메뉴 건너뛰기




Volumn 15, Issue 2, 2014, Pages 143-152

Stability and cytotoxicity of angiotensin-I-converting enzyme inhibitory peptides derived from bovine casein

Author keywords

Angiotensin I converting enzyme inhibitory peptide; Cytotoxicity; Heat treatment; Stability

Indexed keywords

ACID; ALKALI; CASEIN; DIPEPTIDYL CARBOXYPEPTIDASE; PEPTIDE;

EID: 84896072506     PISSN: 16731581     EISSN: 18621783     Source Type: Journal    
DOI: 10.1631/jzus.B1300239     Document Type: Article
Times cited : (22)

References (33)
  • 1
    • 77952098905 scopus 로고    scopus 로고
    • Effects of heat treatment and in vitro digestion on the angiotensin converting enzyme inhibitory activity of some legume species
    • doi:10.1007/s00217-009-1133-x
    • Akillioǧlu, H.G., Karakaya, S., 2009. Effects of heat treatment and in vitro digestion on the angiotensin converting enzyme inhibitory activity of some legume species. Eur. Food Res. Technol., 229(6):915-921. [doi:10.1007/s00217-009-1133-x]
    • (2009) Eur. Food Res. Technol. , vol.229 , Issue.6 , pp. 915-921
    • Akillioǧlu, H.G.1    Karakaya, S.2
  • 2
    • 0018940463 scopus 로고
    • Captopril in clinical hypertension. Changes in components of renin-angiotensin system and in body composition in relation to fall in blood pressure with a note on measurement of angiotensin II during converting enzyme inhibition
    • Atkinson, A.B., Morton, J.J., Brown, J.J., et al., 1980. Captopril in clinical hypertension. Changes in components of renin-angiotensin system and in body composition in relation to fall in blood pressure with a note on measurement of angiotensin II during converting enzyme inhibition. Br. Heart J., 44 (3):290-296. [doi:10.1136/hrt.44.3.290] (Pubitemid 10020808)
    • (1980) British Heart Journal , vol.44 , Issue.3 , pp. 290-296
    • Atkinson, A.B.1    Morton, J.J.2    Brown, J.J.3
  • 4
    • 0642302370 scopus 로고    scopus 로고
    • Molecular and Microstructural Studies of Thermal Denaturation and Gelation of β-Lactoglobulins A and B
    • Boye, J.I., Ma, C.Y., Ismail, A., et al., 1997. Molecular and microstructural studies of thermal denaturation and gelation of β-lactoglobulins A and B. J. Agric. Food Chem., 45(5):1608-1618. [doi:10.1021/jf960622x] (Pubitemid 127485589)
    • (1997) Journal of Agricultural and Food Chemistry , vol.45 , Issue.5 , pp. 1608-1618
    • Boye, J.I.1    Ma, C.-Y.2    Ismail, A.3    Harwalkar, V.R.4    Kalab, M.5
  • 5
    • 33847039492 scopus 로고    scopus 로고
    • Purification of angiotensin I-converting enzyme inhibitory peptides and antihypertensive effect of milk produced by protease-facilitated lactic fermentation
    • doi:10.1016/j.idairyj.2006.07.004
    • Chen, G.W., Tsai, J.S., Pan, B.S., 2007. Purification of angiotensin I-converting enzyme inhibitory peptides and antihypertensive effect of milk produced by protease-facilitated lactic fermentation. Int. Dairy J., 17(6):641-647. [doi:10.1016/j.idairyj.2006.07.004]
    • (2007) Int. Dairy J. , vol.17 , Issue.6 , pp. 641-647
    • Chen, G.W.1    Tsai, J.S.2    Pan, B.S.3
  • 6
    • 84855819460 scopus 로고    scopus 로고
