
    • De Mejia, E.G.1    Dia, V.P.2
  • 17
    • 33947384164 scopus 로고    scopus 로고
    • Influence of different genotypes on trypsin inhibitor levels and activity in soybeans
    • Pesic, M.; Vucelic-RAdovic, B.V.; Barac, M.B.; Stanojevic, S.P.; Nedovic, V.A. Influence of different genotypes on trypsin inhibitor levels and activity in soybeans. Sensors 2007, 7, 67-74.
    • (2007) Sensors , vol.7 , pp. 67-74
    • Pesic, M.1    Vucelic-Radovic, B.V.2    Barac, M.B.3    Stanojevic, S.P.4    Nedovic, V.A.5
  • 18
    • 84863565761 scopus 로고    scopus 로고
    • Growing location has a pronounced effect on the accumulation of cancer chemopreventive agent Bowman-Birk inhibitor in soybean seeds
    • Krishnan H.B.; Jang, S.; Baxter, I.; Wiebold, W. Growing location has a pronounced effect on the accumulation of cancer chemopreventive agent Bowman-Birk inhibitor in soybean seeds. Crop Sci. 2012, 52, 1786-1794.
    • (2012) Crop Sci , vol.52 , pp. 1786-1794
    • Krishnan, H.B.1    Jang, S.2    Baxter, I.3    Wiebold, W.4
  • 19
    • 0032964107 scopus 로고    scopus 로고
    • Soybean cDNA encoding a chromatin-binding peptide inhibits mitosis of mammalian cells
    • Galvez, A.F.; de Lumen, B.O. A soybean cDNA encoding a chromatin-binding peptide inhibits mitosis of mammalian cells. Nat. Biotechnol. 1999, 17, 495-500.
    • (1999) Nat. Biotechnol , vol.17 , pp. 495-500
    • Galvez, A.F.1    De Lumen, B.2
  • 20
    • 0035887086 scopus 로고    scopus 로고
    • Chemopreventive property of a soybean peptide (lunasin) that binds to deacetylated histones and inhibits acetylation
    • Galvez, A.F.; Chen, N.; Macasieb, J.; de Lumen, B.O. Chemopreventive property of a soybean peptide (lunasin) that binds to deacetylated histones and inhibits acetylation. Cancer Res. 2001, 61, 7473-7478.
    • (2001) Cancer Res , vol.61 , pp. 7473-7478
    • Galvez, A.F.1    Chen, N.2    Macasieb, J.3    De Lumen, B.O.4
  • 21
    • 1342301633 scopus 로고    scopus 로고
    • B.O. Lunasin suppresses E1A-mediated transformation of mammalian cells but does not inhibit growth of immortalized and established cancer cell lines
    • Lam, A.F.; Galvez, A.; de Lumen, B.O. Lunasin suppresses E1A-mediated transformation of mammalian cells but does not inhibit growth of immortalized and established cancer cell lines. Nutr. Cancer 2003, 47, 88-94.
    • (2003) Nutr. Cancer , vol.47 , pp. 88-94
    • Lam, A.F.1    Galvez, A.2    Lumen, D.3
  • 22
    • 0037048768 scopus 로고    scopus 로고
    • Barley lunasin suppresses ras-induced colony formation and inhibits core histone acetylation in mammalian cells
    • Jeong, H.J.; Lam, Y.; de Lumen, B.O. Barley lunasin suppresses ras-induced colony formation and inhibits core histone acetylation in mammalian cells. J. Agric. Food Chem. 2002, 50, 5903-5908.
    • (2002) J. Agric. Food Chem , vol.50 , pp. 5903-5908
    • Jeong, H.J.1    Lam, Y.2    De Lumen, B.O.3
  • 24
    • 77649321216 scopus 로고    scopus 로고
    • Lunasin, with an arginine-glycine-aspartic acid motif, causes apoptosis to L1210 leukemia cells by activation of caspase-3
    • De Mejia, E.G.; Wang, W.; Dia, V.P. Lunasin, with an arginine-glycine-aspartic acid motif, causes apoptosis to L1210 leukemia cells by activation of caspase-3. Mol. Nutr. Food Res. 2010, 54, 406-414.
    • (2010) Mol. Nutr. Food Res , vol.54 , pp. 406-414
    • De Mejia, E.G.1    Wang, W.2    Dia, V.P.3
  • 25
    • 77953622693 scopus 로고    scopus 로고
    • Lunasin promotes apoptosis in human colon cancer cells by mitochondrial pathway activation and induction of nuclear clusterin expression
    • Dia, V.P.; Mejia, E.G. Lunasin promotes apoptosis in human colon cancer cells by mitochondrial pathway activation and induction of nuclear clusterin expression. Cancer Lett. 2010, 295, 44-53.
