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Volumn 27, Issue , 2016, Pages 104-114

Isolation and biochemical characterisation of angiotensin-converting enzyme inhibitory peptides derived from the enzymatic hydrolysis of cupuassu seed protein isolate

Author keywords

ACE inhibitory activity; Bioactive peptides; Cupuassu seeds; Protein hydrolysates

Indexed keywords


EID: 84988039947     PISSN: 17564646     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jff.2016.08.048     Document Type: Article
Times cited : (18)

References (51)
  • 1
    • 0018536145 scopus 로고
    • Determination of the degree of hydrolysis of food protein hydrolysates by trinitrobenzenesulfonic acid
    • Adler-Nissen, J., Determination of the degree of hydrolysis of food protein hydrolysates by trinitrobenzenesulfonic 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
    • 84870781389 scopus 로고    scopus 로고
    • Angiotensin I converting enzyme (ACE) inhibitory peptides from salmon byproduct protein hydrolysate by alcalase hydrolysis
    • Ahn, C.B., Jeon, Y.J., Kim, Y.T., Je, J.Y., Angiotensin I converting enzyme (ACE) inhibitory peptides from salmon byproduct protein hydrolysate by alcalase hydrolysis. Process Biochemistry 47 (2012), 2240–2245.
    • (2012) Process Biochemistry , vol.47 , pp. 2240-2245
    • Ahn, C.B.1    Jeon, Y.J.2    Kim, Y.T.3    Je, J.Y.4
  • 4
    • 49749107397 scopus 로고
    • Official Methods of Analysis of AOAC International
    • 16th ed. AOAC Arlington 2 v
    • AOAC, Official Methods of Analysis of AOAC International. 16th ed., 1995, AOAC, Arlington 2 v.
    • (1995)
    • AOAC1
  • 5
    • 0004268863 scopus 로고    scopus 로고
    • Proteolytic enzymes: A Practical Approach
    • 2nd ed. Oxford University Press Oxford, UK 340p
    • Beynon, R., Bond, J.S., Proteolytic enzymes: A Practical Approach. 2nd ed., 2001, Oxford University Press, Oxford, UK 340p.
    • (2001)
    • Beynon, R.1    Bond, J.S.2
  • 6
    • 0142220894 scopus 로고
    • Fruticultura tropical: o cupuaçuzeiro – cultivo, beneficiamento e utilização do fruto
    • EMBRAPA, CPATU Belém
    • Calzavara, B.B.G., Muller, C.H., Kahwage, O.N.C., Fruticultura tropical: o cupuaçuzeiro – cultivo, beneficiamento e utilização do fruto. 1984, EMBRAPA, CPATU, Belém.
    • (1984)
    • Calzavara, B.B.G.1    Muller, C.H.2    Kahwage, O.N.C.3
  • 7
    • 34248672821 scopus 로고    scopus 로고
    • A continuous fluorescence resonance energy transfer angiotensin I-converting enzyme assay
    • Carmona, A.K., Schwager, S.L., Juliano, M.A., Juliano, L., Sturrock, E.D., A continuous fluorescence resonance energy transfer angiotensin I-converting enzyme assay. Nature Protocols, 1, 2006, 04.
    • (2006) Nature Protocols , vol.1 , pp. 04
    • Carmona, A.K.1    Schwager, S.L.2    Juliano, M.A.3    Juliano, L.4    Sturrock, E.D.5
  • 8
    • 84987979736 scopus 로고    scopus 로고
    • Caracterização de concentrado e isolado proteico extraído de sementes de cupuaçu (Theobroma grandiflorum, Schum)
    • Carvalho, A.V., Pezoa-Garcia, N.H., Amaya-Farfan, J., Caracterização de concentrado e isolado proteico extraído de sementes de cupuaçu (Theobroma grandiflorum, Schum). Brazilian Journal of Food Technology 12 (2009), 1–8.
