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Volumn 28, Issue 5, 2012, Pages 1197-1206

Modeling the angiotensin-converting enzyme inhibitory activity of peptide mixtures obtained from cheese whey hydrolysates using concentration-response curves

Author keywords

Antihypertensive activity; Mathematical modeling; Peptides; Ultrafiltration; Whey proteolysis

Indexed keywords

ACE INHIBITION; ACTIVE PEPTIDES; ADEQUATE MODELS; ANGIOTENSIN-CONVERTING ENZYME; ANTI-HYPERTENSIVE ACTIVITIES; BEST FIT; BIOACTIVE PEPTIDES; CHEESE WHEY; INHIBITORY ACTIVITY; LOGISTIC MODELS; MICHAELIS-MENTEN KINETIC; NEUTRASE; PEPTIDE MIXTURES; PHYSICAL MEANINGS; PROTEIN CONTENTS; REGRESSION COEFFICIENT; WHEY PROTEOLYSIS;

EID: 84867395437     PISSN: 87567938     EISSN: 15206033     Source Type: Journal    
DOI: 10.1002/btpr.1587     Document Type: Article
Times cited : (29)

References (43)
  • 1
    • 0030199270 scopus 로고    scopus 로고
    • The biotechnological utilization of cheese whey: a review
    • González Siso MI. The biotechnological utilization of cheese whey: a review. Bioresour Technol. 1996; 57: 1-11.
    • (1996) Bioresour Technol. , vol.57 , pp. 1-11
    • González Siso, M.I.1
  • 2
    • 62349141889 scopus 로고    scopus 로고
    • Partial demineralization and concentration of acid whey by nanofiltration combined with diafiltration
    • Román A, Wang J, Csanádi J, Hodúr C, Vatai G. Partial demineralization and concentration of acid whey by nanofiltration combined with diafiltration. Desalination. 2009; 241: 288-295.
    • (2009) Desalination. , vol.241 , pp. 288-295
    • Román, A.1    Wang, J.2    Csanádi, J.3    Hodúr, C.4    Vatai, G.5
  • 3
    • 84875006401 scopus 로고    scopus 로고
    • Cheese whey utilization for bacteriocin production
    • Cerdán ME, González-Siso MI, Bacerra M, editors. Kerala, India: Transworld Research Network;: -
    • Fajardo P, Fuciños C, Rodríguez I, Pastrana L, Guerra NP. Cheese whey utilization for bacteriocin production. In: Cerdán ME, González-Siso MI, Bacerra M, editors. Advances in Cheese Whey Utilization. Kerala, India: Transworld Research Network; 2008: 163-193.
    • (2008) Advances in Cheese Whey Utilization , pp. 163-193
    • Fajardo, P.1    Fuciños, C.2    Rodríguez, I.3    Pastrana, L.4    Guerra, N.P.5
  • 4
    • 33747503962 scopus 로고    scopus 로고
    • Bioactive peptides: production and functionality
    • Korhonen H, Pihlanto A. Bioactive peptides: production and functionality. Int. Dairy J. 2006; 16: 945-960.
    • (2006) Int. Dairy J. , vol.16 , pp. 945-960
    • Korhonen, H.1    Pihlanto, A.2
  • 5
    • 84875007121 scopus 로고    scopus 로고
    • The effect of pH and thermal treatment on some functional properties of whey proteins hydrolysates as measured by fluorescence spectroscopy
    • Hîntoiu A, Râpeanu G, Stanciu S, Stanciuc N. The effect of pH and thermal treatment on some functional properties of whey proteins hydrolysates as measured by fluorescence spectroscopy. J Agroaliment Process Technol. 2011; 17: 179-185.
    • (2011) J Agroaliment Process Technol. , vol.17 , pp. 179-185
    • Hîntoiu, A.1    Râpeanu, G.2    Stanciu, S.3    Stanciuc, N.4
  • 6
    • 2342544490 scopus 로고    scopus 로고
    • Functional and biological properties of peptides obtained by enzymatic hydrolysis of whey proteins
    • Gauthier SF, Pouliot Y. Functional and biological properties of peptides obtained by enzymatic hydrolysis of whey proteins. J Dairy Sci. 2003; 86: E78-E87.