    • (2010) Cancer Lett , vol.295 , pp. 44-53
    • Dia, V.P.1    Mejia, E.G.2
  • 26
    • 77955659706 scopus 로고    scopus 로고
    • Human cancer cell proliferation inhibition by a pentapeptide isolated and characterized from rice bran
    • Kannan, A.; Hettiarachchy, N.S.; Lay, J.O.; Liyanage, R. Human cancer cell proliferation inhibition by a pentapeptide isolated and characterized from rice bran. Peptides 2010, 31, 1629-1634.
    • (2010) Peptides , vol.31 , pp. 1629-1634
    • Kannan, A.1    Hettiarachchy, N.S.2    Lay, J.O.3    Liyanage, R.4
  • 27
    • 84899959826 scopus 로고    scopus 로고
    • Effects of an anticarcinogenic Bowman-Birk protease inhibitor on purified 20S proteasome and MCF-7 breast cancer cells
    • Souza Lda, C.; Camargo, R.; Demasi, M.; Santana, J.M.; de Sá, C.M.; de Freitas, S.M. Effects of an anticarcinogenic Bowman-Birk protease inhibitor on purified 20S proteasome and MCF-7 breast cancer cells. PLoS One 2014, 9, e86600.
    • (2014) Plos One , vol.9
    • Souza Lda, C.1    Camargo, R.2    Demasi, M.3    Santana, J.M.4    De Sá, C.M.5    De Freitas, S.M.6
  • 28
    • 22844434892 scopus 로고    scopus 로고
    • Bowman-Birk inhibitor abates proteasome function and suppresses the proliferation of MCF7 breast cancer cells through accumulation of MAP kinase phosphatase-1
    • Chen, Y.W.; Huang, S.C.; Lin-Shiau, S.Y.; Lin, J.K. Bowman-Birk inhibitor abates proteasome function and suppresses the proliferation of MCF7 breast cancer cells through accumulation of MAP kinase phosphatase-1. Carcinogenesis 2005, 26, 1296-1306.
    • (2005) Carcinogenesis , vol.26 , pp. 1296-1306
    • Chen, Y.W.1    Huang, S.C.2    Lin-Shiau, S.Y.3    Lin, J.K.4
  • 29
    • 34347344821 scopus 로고    scopus 로고
    • Negative growth control of osteosarcoma cell by Bowman-Birk protease inhibitor from soybean; involvement of connexin 43
    • Saito, T.; Sato, H.; Virgona, N.; Hagiwara, H.; Kashiwagi, K.; Suzuki, K.; Asano, R.; Yano, T. Negative growth control of osteosarcoma cell by Bowman-Birk protease inhibitor from soybean; involvement of connexin 43. Cancer Lett. 2007, 253, 249-257.
    • (2007) Cancer Lett , vol.253 , pp. 249-257
    • Saito, T.1    Sato, H.2    Virgona, N.3    Hagiwara, H.4    Kashiwagi, K.5    Suzuki, K.6    Asano, R.7    Yano, T.8
  • 30
    • 24744463417 scopus 로고    scopus 로고
    • Restoration of connexin 43 by Bowman-Birk protease inhibitor in M5076 bearing mice
    • Suzuki, K.; Yano, T.; Sadzuka, Y.; Sugiyama, T.; Seki, T.; Asano, R. Restoration of connexin 43 by Bowman-Birk protease inhibitor in M5076 bearing mice. Oncol. Rep. 2005, 13, 1247-1250.
    • (2005) Oncol. Rep , vol.13 , pp. 1247-1250
    • Suzuki, K.1    Yano, T.2    Sadzuka, Y.3    Sugiyama, T.4    Seki, T.5    Asano, R.6
  • 31
    • 33646441357 scopus 로고    scopus 로고
    • Bortezomib: Proteasome inhibition as an effective anticancer therapy
    • Richardson, P.G.; Mitsiades, C.; Hideshima, T.; Anderson, K.C. Bortezomib: Proteasome inhibition as an effective anticancer therapy. Future Oncol. 2005, 1, 161-171.
    • (2005) Future Oncol , vol.1 , pp. 161-171
    • Richardson, P.G.1    Mitsiades, C.2    Hideshima, T.3    Anderson, K.C.4
  • 32
    • 0032429122 scopus 로고    scopus 로고
    • Novel dipeptidyl proteasome inhibitors overcome Bcl-2 protective function and selectively accumulate the cyclin-dependent kinase inhibitor p27 and induce apoptosis in transformed, but not normal, human fibroblasts
    • An, B.; Goldfarb, R.H.; Siman, R.; Dou1, Q.P. Novel dipeptidyl proteasome inhibitors overcome Bcl-2 protective function and selectively accumulate the cyclin-dependent kinase inhibitor p27 and induce apoptosis in transformed, but not normal, human fibroblasts. Cell. Death Differ. 1998, 5, 1062-1075.