    • (2009) Brazilian Journal of Food Technology , vol.12 , pp. 1-8
    • Carvalho, A.V.1    Pezoa-Garcia, N.H.2    Amaya-Farfan, J.3
  • 9
    • 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
    • Chen, J., Wang, Y., Zhong, Q., Wu, J., Xia, W., Purification and characterization of a novel angiotensin-I converting enzyme (ACE) inhibitory peptide derived from enzymatic hydrolysate of grass carp protein. Peptides 33 (2012), 52–58.
    • (2012) Peptides , vol.33 , pp. 52-58
    • Chen, J.1    Wang, Y.2    Zhong, Q.3    Wu, J.4    Xia, W.5
  • 10
    • 0019332139 scopus 로고
    • Binding of peptide substrates and inhibitors of angiotensin-converting enzyme importance of the COOH-terminal dipeptide sequence
    • Cheung, H.S., Wang, F.L., Ondetti, M.A., Sabo, E.F., Cushman, D.W., Binding of peptide substrates and inhibitors of angiotensin-converting enzyme importance of the COOH-terminal dipeptide sequence. The Journal of Biological Chemistry 255 (1980), 401–405.
    • (1980) The Journal of Biological Chemistry , vol.255 , pp. 401-405
    • Cheung, H.S.1    Wang, F.L.2    Ondetti, M.A.3    Sabo, E.F.4    Cushman, D.W.5
  • 11
    • 51049097278 scopus 로고    scopus 로고
    • The possible roles of food-derived bioactive peptides in reducing the risk of cardiovascular disease
    • Erdmann, K., Cheung, W.Y.B., Schroder, H., The possible roles of food-derived bioactive peptides in reducing the risk of cardiovascular disease. Journal of Nutritional Biochemistry v:19 (2008), 643–654.
    • (2008) Journal of Nutritional Biochemistry , vol.5 , Issue.19 , pp. 643-654
    • Erdmann, K.1    Cheung, W.Y.B.2    Schroder, H.3
  • 12
    • 0033860508 scopus 로고    scopus 로고
    • Classification and antihypertensive activity of angiotensin I-converting enzyme inhibitory peptides derived from food proteins
    • Fujita, H., Yokoyama, K., Yoshikawa, M., Classification and antihypertensive activity of angiotensin I-converting enzyme inhibitory peptides derived from food proteins. Journal of Food Science 65 (2000), 564–569.
    • (2000) Journal of Food Science , vol.65 , pp. 564-569
    • Fujita, H.1    Yokoyama, K.2    Yoshikawa, M.3
  • 13
    • 0033823597 scopus 로고    scopus 로고
    • Production of angiotensin-I-converting-enzyme-inhibitory peptides in fermented milks started by Lactobacillus delbrueckii subsp. bulgaricus SS1 and Lactococcus lactis subsp. cremoris FT4
    • Gobbetti, M., Ferranti, P., Smacchi, E., Goffredi, F., Addeo, F., Production of angiotensin-I-converting-enzyme-inhibitory peptides in fermented milks started by Lactobacillus delbrueckii subsp. bulgaricus SS1 and Lactococcus lactis subsp. cremoris FT4. Applied and Environment Microbiology 66 (2000), 3898–3904.
    • (2000) Applied and Environment Microbiology , vol.66 , pp. 3898-3904
    • Gobbetti, M.1    Ferranti, P.2    Smacchi, E.3    Goffredi, F.4    Addeo, F.5
  • 15
    • 84879200325 scopus 로고    scopus 로고
    • LC–MS/MS coupled with QSAR modeling in characterizing of angiotensin I-converting enzyme inhibitory peptides from soybean proteins
    • Gu, Y., Wu, J., LC–MS/MS coupled with QSAR modeling in characterizing of angiotensin I-converting enzyme inhibitory peptides from soybean proteins. Food Chemistry 141 (2013), 2682–2690.