    • (2003) J Dairy Sci. , vol.86
    • Gauthier, S.F.1    Pouliot, Y.2
  • 7
    • 51049097278 scopus 로고    scopus 로고
    • The possible roles of food-derived bioactive peptides in reducing the risk of cardiovascular disease
    • Erdmann K, Cheung BWY, Schröder H. The possible roles of food-derived bioactive peptides in reducing the risk of cardiovascular disease. J Nutr Biochem. 2008; 19: 643-654.
    • (2008) J Nutr Biochem. , vol.19 , pp. 643-654
    • Erdmann, K.1    Cheung, B.W.Y.2    Schröder, H.3
  • 8
    • 3242774456 scopus 로고    scopus 로고
    • Angiotensin I-converting enzyme inhibitory peptides derived from food proteins and their physiological and pharmacological effects
    • Li G, Le G, Shi Y, Shrestha S. Angiotensin I-converting enzyme inhibitory peptides derived from food proteins and their physiological and pharmacological effects. Nutr Res. 2004; 24: 469-486.
    • (2004) Nutr Res. , vol.24 , pp. 469-486
    • Li, G.1    Le, G.2    Shi, Y.3    Shrestha, S.4
  • 9
    • 0037017785 scopus 로고    scopus 로고
    • Optimisation and validation of an angiotensin-converting enzyme inhibition assay for the screening of bioactive peptides
    • Vermeirssen V, Van Camp J, Verstraete W. Optimisation and validation of an angiotensin-converting enzyme inhibition assay for the screening of bioactive peptides. J Biochem Biophys Methods. 2002; 51: 75-87.
    • (2002) J Biochem Biophys Methods. , vol.51 , pp. 75-87
    • Vermeirssen, V.1    Van Camp, J.2    Verstraete, W.3
  • 10
    • 78751580546 scopus 로고    scopus 로고
    • Amaranth seed protein hydrolysates have in vivo and in vitro antihypertensive activity
    • Fritz M, Vecchi B, Rinaldi G, Añón MC. Amaranth seed protein hydrolysates have in vivo and in vitro antihypertensive activity. Food Chem. 2011; 126: 878-884.
    • (2011) Food Chem. , vol.126 , pp. 878-884
    • Fritz, M.1    Vecchi, B.2    Rinaldi, G.3    Añón, M.C.4
  • 11
    • 22244448044 scopus 로고    scopus 로고
    • ACE inhibitory activity in enzymatic hydrolysates of insect protein
    • Vercruysse L, Smagghe G, Herregods G, Van Camp J. ACE inhibitory activity in enzymatic hydrolysates of insect protein. J Agric Food Chem. 2005; 53: 5207-5211.
    • (2005) J Agric Food Chem. , vol.53 , pp. 5207-5211
    • Vercruysse, L.1    Smagghe, G.2    Herregods, G.3    Van Camp, J.4
  • 12
    • 70450257667 scopus 로고    scopus 로고
    • Angiotensin I converting enzyme (ACE) inhibitory activity and antihypertensive effect of fermented milk
    • Pihlanto A, Virtanen T, Korhonen H. Angiotensin I converting enzyme (ACE) inhibitory activity and antihypertensive effect of fermented milk. Int Dairy J. 2010; 20: 3-10.
    • (2010) Int Dairy J. , vol.20 , pp. 3-10
    • Pihlanto, A.1    Virtanen, T.2    Korhonen, H.3
  • 13
    • 44249117319 scopus 로고    scopus 로고
    • ACE-inhibitory peptides identified from the muscle protein hydrolysate of hard clam (Meretrix lusoria)
    • Tsai J, Chen J, Pan BS. ACE-inhibitory peptides identified from the muscle protein hydrolysate of hard clam (Meretrix lusoria). Process Biochem. 2008; 43: 743-747.