    • (1998) Cell. Death Differ , vol.5 , pp. 1062-1075
    • An, B.1    Goldfarb, R.H.2    Siman, R.3    Dou1, Q.P.4
  • 34
    • 77749251910 scopus 로고    scopus 로고
    • Complementary roles in cancer prevention: Protease inhibitor makes the cancer preventive peptide lunasin bioavailable
    • Hsieh, C.C.; Hernández-Ledesma, B.; Jeong, H.J.; Park, J.H., de Lumen, B.O. Complementary roles in cancer prevention: Protease inhibitor makes the cancer preventive peptide lunasin bioavailable. PLoS One 2010, 5, e8890.
    • (2010) Plos One , vol.5
    • Hsieh, C.C.1    Hernández-Ledesma, B.2    Jeong, H.J.3    Park, J.H.4    De Lumen, B.O.5
  • 35
    • 0032488367 scopus 로고    scopus 로고
    • Identification of intact peanut lectin in peripheral venous blood
    • Wang, Q.; Yu, L.G.; Campbell, B.J.; Milton, J.D.; Rhodes, J.M. Identification of intact peanut lectin in peripheral venous blood. Lancet 1998, 352, 1831-1832.
    • (1998) Lancet , vol.352 , pp. 1831-1832
    • Wang, Q.1    Yu, L.G.2    Campbell, B.J.3    Milton, J.D.4    Rhodes, J.M.5
  • 36
    • 0034857467 scopus 로고    scopus 로고
    • Carbohydrate binding properties of banana (Musa acuminata) lectin II. Binding of laminaribiose oligosaccharides and beta-glucans containing β1,6-glucosyl end groups
    • Goldstein, I.J.; Winter, H.C.; Mo, H.; Misaki, A.; van Damme, E.J.; Peumans, W.J. Carbohydrate binding properties of banana (Musa acuminata) lectin II. Binding of laminaribiose oligosaccharides and beta-glucans containing β1,6-glucosyl end groups. Eur. J. Biochem. 2001, 268, 2616-2619.
    • (2001) Eur. J. Biochem , vol.268 , pp. 2616-2619
    • Goldstein, I.J.1    Winter, H.C.2    Mo, H.3    Misaki, A.4    Van Damme, E.J.5    Peumans, W.J.6
  • 37
    • 0031404810 scopus 로고    scopus 로고
    • Composition, toxic, and anti-nutritional factorsof newly developed cultivars of Brazilian soybean (Glycine max)
    • Vasconcelos, I.M.; Siebra, E.A.; Maia, A.A.B.; Moreira, R.A.; Neto, A.F.; Campelo, G.J.A.; Oliveira, J.T.A. Composition, toxic, and anti-nutritional factorsof newly developed cultivars of Brazilian soybean (Glycine max). J. Food Sci. Agric. 1997, 75, 419-426.
    • (1997) J. Food Sci. Agric , vol.75 , pp. 419-426
    • Vasconcelos, I.M.1    Siebra, E.A.2    Maia, A.3    Moreira, R.A.4    Neto, A.F.5    Campelo, G.6    Oliveira, J.7
  • 38
    • 0025902249 scopus 로고
    • From soybeans to lectins: A trail of research revisited
    • Liener, I.E. From soybeans to lectins: A trail of research revisited. Carbohydr. Res. 1991, 213, 1-5.
    • (1991) Carbohydr. Res , vol.213 , pp. 1-5
    • Liener, I.E.1
  • 39
    • 0026497620 scopus 로고
    • Lectin reactivities as intermediate biomarkers in premalignant colorectal epithelium
    • Boland, C.R.; Martin, M.A.; Goldstein, I.J. Lectin reactivities as intermediate biomarkers in premalignant colorectal epithelium. J. Cell. Biochem. Suppl. 1992, 16G, 103-109.
    • (1992) J. Cell. Biochem. Suppl , vol.16 , pp. 103-109
    • Boland, C.R.1    Martin, M.A.2    Goldstein, I.J.3
  • 41
    • 58149522343 scopus 로고    scopus 로고
    • Isolation, purification and characterization of lunasin from defatted soybean flour and in vitro evaluation of its antinflammatory activity
    • Dia, V.P.; Wang, W.; Oh, V.L.; de Lumen, B.O.; de Meja, E.G. Isolation, purification and characterization of lunasin from defatted soybean flour and in vitro evaluation of its antinflammatory activity. Food Chem. 2009, 114, 108-115.
    • (2009) Food Chem , vol.114 , pp. 108-115
    • Dia, V.P.1    Wang, W.2    Oh, V.L.3    De Lumen, B.O.4    De Meja, E.G.5
  • 42
    • 70449697863 scopus 로고    scopus 로고
    • Antioxidant and anti-inflammatory properties of cancer preventive peptide lunasin in RAW 264.7 macrophages
    • Hernandez-Ledesma, B.; Hsieh, C.C.; de Lumen, B.O. Antioxidant and anti-inflammatory properties of cancer preventive peptide lunasin in RAW 264.7 macrophages. Biochem. Biophys. Res. Commun. 2009, 390, 803-808.