    • Purification and characterization of a novel angiotensin-I converting enzyme (ACE) inhibitory peptide derived from enzymatic hydrolysate of grass carp protein
    • doi:10.1016/j.peptides.2011.11.006
    • Chen, J.W., Wang, Y.M., Zhong, Q.X., et al., 2012. Purification and characterization of a novel angiotensin-I converting enzyme (ACE) inhibitory peptide derived from enzymatic hydrolysate of grass carp protein. Peptides, 33(1):52-58. [doi:10.1016/j.peptides.2011.11.006]
    • (2012) Peptides , vol.33 , Issue.1 , pp. 52-58
    • Chen, J.W.1    Wang, Y.M.2    Zhong, Q.X.3
  • 7
    • 85022241054 scopus 로고
    • Spectrophotometric assay using o-phthaldialdehyde for determination of proteolysis in milk and isolated milk proteins
    • doi:10.3168/jds.S0022-0302(83)81926-2
    • Church, F.C., Swaisgood, H.E., Porter, D.H., et al., 1983. Spectrophotometric assay using o-phthaldialdehyde for determination of proteolysis in milk and isolated milk proteins. J. Dairy Sci., 66(6):1219-1227. [doi:10.3168/jds.S0022-0302(83)81926-2]
    • (1983) J. Dairy Sci. , vol.66 , Issue.6 , pp. 1219-1227
    • Church, F.C.1    Swaisgood, H.E.2    Porter, D.H.3
  • 8
    • 33847159988 scopus 로고    scopus 로고
    • Effect of heat and enzymatic treatment on the antihypertensive activity of whey protein hydrolysates
    • DOI 10.1016/j.idairyj.2006.09.003, PII S0958694606002135
    • Costa, E.L., Gontijo, J.A.D., Netto, F.M., 2007. Effect of heat and enzymatic treatment on the antihypertensive activity of whey protein hydrolysates. Int. Dairy J., 17(6):632-640. [doi:10.1016/j.idairyj.2006.09.003] (Pubitemid 46290625)
    • (2007) International Dairy Journal , vol.17 , Issue.6 , pp. 632-640
    • Lourenco Da, C.E.1    Antonio Da, R.G.J.2    Netto, F.M.3
  • 9
    • 0015083353 scopus 로고
    • Spectrophotometric assay and properties of the angiotensin converting enzyme of rabbit lung
    • doi:10.1016/0006-2952(71)90292-9
    • Cushman, D.W., Cheung, H.S., 1971. Spectrophotometric assay and properties of the angiotensin converting enzyme of rabbit lung. Biochem. Pharmacol., 20(7):1637-1648. [doi:10.1016/0006-2952(71)90292-9]
    • (1971) Biochem. Pharmacol. , vol.20 , Issue.7 , pp. 1637-1648
    • Cushman, D.W.1    Cheung, H.S.2
  • 10
    • 84873780743 scopus 로고
    • A bradykinin-potentiating factor (BPF) present in the venom of Bothrops jararaca
    • doi:10.1111/j.1476-5381.1965.tb02091.x
    • Ferreira, S.H., 1965. A bradykinin-potentiating factor (BPF) present in the venom of Bothrops jararaca. Br. J. Pharmacol. Chemother., 24(1):163-169. [doi:10.1111/j.1476-5381.1965.tb02091.x]
    • (1965) Br. J. Pharmacol. Chemother. , vol.24 , Issue.1 , pp. 163-169
    • Ferreira, S.H.1
  • 11
    • 16444373369 scopus 로고    scopus 로고
    • Caseinophosphopeptides and their cell modulating potential
    • Hartmann, R., Meisel, H., 2004. Caseinophosphopeptides and their cell modulting potential. Biofactors, 21(1-4):73-78. [doi:10.1002/biof.552210114] (Pubitemid 40921829)
    • (2004) BioFactors , vol.21 , Issue.1-4 , pp. 73-78
    • Hartmann, R.1    Meisel, H.2
  • 12