    • (2013) Food Chemistry , vol.141 , pp. 2682-2690
    • Gu, Y.1    Wu, J.2
  • 16
    • 0021312893 scopus 로고
    • Amino acid analysis by reverse-phase high performance liquid chromatography: Precolumn derivatization with phenylisothiocyanate
    • Heinrikson, R.L., Meredith, S.C., Amino acid analysis by reverse-phase high performance liquid chromatography: Precolumn derivatization with phenylisothiocyanate. Analytical Biochemistry 136 (1984), 65–74.
    • (1984) Analytical Biochemistry , vol.136 , pp. 65-74
    • Heinrikson, R.L.1    Meredith, S.C.2
  • 17
    • 75749122983 scopus 로고    scopus 로고
    • Influence of degree of hydrolysis on functional properties, antioxidant activity and ACE inhibitory activity of peanut protein hydrolysate
    • Jamdar, S.N., Rajalakshimi, V., Pednekar, M.D., Juan, F., YardiI, V., Sharma, A., Influence of degree of hydrolysis on functional properties, antioxidant activity and ACE inhibitory activity of peanut protein hydrolysate. Food Chemistry 121 (2010), 178–184.
    • (2010) Food Chemistry , vol.121 , pp. 178-184
    • Jamdar, S.N.1    Rajalakshimi, V.2    Pednekar, M.D.3    Juan, F.4    YardiI, V.5    Sharma, A.6
  • 18
    • 77349090649 scopus 로고    scopus 로고
    • Development and biological activities of marine-derived bioactive peptides: A review
    • Kim, S.K., Wijesekara, I., Development and biological activities of marine-derived bioactive peptides: A review. Journal of Functional Foods 2 (2010), 1–9.
    • (2010) Journal of Functional Foods , vol.2 , pp. 1-9
    • Kim, S.K.1    Wijesekara, I.2
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • 1970
    • Laemmli, U.K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, London 227 (1970), 680–685 1970.
    • (1970) Nature, London , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 20
    • 84887192119 scopus 로고    scopus 로고
    • Novel angiotensin I-converting enzyme inhibitory peptides derived from edible mushroom Agaricus bisporus (J.E. Lange) Imbach identified by LC–MS/MS
    • Lau, C.C., Abdullah, N., Shuib, A.S., Aminudin, N., Novel angiotensin I-converting enzyme inhibitory peptides derived from edible mushroom Agaricus bisporus (J.E. Lange) Imbach identified by LC–MS/MS. Food Chemistry 148 (2014), 396–401.
    • (2014) Food Chemistry , vol.148 , pp. 396-401
    • Lau, C.C.1    Abdullah, N.2    Shuib, A.S.3    Aminudin, N.4
  • 21
    • 80053063462 scopus 로고    scopus 로고
    • GraFit version 7
    • Erithacus Software Ltd. Horley, UK
    • Leatherbarrow, R.J., GraFit version 7. 2009, Erithacus Software Ltd., Horley, UK.
    • (2009)
    • Leatherbarrow, R.J.1
  • 24
    • 84904012978 scopus 로고    scopus 로고
    • Tryptophan-containing dipeptides are C-domain selective inhibitors of angiotensin converting enzyme
    • Lunow, D., Kaiser, S., Ruckriemen, J., Phil, C., Henle, T., Tryptophan-containing dipeptides are C-domain selective inhibitors of angiotensin converting enzyme. Food Chemistry 166 (2015), 596–602.
    • (2015) Food Chemistry , vol.166 , pp. 596-602
    • Lunow, D.1    Kaiser, S.2    Ruckriemen, J.3    Phil, C.4    Henle, T.5
  • 26
    • 51049085868 scopus 로고    scopus 로고
    • Membrane-based fractionation and purification strategies for bioactive peptides
    • Y. Mine F. Shahidi Taylor & Francis Group Boca Raton, FL
    • Mine, Y., Shahidi, F., Membrane-based fractionation and purification strategies for bioactive peptides. Mine, Y., Shahidi, F., (eds.) Nutraceutical proteins and peptides in health and disease, 2006, Taylor & Francis Group, Boca Raton, FL, 639–658.