    • (2009) Biochem. Biophys. Res. Commun , vol.390 , pp. 803-808
    • Hernandez-Ledesma, B.1    Hsieh, C.C.2    De Lumen, B.O.3
  • 43
    • 84867090699 scopus 로고    scopus 로고
    • RGD-peptide lunasin inhibits Akt-mediated NF-κB activation in humanmacrophages through interaction with the αVβ3 integrin
    • Cam, A.; de Mejia, E.G. RGD-peptide lunasin inhibits Akt-mediated NF-κB activation in human macrophages through interaction with the αVβ3 integrin. Mol. Nutr. Food Res. 2012, 56, 1569-1581.
    • (2012) Mol. Nutr. Food Res , vol.56 , pp. 1569-1581
    • Cam, A.1    De Mejia, E.G.2
  • 45
    • 49249106417 scopus 로고    scopus 로고
    • Resistant hypertension: Diagnosis, evaluation, and treatment. A scientific statement from the American Heart Association Professional Education Committee of the Council for High Blood Pressure Research
    • Calhoun, D.A.; Jones, D.; Textor, S.; Goff, D.C.; Murphy, T.P.; Toto, R.D.; White, A.; Cushman, W.C.; White, W.; Sica, D., et al. Resistant hypertension: Diagnosis, evaluation, and treatment. A scientific statement from the American Heart Association Professional Education Committee of the Council for High Blood Pressure Research. Hypertension 2008, 51, 1403-1419.
    • (2008) Hypertension , vol.51 , pp. 1403-1419
    • Calhoun, D.A.1    Jones, D.2    Textor, S.3    Goff, D.C.4    Murphy, T.P.5    Toto, R.D.6    White, A.7    Cushman, W.C.8    White, W.9    Sica, D.10
  • 46
    • 53049095824 scopus 로고    scopus 로고
    • Lifestyle modifications for patients with hypertension
    • Lenz, T.L.; Monaghan, M.S. Lifestyle modifications for patients with hypertension. J. Am. Pharm. Assoc. 2008, 48, e92-e102.
    • (2008) J. Am. Pharm. Assoc , vol.48 , pp. ee92-e102
    • Lenz, T.L.1    Monaghan, M.S.2
  • 48
    • 32644459928 scopus 로고    scopus 로고
    • An angiotensin-I converting enzyme inhibitor from buckwheat (Fagopyrum esculentum Moench) flour
    • Aoyagi, Y. An angiotensin-I converting enzyme inhibitor from buckwheat (Fagopyrum esculentum Moench) flour. Phytochemistry 2006, 67, 618-621.
    • (2006) Phytochemistry , vol.67 , pp. 618-621
    • Aoyagi, Y.1
  • 49
    • 84876010527 scopus 로고    scopus 로고
    • Bioactive natural constituents from food sources-potential use in hypertension prevention and treatment
    • Huang, W.Y.; Davidge, S.T.; Wu, J. Bioactive natural constituents from food sources-potential use in hypertension prevention and treatment. Crit. Rev. Food Sci. Nutr. 2013, 53, 615-630.
    • (2013) Crit. Rev. Food Sci. Nutr , vol.53 , pp. 615-630
    • Huang, W.Y.1    Davidge, S.T.2    Wu, J.3
  • 50
    • 34547113083 scopus 로고    scopus 로고
    • Health benefits of traditional corn, beans, and pumpkin: In vitro studies for hyperglycemia and hypertension management
    • Kwon, Y.I.; Apostolidis, E.; Kim, Y.C.; Shetty, K. Health benefits of traditional corn, beans, and pumpkin: In vitro studies for hyperglycemia and hypertension management. J. Med. Food 2007, 10, 266-275.
    • (2007) J. Med. Food , vol.10 , pp. 266-275
    • Kwon, Y.I.1    Apostolidis, E.2    Kim, Y.C.3    Shetty, K.4
  • 51
    • 51649128893 scopus 로고    scopus 로고
    • Synthesis of angiotensin I-converting enzyme (ACE)-inhibitory peptides and γ-aminobutyric acid (GABA) during sourdough fermentation by selected lactic acid bacteria
    • Rizzello, C.G.; Cassone, A.; di Cagno, R.; Gobbetti, M. Synthesis of angiotensin I-converting enzyme (ACE)-inhibitory peptides and γ-aminobutyric acid (GABA) during sourdough fermentation by selected lactic acid bacteria. J. Agric. Food Chem. 2008, 56, 6936-6943.
    • (2008) J. Agric. Food Chem , vol.56 , pp. 6936-6943
    • Rizzello, C.G.1    Cassone, A.2    Di Cagno, R.3    Gobbetti, M.4
  • 52
    • 0032807257 scopus 로고    scopus 로고
    • Preparation and characterization of novelbioactive peptides responsible for angiotensin I-converting enzymes from wheat germ
    • Matsui, T.; Li, C.H.; Osajima, Y. Preparation and characterization of novelbioactive peptides responsible for angiotensin I-converting enzymes from wheat germ. J. Pept. Sci. 1999, 5, 289-297.