    • (2008) Process Biochem. , vol.43 , pp. 743-747
    • Tsai, J.1    Chen, J.2    Pan, B.S.3
  • 14
    • 68849118960 scopus 로고    scopus 로고
    • Angiotensin I-converting enzyme (ACE) inhibitory peptides from whey fermented by lactobacillus species
    • Ahn JE, Park SY, Atwal A, Gibbs BF, Lee BH. Angiotensin I-converting enzyme (ACE) inhibitory peptides from whey fermented by lactobacillus species. J Food Biochem. 2009; 33: 587-602.
    • (2009) J Food Biochem. , vol.33 , pp. 587-602
    • Ahn, J.E.1    Park, S.Y.2    Atwal, A.3    Gibbs, B.F.4    Lee, B.H.5
  • 15
    • 67349268149 scopus 로고    scopus 로고
    • Angiotensin I-converting enzyme-inhibitory peptide fractions from albumin 1 and globulin as obtained of amaranth grain
    • Tovar-Pérez EG, Guerrero-Legarreta I, Farrés-González A, Soriano-Santos J. Angiotensin I-converting enzyme-inhibitory peptide fractions from albumin 1 and globulin as obtained of amaranth grain. Food Chem. 2009; 116: 437-444.
    • (2009) Food Chem. , vol.116 , pp. 437-444
    • Tovar-Pérez, E.G.1    Guerrero-Legarreta, I.2    Farrés-González, A.3    Soriano-Santos, J.4
  • 16
    • 70449116398 scopus 로고    scopus 로고
    • Purification, activity and sequence of angiotensin converting enzyme inhibitory peptide from alcalase hydrolysate of peanut flour
    • Guang C, Phillips RD. Purification, activity and sequence of angiotensin converting enzyme inhibitory peptide from alcalase hydrolysate of peanut flour. J Agric Food Chem. 2009; 57: 10102-10106.
    • (2009) J Agric Food Chem. , vol.57 , pp. 10102-10106
    • Guang, C.1    Phillips, R.D.2
  • 17
    • 33646464385 scopus 로고    scopus 로고
    • Performance of two commonly used angiotensin-converting enzyme inhibition assays using FA-PGG and HHL as substrates
    • Shalaby SM, Zakora M, Otte J. Performance of two commonly used angiotensin-converting enzyme inhibition assays using FA-PGG and HHL as substrates. J Diary Res. 2006; 73: 178-186.
    • (2006) J Diary Res. , vol.73 , pp. 178-186
    • Shalaby, S.M.1    Zakora, M.2    Otte, J.3
  • 18
    • 13544276309 scopus 로고    scopus 로고
    • Direct spectrophotometric measurement of angiotensin I-converting enzyme inhibitory activity for screening bioactive peptides
    • Li G, Liu H, Shi Y, Le G. Direct spectrophotometric measurement of angiotensin I-converting enzyme inhibitory activity for screening bioactive peptides. J Pharm Biomed Anal. 2005; 37: 219-224.
    • (2005) J Pharm Biomed Anal. , vol.37 , pp. 219-224
    • Li, G.1    Liu, H.2    Shi, Y.3    Le, G.4
  • 19
    • 77952428375 scopus 로고    scopus 로고
    • Production and characterization of angiotensin converting enzyme (ACE) inhibitory peptides from apricot (Prunus armeniaca L.) kernel protein hydrolysate
    • Zhu Z, Qiu N, Yi J. Production and characterization of angiotensin converting enzyme (ACE) inhibitory peptides from apricot (Prunus armeniaca L.) kernel protein hydrolysate. Eur Food Res Technol. 2010; 231: 13-19.
    • (2010) Eur Food Res Technol. , vol.231 , pp. 13-19
    • Zhu, Z.1    Qiu, N.2    Yi, J.3
  • 20
    • 69449106743 scopus 로고    scopus 로고
    • A HPLC-UV method for the determination of angiotensin I-converting enzyme (ACE) inhibitory activity
    • Lahogue V, Réhel K, Taupin L, Haras D, Allaume P. A HPLC-UV method for the determination of angiotensin I-converting enzyme (ACE) inhibitory activity. Food Chem. 2010; 118: 870-875.