    • 76349110759 scopus 로고    scopus 로고
    • Impact of processing on stability of angiotensin I-converting enzyme (ACE) inhibitory peptides obtained from tuna cooking juice
    • doi:10.1016/j.foodres.2009.12.012
    • Hwang, J.S., 2010. Impact of processing on stability of angiotensin I-converting enzyme (ACE) inhibitory peptides obtained from tuna cooking juice. Food Res. Int., 43(3):902-906. [doi:10.1016/j.foodres.2009.12.012]
    • (2010) Food Res. Int. , vol.43 , Issue.3 , pp. 902-906
    • Hwang, J.S.1
  • 13
    • 0346752503 scopus 로고    scopus 로고
    • Angiotensin I-Converting Enzyme Inhibitory Activity and Insulin Secretion Stimulative Activity of Fermented Fish Sauce
    • DOI 10.1016/S1389-1723(03)70138-8
    • Ichimura, T., Hu, J.N., Aita, D.Q., et al., 2003. Angiotensin I-converting enzyme inhibitory activity and insulin secretion stimulative activity of fermented fish sauce. J. Biosci. Bioeng., 96(5):496-499. [doi:10.1016/S1389-1723(03)70138-8] (Pubitemid 37533395)
    • (2003) Journal of Bioscience and Bioengineering , vol.96 , Issue.5 , pp. 496-499
    • Ichimura, T.1    Hu, J.2    Aita, D.Q.3    Maruyama, S.4
  • 14
    • 12344308529 scopus 로고    scopus 로고
    • Purification and identification of angiotensin converting enzyme inhibitory peptides from beef hydrolysates
    • DOI 10.1016/j.meatsci.2004.10.014, PII S0309174004002670
    • Jang, A., Lee, M., 2005. Purification and identification of angiotensin converting enzyme inhibitory peptides from beef hydrolysates. Meat Sci., 69(4):653-661. [doi:10.1016/j.meatsci.2004.10.014] (Pubitemid 40119920)
    • (2005) Meat Science , vol.69 , Issue.4 , pp. 653-661
    • Jang, A.1    Lee, M.2
  • 15
    • 49649099436 scopus 로고    scopus 로고
    • Storage stability of the synthetic angiotensin converting enzyme (ACE) inhibitory peptides separated from beef sareoplasmic protein extracts at different pH, temperature, and gastric digestion
    • Jang, A., Jo, C., Lee, M., 2007. Storage stability of the synthetic angiotensin converting enzyme (ACE) inhibitory peptides separated from beef sareoplasmic protein extracts at different pH, temperature, and gastric digestion. Food Sci. Biotechnol., 16(4):572-575.
    • (2007) Food Sci. Biotechnol. , vol.16 , Issue.4 , pp. 572-575
    • Jang, A.1    Jo, C.2    Lee, M.3
  • 16
    • 77954620363 scopus 로고    scopus 로고
    • Production, analysis and in vivo evaluation of novel angiotensin-I- converting enzyme inhibitory peptides from bovine casein
    • doi:10.1016/j.foodchem.2010.05.026
    • Jiang, Z.M., Tian, B., Brodkorb, A., et al., 2010. Production, analysis and in vivo evaluation of novel angiotensin-I-converting enzyme inhibitory peptides from bovine casein. Food Chem., 123(3):779-786. [doi:10.1016/j. foodchem.2010.05.026]
    • (2010) Food Chem. , vol.123 , Issue.3 , pp. 779-786
    • Jiang, Z.M.1    Tian, B.2    Brodkorb, A.3
  • 17
    • 0032422201 scopus 로고    scopus 로고
    • Impact of processing on bioactive proteins and peptides
    • DOI 10.1016/S0924-2244(98)00054-5, PII S0924224498000545