    • (1999) J. Pept. Sci , vol.5 , pp. 289-297
    • Matsui, T.1    Li, C.H.2    Osajima, Y.3
  • 53
    • 0242467926 scopus 로고    scopus 로고
    • Isolation and characterization of angiotensin I-converting enzyme inhibitory peptides from wheat gliadin hydrolysate
    • Motoi, H.; Kodama, T. Isolation and characterization of angiotensin I-converting enzyme inhibitory peptides from wheat gliadin hydrolysate. Nahrung 2003, 47, 354-358.
    • (2003) Nahrung , vol.47 , pp. 354-358
    • Motoi, H.1    Kodama, T.2
  • 54
    • 34047114512 scopus 로고    scopus 로고
    • Antihypertensive effect of rice protein hydrolysate with in vitro angiotensin I-converting enzyme inhibitory activity in spontaneously hypertensive rats
    • Li, G.H.; Qu, M.R.; Wan, J.Z.; You, J.M. Antihypertensive effect of rice protein hydrolysate with in vitro angiotensin I-converting enzyme inhibitory activity in spontaneously hypertensive rats. Asia Pac. J. Clin. Nutr. 2007, 16, 275-280.
    • (2007) Asia Pac. J. Clin. Nutr , vol.16 , pp. 275-280
    • Li, G.H.1    Qu, M.R.2    Wan, J.Z.3    You, J.M.4
  • 56
    • 0030115607 scopus 로고    scopus 로고
    • Isolation from alpha-zein of thermolysin peptides with angiotensin I-converting enzyme inhibitory activity
    • Yano, S.; Suzuki, K.; Funatsu, G. Isolation from alpha-zein of thermolysin peptides with angiotensin I-converting enzyme inhibitory activity. Biosci. Biotechnol. Biochem. 1996, 60, 661-663.
    • (1996) Biosci. Biotechnol. Biochem , vol.60 , pp. 661-663
    • Yano, S.1    Suzuki, K.2    Funatsu, G.3
  • 57
    • 78149344550 scopus 로고    scopus 로고
    • Identification and inhibitory properties of multifunctional peptides from pea protein hydrolysate
    • Li, H.; Aluko, R.E. Identification and inhibitory properties of multifunctional peptides from pea protein hydrolysate. J. Agric. Food Chem. 2010, 58, 11471-11476.
    • (2010) J. Agric. Food Chem , vol.58 , pp. 11471-11476
    • Li, H.1    Aluko, R.E.2
  • 58
    • 33244488716 scopus 로고    scopus 로고
    • Structural requirements of angiotensin I-converting enzyme inhibitory peptides: Quantitative structure-activity relationship study of di-and tri-peptides
    • Wu, J.; Aluko, R.E.; Nakai, S. Structural requirements of angiotensin I-converting enzyme inhibitory peptides: Quantitative structure-activity relationship study of di-and tri-peptides. J. Agric. Food Chem. 2006, 54, 732-738.
    • (2006) J. Agric. Food Chem , vol.54 , pp. 732-738
    • Wu, J.1    Aluko, R.E.2    Nakai, S.3
  • 59
    • 33644631847 scopus 로고    scopus 로고
    • Isolation and identification of peptides from Soy 11S-globulin with hypocholesterolemic activity
    • Pak, V.V.; Koo, M.S.; Kasymova, T.D.; Kwon, D.Y. Isolation and identification of peptides from Soy 11S-globulin with hypocholesterolemic activity. Chem. Nat. Compd. 2005, 41, 710-714.
    • (2005) Chem. Nat. Compd , vol.41 , pp. 710-714
    • Pak, V.V.1    Koo, M.S.2    Kasymova, T.D.3    Kwon, D.Y.4
  • 60
    • 79952095367 scopus 로고    scopus 로고
    • Soy β-conglycinin (7S Globulin) reduces plasma and liver cholesterol in rats fed hypercholesterolemic diet
    • Ferreira Ede, S.; Silva, M.A.; Demonte, A.; Neves, V.A. Soy β-conglycinin (7S Globulin) reduces plasma and liver cholesterol in rats fed hypercholesterolemic diet. J. Med. Food 2011, 14, 94-100.
    • (2011) J. Med. Food , vol.14 , pp. 94-100
    • Ferreira Ede, S.1    Silva, M.A.2    Demonte, A.3    Neves, V.A.4
  • 61
    • 2642556417 scopus 로고    scopus 로고
    • The α' subunit from soybean 7S globulin lowers plasma lipids and upregulates liverβ-VLDL receptors in rats fed a hypercholesterolemic diet
    • Duranti, M.; Lovati, M.R.; Dani, V.; Barbiroli, A.; Scarafoni, A.; Castiglioni, S.; Ponzone, C.; Morazzoni, P. The α' subunit from soybean 7S globulin lowers plasma lipids and upregulates liver β-VLDL receptors in rats fed a hypercholesterolemic diet. J. Nutr. 2004, 134, 1334-1339.