    • (2010) Food Chem. , vol.118 , pp. 870-875
    • Lahogue, V.1    Réhel, K.2    Taupin, L.3    Haras, D.4    Allaume, P.5
  • 22
    • 1642641507 scopus 로고    scopus 로고
    • Data smoothing: prediction of human behavior, detection of behavioral patterns, and monitoring treatment effectiveness in single-subject behavioral studies
    • Sideridis GD. Data smoothing: prediction of human behavior, detection of behavioral patterns, and monitoring treatment effectiveness in single-subject behavioral studies. J Behav Educ. 1997; 7: 191-203.
    • (1997) J Behav Educ. , vol.7 , pp. 191-203
    • Sideridis, G.D.1
  • 23
    • 84867397183 scopus 로고    scopus 로고
    • Modelling the effects of ageing time of starch on the enzymatic activity of three amylolytic enzymes
    • Guerra NP, Pastrana Castro L. Modelling the effects of ageing time of starch on the enzymatic activity of three amylolytic enzymes. Sci World J. 2012;2:1-13.
    • (2012) Sci World J. , vol.2 , pp. 1-13
    • Guerra, N.P.1    Pastrana Castro, L.2
  • 24
    • 0000873069 scopus 로고
    • A method for the solution of certain problems in least squares
    • Levenberg K. A method for the solution of certain problems in least squares. Quart Appl Math. 1944; 2012: 164-168.
    • (1944) Quart Appl Math. , vol.2012 , pp. 164-168
    • Levenberg, K.1
  • 25
    • 0000169232 scopus 로고
    • An algorithm for least-squares estimation of nonlinear parameters
    • Marquardt DW. An algorithm for least-squares estimation of nonlinear parameters. SIAM J Appl Math. 1963; 11: 431-441.
    • (1963) SIAM J Appl Math. , vol.11 , pp. 431-441
    • Marquardt, D.W.1
  • 26
    • 0036394055 scopus 로고    scopus 로고
    • Preparation of ovine and caprine β-lactoglobulin hydrolysates with ACE-inhibitory activity. Identification of active peptides from caprine β-lactoglobulin hydrolysed with thermolysin
    • Hernández-Ledesma B, Recio I, Ramos M, Amigo L. Preparation of ovine and caprine β-lactoglobulin hydrolysates with ACE-inhibitory activity. Identification of active peptides from caprine β-lactoglobulin hydrolysed with thermolysin. Int Dairy J. 2002; 12: 805-812.
    • (2002) Int Dairy J. , vol.12 , pp. 805-812
    • Hernández-Ledesma, B.1    Recio, I.2    Ramos, M.3    Amigo, L.4
  • 27
    • 33646168104 scopus 로고    scopus 로고
    • Effect of β-lactoglobulin hydrolysis with thermolysin under denaturing temperatures on the release of bioactive peptides
    • Hernández-Ledesma B, Ramos M, Recio I, Amigo L. Effect of β-lactoglobulin hydrolysis with thermolysin under denaturing temperatures on the release of bioactive peptides. J Chromatogr A. 2006; 1116: 31-37.
    • (2006) J Chromatogr A. , vol.1116 , pp. 31-37
    • Hernández-Ledesma, B.1    Ramos, M.2    Recio, I.3    Amigo, L.4
  • 28
    • 33748297647 scopus 로고    scopus 로고
    • Physiological, chemical and technological aspects of milk-protein-derived peptides with antihypertensive and ACE-inhibitory activity
    • López-Fandiño R, Otte J, van Camp J. Physiological, chemical and technological aspects of milk-protein-derived peptides with antihypertensive and ACE-inhibitory activity. Int Dairy J. 2006; 16: 1277-1293.