    • Korhonen, H., Pihlanto-Leppala, A., Rantamaki, P., et al., 1998. Impact of processing on bioactive proteins and peptides. Trends Food Sci. Technol., 9(8-9):307-319. [doi:10.1016/S0924-2244(98)00054-5] (Pubitemid 29032225)
    • (1998) Trends in Food Science and Technology , vol.9 , Issue.8-9 , pp. 307-319
    • Korhonen, H.1    Pihlanto-Leppala, A.2    Rantamaki, P.3    Tupasela, T.4
  • 18
    • 67650269402 scopus 로고    scopus 로고
    • Purification and characterization of angiotensin I converting enzyme inhibitory peptides from the rotifer, Brachionus rotundiformis
    • doi:10.1016/j.biortech.2009.05.057
    • Lee, J.K., Hong, S., Jeon, J.K., et al., 2009. Purification and characterization of angiotensin I converting enzyme inhibitory peptides from the rotifer, Brachionus rotundiformis. Bioresource Technol., 100(21):5255-5259. [doi:10.1016/j.biortech.2009.05.057]
    • (2009) Bioresource Technol. , vol.100 , Issue.21 , pp. 5255-5259
    • Lee, J.K.1    Hong, S.2    Jeon, J.K.3
  • 19
    • 77955038529 scopus 로고    scopus 로고
    • Angiotensin I-converting enzyme inhibitory activities of extracts from commercial Chinese style fermented soypaste
    • doi:10.6090/jarq.44.167
    • Li, F.J., Yin, L.J., Cheng, Y.Q., et al., 2010. Angiotensin I-converting enzyme inhibitory activities of extracts from commercial Chinese style fermented soypaste. Jpn. Agric. Res. Q., 44(2):167-172. [doi:10.6090/jarq.44.167]
    • (2010) Jpn. Agric. Res. Q. , vol.44 , Issue.2 , pp. 167-172
    • Li, F.J.1    Yin, L.J.2    Cheng, Y.Q.3
  • 20
    • 3242774456 scopus 로고    scopus 로고
    • Angiotensin I-converting enzyme inhibitory peptides derived from food proteins and their physiological and pharmacological effects
    • doi:10.1016/j.nutres.2003.10.014
    • Li, G.H., Le, G.W., Shi, Y.H., et al., 2004. Angiotensin I-converting enzyme inhibitory peptides derived from food proteins and their physiological and pharmacological effects. Nutr. Res., 24(7):469-486. [doi:10.1016/j.nutres. 2003.10.014]
    • (2004) Nutr. Res. , vol.24 , Issue.7 , pp. 469-486
    • Li, G.H.1    Le, G.W.2    Shi, Y.H.3
  • 21
    • 33748297647 scopus 로고    scopus 로고
    • Physiological, chemical and technological aspects of milk-protein-derived peptides with antihypertensive and ACE-inhibitory activity
    • DOI 10.1016/j.idairyj.2006.06.004, PII S0958694606001476
    • López-Fandino, R, Otte, J., van Camp, J., 2006. Physiological, chemical and technological aspects of milk-protein-derived peptides with antihypertensive and ACE-inhibitory activity. Int. Dairy J., 16(11):1277-1293. [doi:10.1016/j.idairyj.2006.06.004] (Pubitemid 44331581)
    • (2006) International Dairy Journal , vol.16 , Issue.11 , pp. 1277-1293
    • Lopez-Fandino, R.1    Otte, J.2    Van Camp, J.3
  • 22
    • 0028438376 scopus 로고
    • A cell culture model to identify biologically active peptides generated by bacterial hydrolysis of casein
    • doi:10.3168/jds.S0022-0302(94)77054-5
    • MacDonald, R., Thornton, W.H., Marshall, R.A., 1994. A cell culture model to identify biologically active peptides generated by bacterial hydrolysis of casein. J. Dairy Sci., 77(5):1167-1175. [doi:10.3168/jds.S0022-0302(94)77054-5]