    • (2004) J. Nutr , vol.134 , pp. 1334-1339
    • Duranti, M.1    Lovati, M.R.2    Dani, V.3    Barbiroli, A.4    Scarafoni, A.5    Castiglioni, S.6    Ponzone, C.7    Morazzoni, P.8
  • 62
    • 0346726203 scopus 로고    scopus 로고
    • Proteins of white lupin seed, a naturally isoflavone-poor legume, reduce cholesterolemia in rats and increase LDL receptor activity in HepG2 cells
    • Sirtori, C.R.; Lovati, M.R.; Manzoni, C.; Castiglioni, S.; Duranti, M.; Magni, C.; Morandi, S.; D’Agostina, A.; Arnoldi, A. Proteins of white lupin seed, a naturally isoflavone-poor legume, reduce cholesterolemia in rats and increase LDL receptor activity in HepG2 cells. J. Nutr. 2004, 134, 18-23.
    • (2004) J. Nutr , vol.134 , pp. 18-23
    • Sirtori, C.R.1    Lovati, M.R.2    Manzoni, C.3    Castiglioni, S.4    Duranti, M.5    Magni, C.6    Morandi, S.7    D’agostina, A.8    Arnoldi, A.9
  • 63
    • 33748747614 scopus 로고    scopus 로고
    • New frontier in soy bioactive that may prevent age-related chronic diseases
    • Wang, W.; de Mejia, E.G. A new frontier in soy bioactive that may prevent age-related chronic diseases. Compr. Rev. Food Sci. Food Saf. 2005, 4, 63-78.
    • (2005) Compr. Rev. Food Sci. Food Saf , vol.4 , pp. 63-78
    • Wang, W.1    De Mejia, E.2
  • 65
    • 84856032752 scopus 로고    scopus 로고
    • Food protein-derived bioactive peptides: Production, processing, and potential health benefits
    • Udenigwe, C.C.; Aluko, R.E. Food protein-derived bioactive peptides: Production, processing, and potential health benefits. J. Food Sci. 2012, 77, R11-R24.
    • (2012) J. Food Sci , vol.77 , pp. R11-R24
    • Udenigwe, C.C.1    Aluko, R.E.2
  • 66
    • 0038058742 scopus 로고    scopus 로고
    • Bioactive proteins and peptides from food sources. Applications of bioprocesses used in isolation and recovery
    • Kitts, D.D.; Weiler, K. Bioactive proteins and peptides from food sources. Applications of bioprocesses used in isolation and recovery. Curr. Pharm. Des. 2003, 9, 1309-1323.
    • (2003) Curr. Pharm. Des , vol.9 , pp. 1309-1323
    • Kitts, D.D.1    Weiler, K.2
  • 67
    • 84856032175 scopus 로고    scopus 로고
    • Structural and antioxidant modification of wheat peptides modified by the heat and lipid peroxidation product malondialdehyde
    • Tang, X.; Wu, Q.; Le, G.; Wang, J.; Yin, K.; Shi, Y. Structural and antioxidant modification of wheat peptides modified by the heat and lipid peroxidation product malondialdehyde. J. Food Sci. 2012, 77, H16-H22.
    • (2012) J. Food Sci , vol.77 , pp. H16-H22
    • Tang, X.1    Wu, Q.2    Le, G.3    Wang, J.4    Yin, K.5    Shi, Y.6
  • 68
    • 0002384554 scopus 로고    scopus 로고
    • Antioxidative properties of histidine-containing peptides designed from peptide fragments found in the digests of a soybean protein
    • Chen, H.M.; Muramoto, K.; Yamauchi, F.; Fujimoto, K.; Nokihara, K. Antioxidative properties of histidine-containing peptides designed from peptide fragments found in the digests of a soybean protein. J. Agric. Food Chem. 1998, 46, 49-53.
    • (1998) J. Agric. Food Chem , vol.46 , pp. 49-53
    • Chen, H.M.1    Muramoto, K.2    Yamauchi, F.3    Fujimoto, K.4    Nokihara, K.5
  • 69
    • 33646085799 scopus 로고    scopus 로고
    • Antioxidant and free radical-scavenging activities of wheat germ protein hydrolysates (WGPH) prepared with alcalase
    • Zhu, K.; Zhou, H.; Quian, H. Antioxidant and free radical-scavenging activities of wheat germ protein hydrolysates (WGPH) prepared with alcalase. Process Biochem. 2006, 41, 1296-1302.
    • (2006) Process Biochem , vol.41 , pp. 1296-1302
    • Zhu, K.1    Zhou, H.2    Quian, H.3
  • 70
    • 77951270043 scopus 로고    scopus 로고
    • Amino acid composition and antioxidant properties of pea seed (Pisum sativum L.) enzymatic protein hydrolysate fractions
    • Pownall, T.L.; Udenigwe, C.C.; Aluko, R.E. Amino acid composition and antioxidant properties of pea seed (Pisum sativum L.) enzymatic protein hydrolysate fractions. J. Agric. Food Chem. 2010, 58, 4712-4718.