    • (2006) Int Dairy J. , vol.16 , pp. 1277-1293
    • López-Fandiño, R.1    Otte, J.2    van Camp, J.3
  • 29
    • 33644774599 scopus 로고    scopus 로고
    • Relationship between proteolysis and angiotensin-I-converting enzyme inhibition in different cheeses
    • Pripp AH, Sørensen R, Stepaniak L, Sørhaug T. Relationship between proteolysis and angiotensin-I-converting enzyme inhibition in different cheeses. LWT-Food Sci Technol. 2006; 39: 677-683.
    • (2006) LWT-Food Sci Technol. , vol.39 , pp. 677-683
    • Pripp, A.H.1    Sørensen, R.2    Stepaniak, L.3    Sørhaug, T.4
  • 30
    • 34548484135 scopus 로고    scopus 로고
    • Fractionation and identification of ACE-inhibitory peptides from α-lactalbumin and β-casein produced by thermolysin-catalysed hydrolysis
    • Otte J, Shalaby SMA, Zakora M, Nielsen MS. Fractionation and identification of ACE-inhibitory peptides from α-lactalbumin and β-casein produced by thermolysin-catalysed hydrolysis. Int Dairy J. 2007; 17: 1460-1472.
    • (2007) Int Dairy J. , vol.17 , pp. 1460-1472
    • Otte, J.1    Shalaby, S.M.A.2    Zakora, M.3    Nielsen, M.S.4
  • 31
    • 33847159988 scopus 로고    scopus 로고
    • Effect of heat and enzymatic treatment on the antihypertensive activity of whey protein hydrolysates
    • Lourenço da Costa E, Antonio da Rocha Gontijo J, Netto FM. Effect of heat and enzymatic treatment on the antihypertensive activity of whey protein hydrolysates. Int Dairy J. 2007; 17: 632-640.
    • (2007) Int Dairy J. , vol.17 , pp. 632-640
    • Lourenço da Costa, E.1    Antonio da Rocha Gontijo, J.2    Netto, F.M.3
  • 32
    • 24944554968 scopus 로고    scopus 로고
    • Mung-bean protein hydrolysates obtained with alcalase exhibit angiotensin I-converting enzyme inhibitory activity
    • Li GH, Le GW, Liu H, Shi YH. Mung-bean protein hydrolysates obtained with alcalase exhibit angiotensin I-converting enzyme inhibitory activity. Food Sci Technol Int. 2005; 11: 281-287.
    • (2005) Food Sci Technol Int. , vol.11 , pp. 281-287
    • Li, G.H.1    Le, G.W.2    Liu, H.3    Shi, Y.H.4
  • 33
    • 0033007311 scopus 로고    scopus 로고
    • Effect of chain length on absorption of biologically active peptides from the gastrointestinal tract
    • Roberts PR, Burney JD, Black KW, Zaloga GP. Effect of chain length on absorption of biologically active peptides from the gastrointestinal tract. Digestion. 1999; 60: 332-337.
    • (1999) Digestion. , vol.60 , pp. 332-337
    • Roberts, P.R.1    Burney, J.D.2    Black, K.W.3    Zaloga, G.P.4
  • 34
    • 0036397541 scopus 로고    scopus 로고
    • Optimisation of the angiotensin converting enzyme inhibition by whey protein hydrolysates using response surface methodology
    • Van der Ven C, Gruppen H, De Bont DBA, Voragen AGJ. Optimisation of the angiotensin converting enzyme inhibition by whey protein hydrolysates using response surface methodology. Int Dairy J. 2002; 12: 813-820.
    • (2002) Int Dairy J. , vol.12 , pp. 813-820
    • Van der Ven, C.1    Gruppen, H.2    De Bont, D.B.A.3    Voragen, A.G.J.4
  • 35
    • 0037009176 scopus 로고    scopus 로고
    • Dose-response relationships: an overview, a generative model and its application to the verification of descriptive models
    • Murado MA, González MP, Vázquez JA. Dose-response relationships: an overview, a generative model and its application to the verification of descriptive models. Enzyme Microb Technol. 2002; 31: 439-455.