    • (1994) J. Dairy Sci. , vol.77 , Issue.5 , pp. 1167-1175
    • MacDonald, R.1    Thornton, W.H.2    Marshall, R.A.3
  • 23
    • 0029315309 scopus 로고
    • Angiotensin I converting enzyme inhibitory activities of various fermented foods
    • doi:10.1271/bbb.59.1147
    • Okamoto, A., Hanagata, H., Matsumoto, E., et al., 1995. Angiotensin I converting enzyme inhibitory activities of various fermented foods. Biosci. Biotechnol. Biochem., 59(6):1147-1149. [doi:10.1271/bbb.59.1147]
    • (1995) Biosci. Biotechnol. Biochem. , vol.59 , Issue.6 , pp. 1147-1149
    • Okamoto, A.1    Hanagata, H.2    Matsumoto, E.3
  • 24
    • 0020002135 scopus 로고
    • Enzymes of the renin-angiotensin system and their inhibitors
    • Ondetti, M.A., Cushman, D.W., 1982. Enzyme of the rennin-angiotensin system and their inhibitors. Annu. Rev. Biochem., 51(1):283-308. [doi:10.1146/annurev.bi.51.070182.001435] (Pubitemid 12024690)
    • (1982) Annual Review of Biochemistry , vol.51 , pp. 283-308
    • Ondetti, M.A.1    Cushman, D.W.2
  • 25
    • 0018305067 scopus 로고
    • Peptide inhibitors of angiotensin I-converting enzyme in digests of gelatin by bacterial collagenase
    • Oshima, G., Shimabukuro, H., Nagasawa, K., 1979. Peptide inhibitors of angiotensin I-converting enzyme in digests of gelatin by bacterial collagenase. Biochim. Biophys. Acta Enzymol., 566(1):128-137. [doi:10.1016/0005-2744(79) 90255-9] (Pubitemid 9076461)
    • (1979) Biochimica et Biophysica Acta , vol.566 , Issue.1 , pp. 128-137
    • Oshima, G.1    Shimabukuro, H.2    Nagasawa, K.3
  • 26
    • 69349102184 scopus 로고    scopus 로고
    • Casein-derived bioactive peptides: Biological effects, industrial uses, safety aspects and regulatory status
    • doi:10.1016/j.idairyj.2009.06.001
    • Phelan, M., Aherne, A., FitzGerald, R.J., et al., 2009. Casein-derived bioactive peptides: biological effects, industrial uses, safety aspects and regulatory status. Int. Dairy J., 19(11):643-654. [doi:10.1016/j.idairyj.2009. 06.001]
    • (2009) Int. Dairy J. , vol.19 , Issue.11 , pp. 643-654
    • Phelan, M.1    Aherne, A.2    FitzGerald, R.J.3
  • 27
    • 34548595098 scopus 로고    scopus 로고
    • Antihypertensive effect of an angiotensin I-converting enzyme inhibitory peptide from bullfrog (Rana catesbeiana Shaw) muscle protein in spontaneously hypertensive rats
    • doi:10.1016/j.procbio.2007.05.013
    • Qian, Z.J., Jung, W.K., Lee, S.H., et al., 2007. Antihypertensive effect of an angiotensin I-converting enzyme inhibitory peptide from bullfrog (Rana catesbeiana Shaw) muscle protein in spontaneously hypertensive rats. Process Biochem., 42(10):1443-1448. [doi:10.1016/j.procbio.2007.05.013]
    • (2007) Process Biochem. , vol.42 , Issue.10 , pp. 1443-1448
    • Qian, Z.J.1    Jung, W.K.2    Lee, S.H.3
  • 28
    • 33646588670 scopus 로고    scopus 로고
    • Effects of heat treatment and high pressure on the subsequent lactosylation of β-lactoglobulin
    • DOI 10.1016/j.foodchem.2005.08.039, PII S0308814605007077