    • (2010) J. Agric. Food Chem , vol.58 , pp. 4712-4718
    • Pownall, T.L.1    Udenigwe, C.C.2    Aluko, R.E.3
  • 71
    • 33947319293 scopus 로고    scopus 로고
    • Antioxidant properties of papain hydrolysates of wheat gluten in different oxidation systems
    • Wang, J.; Zhao, M.; Zhao, Q.; Jiang, Y. Antioxidant properties of papain hydrolysates of wheat gluten in different oxidation systems. Food Chem. 2007, 101, 1658-1663.
    • (2007) Food Chem , vol.101 , pp. 1658-1663
    • Wang, J.1    Zhao, M.2    Zhao, Q.3    Jiang, Y.4
  • 72
    • 77952430321 scopus 로고    scopus 로고
    • Lunasin peptide purified from Solanum nigrum L. Protects DNA from oxidative damage by suppressing the generation of hydroxyl radical via blocking fenton reaction
    • Jeong, J.B.; de Lumen, B.O.; Jeong, H.J. Lunasin peptide purified from Solanum nigrum L. protects DNA from oxidative damage by suppressing the generation of hydroxyl radical via blocking fenton reaction. Cancer Lett. 2010, 293, 58-64.
    • (2010) Cancer Lett , vol.293 , pp. 58-64
    • Jeong, J.B.1    De Lumen, B.O.2    Jeong, H.J.3
  • 73
    • 84892638582 scopus 로고    scopus 로고
    • Antioxidant activity and protective effects of peptide lunasin against oxidative stress in intestinal Caco-2 cells
    • Garcia-Nebot, M.J.; Recio, I.; Hernandez-Ledesma, B. Antioxidant activity and protective effects of peptide lunasin against oxidative stress in intestinal Caco-2 cells. Food Chem. Toxicol. 2014, 65, 155-161.
    • (2014) Food Chem. Toxicol , vol.65 , pp. 155-161
    • Garcia-Nebot, M.J.1    Recio, I.2    Hernandez-Ledesma, B.3
  • 74
    • 84893268921 scopus 로고    scopus 로고
    • Protective effect of wheat peptides against indomethacin-induced oxidative stress in IEC-6 cells
    • Yin, H.; Pan, X.; Song, Z.; Wang, S.; Yang, L.; Sun, G. Protective effect of wheat peptides against indomethacin-induced oxidative stress in IEC-6 cells. Nutrients 2014, 6, 564-574.
    • (2014) Nutrients , vol.6 , pp. 564-574
    • Yin, H.1    Pan, X.2    Song, Z.3    Wang, S.4    Yang, L.5    Sun, G.6
  • 75
    • 84886903363 scopus 로고    scopus 로고
    • Vegetable foods: A cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities
    • García, M.C.; Puchalska, P.; Esteve, C.; Marina, M.L. Vegetable foods: A cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities. Talanta 2013, 106, 328-349.
    • (2013) Talanta , vol.106 , pp. 328-349
    • García, M.C.1    Puchalska, P.2    Esteve, C.3    Marina, M.L.4
  • 76
    • 84868123294 scopus 로고    scopus 로고
    • Food proteins as a source of bioactive peptides with different functions
    • Rutherfurd-Markwick, K.J. Food proteins as a source of bioactive peptides with different functions. Br. J. Nutr. 2012, 108, 149-157.
    • (2012) Br. J. Nutr , vol.108 , pp. 149-157
    • Rutherfurd-Markwick, K.J.1
  • 77
    • 79960401023 scopus 로고    scopus 로고
    • Soy protein effects on serum lipoproteins: A quality assessment and meta-analysis of randomized, controlled studies
    • Anderson, J.W.; Bush, H.M. Soy protein effects on serum lipoproteins: A quality assessment and meta-analysis of randomized, controlled studies. J. Am. Coll. Nutr. 2011, 30, 79-91.
    • (2011) J. Am. Coll. Nutr , vol.30 , pp. 79-91
    • Anderson, J.W.1    Bush, H.M.2
  • 79
    • 78650271712 scopus 로고    scopus 로고
    • Treatment with marine collagen peptides modulates glucose and lipid metabolism in Chinese patients with type 2 diabetes mellitus
    • Zhu, C.F.; Li, G.Z.; Peng, H.B.; Zhang, F.; Chen, Y.; Li, Y. Treatment with marine collagen peptides modulates glucose and lipid metabolism in Chinese patients with type 2 diabetes mellitus. Appl. Physiol. Nutr. Metab. 2010, 35, 797-804.