    • (2006) Nutraceutical proteins and peptides in health and disease , pp. 639-658
    • Mine, Y.1    Shahidi, F.2
  • 29
    • 0029937138 scopus 로고    scopus 로고
    • Synthetic peptides corresponding to α-lactalbumin and β-lactoglobulin sequences with angiotensin-I-converting enzyme inhibitory activity
    • Mullally, M.M., Meisel, H., Fitzgerald, R.J., Synthetic peptides corresponding to α-lactalbumin and β-lactoglobulin sequences with angiotensin-I-converting enzyme inhibitory activity. Biological Chemistry Hoppe-Seyler 377 (1996), 259–260.
    • (1996) Biological Chemistry Hoppe-Seyler , vol.377 , pp. 259-260
    • Mullally, M.M.1    Meisel, H.2    Fitzgerald, R.J.3
  • 30
    • 0029286291 scopus 로고
    • Purification and characterization of angiotensin I-converting enzyme inhibitors from sour milk
    • Nakamura, Y., Yamamoto, N., Sakai, K., Yamazaki, S., Takano, T., Purification and characterization of angiotensin I-converting enzyme inhibitors from sour milk. Journal of Dairy Science 78 (1995), 777–783.
    • (1995) Journal of Dairy Science , vol.78 , pp. 777-783
    • Nakamura, Y.1    Yamamoto, N.2    Sakai, K.3    Yamazaki, S.4    Takano, T.5
  • 31
    • 84858439144 scopus 로고    scopus 로고
    • Lehninger, principles of biochemistry
    • 4th ed. W. H. Freeman New York; 1216 pp
    • Nelson, D.L., Cox, M.M., Lehninger, principles of biochemistry. 4th ed., 2005, W. H. Freeman New York; 1216 pp.
    • (2005)
    • Nelson, D.L.1    Cox, M.M.2
  • 32
    • 84860997466 scopus 로고    scopus 로고
    • Inhibition mechanism and model of an angiotensin I-converting enzyme (ACE)-inhibitory hexapeptide from yeast (Saccharomyces cerevisiae)
    • Ni, H., Li, L., Liu, G., Hu, S.Q., Inhibition mechanism and model of an angiotensin I-converting enzyme (ACE)-inhibitory hexapeptide from yeast (Saccharomyces cerevisiae). PLoS ONE, 7, 2012, 5.
    • (2012) PLoS ONE , vol.7 , pp. 5
    • Ni, H.1    Li, L.2    Liu, G.3    Hu, S.Q.4
  • 33
    • 70349193230 scopus 로고    scopus 로고
    • Reliable and inexpensive colorimetric method for determining protein-bound tryptophan in maize kernels
    • Nurit, E., Tiessen, A., Pixley, K.V., Palacios-Rojas, N., Reliable and inexpensive colorimetric method for determining protein-bound tryptophan in maize kernels. Journal of Agricultural and Food Chemistry 57 (2009), 7233–7338.
    • (2009) Journal of Agricultural and Food Chemistry , vol.57 , pp. 7233-7338
    • Nurit, E.1    Tiessen, A.2    Pixley, K.V.3    Palacios-Rojas, N.4
  • 34
    • 36148988384 scopus 로고    scopus 로고
    • Cryptides: Buried secrets in proteins
    • Pimenta, D.C., Lebrun, I., Cryptides: Buried secrets in proteins. Peptides 28 (2007), 2403–2410.