    • Rada-Mendoza, M., Villamie, M., Molina, E., et al., 2006. Effects of heat treatment and high pressure on the subsequent lactosylation of beta-lactoglobulin. Food Chem., 99(4):651-655. [doi:10.1016/j.foodchem.2005.08. 039] (Pubitemid 43729570)
    • (2006) Food Chemistry , vol.99 , Issue.4 , pp. 651-655
    • Rada-Mendoza, M.1    Villamiel, M.2    Molina, E.3    Olano, A.4
  • 29
    • 59049085867 scopus 로고    scopus 로고
    • Stability of new potential ACE inhibitor in the aqueous solutions of different pH
    • doi:10.1016/j.jpba.2008.11.029
    • Roškar, R., Simončič, Z., Gartner, A., et al., 2009. Stability of new potential ACE inhibitor in the aqueous solutions of different pH. J. Pharm. Biomed. Anal., 49(2):295-303. [doi:10.1016/j.jpba.2008.11.029]
    • (2009) J. Pharm. Biomed. Anal. , vol.49 , Issue.2 , pp. 295-303
    • Roškar, R.1    Simončič, Z.2    Gartner, A.3
  • 30
    • 60749131028 scopus 로고    scopus 로고
    • Isolation and characterisation of a novel angiotensin I-converting enzyme (ACE) inhibitory peptide from the algae protein waste
    • doi:10.1016/j.foodchem.2008.12.019
    • Sheih, I.C., Fang, T.J., Wu, T.K., 2009. Isolation and characterisation of a novel angiotensin I-converting enzyme (ACE) inhibitory peptide from the algae protein waste. Food Chem., 115(1):279-284. [doi:10.1016/j.foodchem.2008. 12.019]
    • (2009) Food Chem. , vol.115 , Issue.1 , pp. 279-284
    • Sheih, I.C.1    Fang, T.J.2    Wu, T.K.3
  • 31
    • 67349268149 scopus 로고    scopus 로고
    • Angiotensin I-converting enzyme-inhibitory peptide fractions from albumin 1 and globulin as obtained of amaranth grain
    • doi:10.1016/j.foodchem.2009.02.062
    • Tovar-Pérez, E.G., Guerrero-Legarreta, I., Farres-Gonzalez, A., et al., 2009. Angiotensin I-converting enzyme-inhibitory peptide fractions from albumin 1 and globulin as obtained of amaranth grain. Food Chem., 116(2):437-444. [doi:10.1016/j.foodchem.2009.02.062]
    • (2009) Food Chem. , vol.116 , Issue.2 , pp. 437-444
    • Tovar-Pérez, E.G.1    Guerrero-Legarreta, I.2    Farres-Gonzalez, A.3
  • 32
    • 0036219595 scopus 로고    scopus 로고
    • Characterization of inhibition and stability of soy-protein-derived angiotensin I-converting enzyme inhibitory peptides
    • doi:10.1016/S0963-9969(01)00131-4
    • Wu, J.P., Ding, X.L., 2002. Characterization of inhibition and stability of soy-protein-derived angiotensin I-converting enzyme inhibitory peptides. Food Res. Int., 35(4):367-375. [doi:10.1016/S0963-9969(01)00131-4]
    • (2002) Food Res. Int. , vol.35 , Issue.4 , pp. 367-375
    • Wu, J.P.1    Ding, X.L.2
  • 33
    • 33645232931 scopus 로고    scopus 로고
    • Angiotensin I-converting enzyme inhibitory peptides in douchi, a Chinese traditional fermented soybean product
    • doi:10.1016/j.foodchem.2005.06.024
    • Zhang, J.H., Tatsumi, E., Ding, C.H., et al., 2006. Angiotensin I-converting enzyme inhibitory peptides in douchi, a Chinese traditional fermented soybean product. Food Chem., 98(3):551-557. [doi:10.1016/j.foodchem. 2005.06.024]
    • (2006) Food Chem. , vol.98 , Issue.3 , pp. 551-557
    • Zhang, J.H.1    Tatsumi, E.2    Ding, C.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.