    • (2010) Appl. Physiol. Nutr. Metab , vol.35 , pp. 797-804
    • Zhu, C.F.1    Li, G.Z.2    Peng, H.B.3    Zhang, F.4    Chen, Y.5    Li, Y.6
  • 80
    • 84876557415 scopus 로고    scopus 로고
    • Do the lactotripeptides isoleucine-proline-proline and valine-proline-proline reduce systolic blood pressure in European subjects? A meta-analysis of randomized controlled trials
    • Cicero, A.F.; Aubin, F.; Azais-Braesco, V.; Borghi, C. Do the lactotripeptides isoleucine-proline-proline and valine-proline-proline reduce systolic blood pressure in European subjects? A meta-analysis of randomized controlled trials. Am. J. Hypertens. 2013, 26, 442-449.
    • (2013) Am. J. Hypertens , vol.26 , pp. 442-449
    • Cicero, A.F.1    Aubin, F.2    Azais-Braesco, V.3    Borghi, C.4
  • 81
    • 79959288378 scopus 로고    scopus 로고
    • Blood pressure lowering effect of lactotripeptides assumed as functional foods: A meta-analysis of current available clinical trials
    • Cicero, A.F.; Gerocarni, B.; Laghi, L.; Borghi, C. Blood pressure lowering effect of lactotripeptides assumed as functional foods: A meta-analysis of current available clinical trials. J. Hum. Hypertens. 2011, 25, 425-436.
    • (2011) J. Hum. Hypertens , vol.25 , pp. 425-436
    • Cicero, A.F.1    Gerocarni, B.2    Laghi, L.3    Borghi, C.4
  • 82
    • 77949652755 scopus 로고    scopus 로고
    • Additive beneficial effects of lactotripeptides intake with regular exercise on endothelium-dependent dilatation in postmenopausal women
    • Yoshizawa, M.; Maeda, S.; Miyaki, A.; Misono, M.; Choi, Y.; Shimojo, N.; Ajisaka, R.; Tanaka, H. Additive beneficial effects of lactotripeptides intake with regular exercise on endothelium-dependent dilatation in postmenopausal women. Am. J. Hypertens. 2010, 23, 368-372.
    • (2010) Am. J. Hypertens , vol.23 , pp. 368-372
    • Yoshizawa, M.1    Maeda, S.2    Miyaki, A.3    Misono, M.4    Choi, Y.5    Shimojo, N.6    Ajisaka, R.7    Tanaka, H.8
  • 83
    • 80052507804 scopus 로고    scopus 로고
    • Lactotripeptides effect on office and 24-h ambulatory blood pressure, blood pressure stress response, pulse wave velocity and cardiac output in patients with high-normal blood pressure or first-degree hypertension: A randomized double-blind clinical trial
    • Cicero, A.F.; Rosticci, M.; Gerocarni, B.; Bacchelli, S.; Veronesi, M.; Strocchi, E.; Borghi, C. Lactotripeptides effect on office and 24-h ambulatory blood pressure, blood pressure stress response, pulse wave velocity and cardiac output in patients with high-normal blood pressure or first-degree hypertension: A randomized double-blind clinical trial. Hypertens. Res. 2011, 34, 1035-1040.
    • (2011) Hypertens. Res , vol.34 , pp. 1035-1040
    • Cicero, A.F.1    Rosticci, M.2    Gerocarni, B.3    Bacchelli, S.4    Veronesi, M.5    Strocchi, E.6    Borghi, C.7
  • 85
    • 75449100518 scopus 로고    scopus 로고
    • Hydroxyproline-containing dipeptides and tripeptides quantified at high concentration in human blood after oral administration of gelatin hydrolysate
    • Ichikawa, S.; Morifuji, M.; Ohara, H.; Matsumoto, H.; Takeuchi, Y.; Sato, K. Hydroxyproline-containing dipeptides and tripeptides quantified at high concentration in human blood after oral administration of gelatin hydrolysate. Int. J. Food. Sci. Nutr. 2010, 61, 52-60.
    • (2010) Int. J. Food. Sci. Nutr , vol.61 , pp. 52-60
    • Ichikawa, S.1    Morifuji, M.2    Ohara, H.3    Matsumoto, H.4    Takeuchi, Y.5    Sato, K.6
  • 86
    • 59849104535 scopus 로고    scopus 로고
    • Effect of Prolyl-hydroxyproline (Pro-Hyp), a food-derived collagen peptide in human blood, on growth of fibroblasts from mouse skin
    • Shigemura, Y.; Iwai, K.; Morimatsu, F.; Iwamoto, T.; Mori, T.; Oda, C.; Taira, T.; Park, E.Y.; Nakamura, Y.; Sato, K., et al. Effect of Prolyl-hydroxyproline (Pro-Hyp), a food-derived collagen peptide in human blood, on growth of fibroblasts from mouse skin. J. Agric. Food. Chem. 2009, 57, 444-449.
    • (2009) J. Agric. Food. Chem , vol.57 , pp. 444-449
    • Shigemura, Y.1    Iwai, K.2    Morimatsu, F.3    Iwamoto, T.4    Mori, T.5    Oda, C.6    Taira, T.7    Park, E.Y.8    Nakamura, Y.9    Sato, K.10


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