    • (2007) Peptides , vol.28 , pp. 2403-2410
    • Pimenta, D.C.1    Lebrun, I.2
  • 35
    • 57849148533 scopus 로고    scopus 로고
    • Angiotensin converting enzyme inhibitory activity of proteolytic digests of peanut (Arachis hypogaea L.) flour
    • Quist, E.E., Phillips, R.D., Saalia, F.K., Angiotensin converting enzyme inhibitory activity of proteolytic digests of peanut (Arachis hypogaea L.) flour. Food Science and Technology 42 (2009), 694–699.
    • (2009) Food Science and Technology , vol.42 , pp. 694-699
    • Quist, E.E.1    Phillips, R.D.2    Saalia, F.K.3
  • 36
    • 77950871987 scopus 로고    scopus 로고
    • Milk protein peptides with angiotensin I-converting enzyme inhibitory (ACEI) activity
    • Ricci, A.R., Olalla, M., Milk protein peptides with angiotensin I-converting enzyme inhibitory (ACEI) activity. Critical Reviews in Food Science and Nutrition 50:5 (2010), 390–402.
    • (2010) Critical Reviews in Food Science and Nutrition , vol.50 , Issue.5 , pp. 390-402
    • Ricci, A.R.1    Olalla, M.2
  • 38
    • 75149190029 scopus 로고    scopus 로고
    • Bioactive proteins and peptides in pulse crops: Pea, chickpea and lentil
    • Roy, F., Boye, J.I., Simpson, B.K., Bioactive proteins and peptides in pulse crops: Pea, chickpea and lentil. Food Research International 43 (2010), 432–442.
    • (2010) Food Research International , vol.43 , pp. 432-442
    • Roy, F.1    Boye, J.I.2    Simpson, B.K.3
  • 39
    • 0028526513 scopus 로고
    • Structure and activity of angiotensin I converting enzyme inhibitory peptides from sake and sake lees
    • Saito, Y., Wanezaki, K., Kawato, A., Imayasu, S., Structure and activity of angiotensin I converting enzyme inhibitory peptides from sake and sake lees. Bioscience, Biotechnology, and Biochemistry 58:10 (1994), 1767–1771.
    • (1994) Bioscience, Biotechnology, and Biochemistry , vol.58 , Issue.10 , pp. 1767-1771
    • Saito, Y.1    Wanezaki, K.2    Kawato, A.3    Imayasu, S.4
  • 40
    • 78651464827 scopus 로고    scopus 로고
    • Antioxidant and angiotensin converting enzyme (ACE) inhibitory activities of cocoa (Theobroma cacao L.) autolysates
    • Samadi, B., Ismail, A., Hamid, M., Antioxidant and angiotensin converting enzyme (ACE) inhibitory activities of cocoa (Theobroma cacao L.) autolysates. Food Research International 44 (2011), 290–296.
    • (2011) Food Research International , vol.44 , pp. 290-296
    • Samadi, B.1    Ismail, A.2    Hamid, M.3
  • 42
    • 0032124780 scopus 로고    scopus 로고
    • Isolation and characterization of angiotensin I-converting enzyme inhibitor dipeptides derived from Allium sativum L (garlic)
    • Suetsuna, K., Isolation and characterization of angiotensin I-converting enzyme inhibitor dipeptides derived from Allium sativum L (garlic). Journal of Nutritional Biochemistry 9 (1998), 415–419.
    • (1998) Journal of Nutritional Biochemistry , vol.9 , pp. 415-419
    • Suetsuna, K.1
  • 43
    • 65849145033 scopus 로고    scopus 로고
    • Characterization and ACE-Inhibitory activity of amaranth proteins
    • Tiengo, A., Faria, M., Netto, F.M., Characterization and ACE-Inhibitory activity of amaranth proteins. Journal of Food Science 74:5 (2009), H121–H126.
    • (2009) Journal of Food Science , vol.74 , Issue.5 , pp. H121-H126
    • Tiengo, A.1    Faria, M.2    Netto, F.M.3
  • 44
    • 84866782465 scopus 로고    scopus 로고
    • Novel angiotensin I-converting enzyme inhibitory peptides derived from soya milk
    • Tomatsu, W., Shimakage, A., Shinho, M., Yamada, S., Takahashi, S., Novel angiotensin I-converting enzyme inhibitory peptides derived from soya milk. Food Chemistry 136 (2013), 612–616.