    • (2002) Enzyme Microb Technol. , vol.31 , pp. 439-455
    • Murado, M.A.1    González, M.P.2    Vázquez, J.A.3
  • 36
    • 0020684765 scopus 로고
    • Substrate specificity and kinetic characteristics of angiotensin converting enzyme
    • Bünning P, Holmquist B, Riordan JF. Substrate specificity and kinetic characteristics of angiotensin converting enzyme. Biochemistry (N.Y.). 1983; 22: 103-110.
    • (1983) Biochemistry (N.Y.). , vol.22 , pp. 103-110
    • Bünning, P.1    Holmquist, B.2    Riordan, J.F.3
  • 37
    • 0033121263 scopus 로고    scopus 로고
    • Competitive inhibitors of the angiotensin-converting enzyme from the venom of the viper Echis multisquamatus
    • L'vov VM, Sadykov ÉS. Competitive inhibitors of the angiotensin-converting enzyme from the venom of the viper Echis multisquamatus. Chem Nat Compd. 1999; 35: 332-335.
    • (1999) Chem Nat Compd. , vol.35 , pp. 332-335
    • L'vov, V.M.1    Sadykov, E.2
  • 38
    • 0036836828 scopus 로고    scopus 로고
    • Novel peptidomimics as angiotensin-converting enzyme inhibitors: a combinatorial approach
    • Bala M, Qadar Pasha MA, Bhardwaj DK, Pasha S. Novel peptidomimics as angiotensin-converting enzyme inhibitors: a combinatorial approach. Bioorg Med Chem. 2002; 10: 3685-3691.
    • (2002) Bioorg Med Chem. , vol.10 , pp. 3685-3691
    • Bala, M.1    Qadar Pasha, M.A.2    Bhardwaj, D.K.3    Pasha, S.4
  • 39
    • 0036004573 scopus 로고    scopus 로고
    • Structure and activity of angiotensin I converting enzyme inhibitory peptides derived from alaskan pollack skin
    • Byun H, Kim S. Structure and activity of angiotensin I converting enzyme inhibitory peptides derived from alaskan pollack skin. J Biochem Mol Biol. 2002; 35: 239-243.
    • (2002) J Biochem Mol Biol. , vol.35 , pp. 239-243
    • Byun, H.1    Kim, S.2
  • 41
    • 0021733926 scopus 로고
    • Inhibition of angiotensin converting enzyme: dependence on chloride
    • Shapiro R, Riordan JF. Inhibition of angiotensin converting enzyme: dependence on chloride. Biochemistry (N.Y.). 1984; 23: 5234-5240.
    • (1984) Biochemistry (N.Y.). , vol.23 , pp. 5234-5240
    • Shapiro, R.1    Riordan, J.F.2
  • 42
    • 0034141231 scopus 로고    scopus 로고
    • Angiotensin I-converting enzyme inhibitory properties of whey protein digests: concentration and characterization of active peptides
    • Pihlanto-Leppälä A, Koskinen P, Phlola K, Tupasela T, Korhonen H. Angiotensin I-converting enzyme inhibitory properties of whey protein digests: concentration and characterization of active peptides. J Diary Res. 2000; 67: 53-64.
    • (2000) J Diary Res. , vol.67 , pp. 53-64
    • Pihlanto-Leppälä, A.1    Koskinen, P.2    Phlola, K.3    Tupasela, T.4    Korhonen, H.5
  • 43
    • 79955468271 scopus 로고    scopus 로고
    • Novel whey-derived peptides with inhibitory effect against angiotensin-converting enzyme: in vitro effect and stability to gastrointestinal enzymes
    • Tavares T, Contreras MDM, Amorim M, Pintado M, Recio I, Malcata FX. Novel whey-derived peptides with inhibitory effect against angiotensin-converting enzyme: in vitro effect and stability to gastrointestinal enzymes. Peptides. 2011; 32: 1013-1019.
    • (2011) Peptides. , vol.32 , pp. 1013-1019
    • Tavares, T.1    Contreras, M.D.M.2    Amorim, M.3    Pintado, M.4    Recio, I.5    Malcata, F.X.6


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