    • (2013) Food Chemistry , vol.136 , pp. 612-616
    • Tomatsu, W.1    Shimakage, A.2    Shinho, M.3    Yamada, S.4    Takahashi, S.5
  • 45
    • 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. Journal of Food Science 77 (2012), R11–R24.
    • (2012) Journal of Food Science , vol.77 , pp. R11-R24
    • Udenigwe, C.C.1    Aluko, R.E.2
  • 46
    • 0036397541 scopus 로고    scopus 로고
    • Optimisation of the angiotensin converting enzyme inhibition by whey protein hydrolysates using response surface methodology
    • Ven, C.V.V., Gruppen, H., Bont, D.B.A., Voragen, A.G.J., Optimisation of the angiotensin converting enzyme inhibition by whey protein hydrolysates using response surface methodology. International Dairy Journal 12 (2002), 813–820.
    • (2002) International Dairy Journal , vol.12 , pp. 813-820
    • Ven, C.V.V.1    Gruppen, H.2    Bont, D.B.A.3    Voragen, A.G.J.4
  • 47
    • 0004053611 scopus 로고    scopus 로고
    • Biochemistry
    • 4th ed. John Wiley & Sons New York
    • Voet, D., Voet, J.G., Biochemistry. 4th ed., 2011, John Wiley & Sons, New York.
    • (2011)
    • Voet, D.1    Voet, J.G.2
  • 48
    • 0027288745 scopus 로고
    • The major seed protein of Theobroma cacao. L
    • Voigt, J., Biehl, B., Wazir, S.K.S., The major seed protein of Theobroma cacao. L. Food Chemistry 47 (1993), 145–151.
    • (1993) Food Chemistry , vol.47 , pp. 145-151
    • Voigt, J.1    Biehl, B.2    Wazir, S.K.S.3
  • 49
    • 0027965355 scopus 로고
    • In vitro studies on the proteolytic formation of the characteristic aroma precursors of fermented cocoa seeds: The significance of endoprotease specificity
    • Voigt, J., Voigt, G., Heinrichs, V.H., Wrann, D., Biehl, B., In vitro studies on the proteolytic formation of the characteristic aroma precursors of fermented cocoa seeds: The significance of endoprotease specificity. Food Chemistry 51 (1994), 7–14.
    • (1994) Food Chemistry , vol.51 , pp. 7-14
    • Voigt, J.1    Voigt, G.2    Heinrichs, V.H.3    Wrann, D.4    Biehl, B.5
  • 50
    • 0032839901 scopus 로고    scopus 로고
    • Phylogenetic relationships of Theobroma and Herrania (Sterculiaceae) based on sequences of the nuclear gene vicilin
    • 1999
    • Whitlock, B.A., Baum, D.A., Phylogenetic relationships of Theobroma and Herrania (Sterculiaceae) based on sequences of the nuclear gene vicilin. Systematic Botany 24 (1999), 128–138 1999.
    • (1999) Systematic Botany , vol.24 , pp. 128-138
    • Whitlock, B.A.1    Baum, D.A.2
  • 51
    • 0037409169 scopus 로고    scopus 로고
    • Production of ace inhibitory peptides by digestion of chickpea legumin with alcalase
    • Yust, M.M., Pedroche, J., Girón-Calle, J., Aaiz, M., Millán, F., Vioque, J., Production of ace inhibitory peptides by digestion of chickpea legumin with alcalase. Food Chemistry 81 (2003), 363–369.
    • (2003) Food Chemistry , vol.81 , pp. 363-369
    • Yust, M.M.1    Pedroche, J.2    Girón-Calle, J.3    Aaiz, M.4    Millán, F.5    Vioque, J.6


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