메뉴 건너뛰기




Volumn 94, Issue , 2017, Pages 79-89

Release of dipeptidyl peptidase IV (DPP-IV) inhibitory peptides from milk protein isolate (MPI) during enzymatic hydrolysis

Author keywords

Bioactive peptides; Dipeptidyl peptidase IV inhibition; Milk protein isolate; Response surface methodology; Trypsin

Indexed keywords

DESIGN OF EXPERIMENTS; LIQUID CHROMATOGRAPHY; MASS SPECTROMETRY; PEPTIDES; SURFACE PROPERTIES;

EID: 85012271455     PISSN: 09639969     EISSN: 18737145     Source Type: Journal    
DOI: 10.1016/j.foodres.2017.02.004     Document Type: Article
Times cited : (73)

References (48)
  • 1
    • 84924807170 scopus 로고    scopus 로고
    • Innovative uses of milk protein concentrates in product development
    • Agarwal, S., Beausire, R.L., Patel, S., Patel, H., Innovative uses of milk protein concentrates in product development. Journal of Food Science 80:S1 (2015), A23–A29.
    • (2015) Journal of Food Science , vol.80 , Issue.S1 , pp. A23-A29
    • Agarwal, S.1    Beausire, R.L.2    Patel, S.3    Patel, H.4
  • 2
    • 84908256009 scopus 로고    scopus 로고
    • Determination of the influence of substrate concentration on enzyme selectivity using whey protein isolate and Bacillus licheniformis protease
    • Butré, C.I., Sforza, S., Gruppen, H., Wierenga, P.A., Determination of the influence of substrate concentration on enzyme selectivity using whey protein isolate and Bacillus licheniformis protease. Journal of Agricultural and Food Chemistry 62:42 (2014), 10230–10239.
    • (2014) Journal of Agricultural and Food Chemistry , vol.62 , Issue.42 , pp. 10230-10239
    • Butré, C.I.1    Sforza, S.2    Gruppen, H.3    Wierenga, P.A.4
  • 3
    • 84922352620 scopus 로고    scopus 로고
    • Determination of the influence of the pH of hydrolysis on enzyme selectivity of Bacillus licheniformis protease towards whey protein isolate
    • Butré, C.I., Sforza, S., Wierenga, P.A., Gruppen, H., Determination of the influence of the pH of hydrolysis on enzyme selectivity of Bacillus licheniformis protease towards whey protein isolate. International Dairy Journal 44 (2015), 44–53.
    • (2015) International Dairy Journal , vol.44 , pp. 44-53
    • Butré, C.I.1    Sforza, S.2    Wierenga, P.A.3    Gruppen, H.4
  • 4
    • 77049102128 scopus 로고    scopus 로고
    • Influence of temperature and degree of hydrolysis on the peptide composition of trypsin hydrolysates of β-lactoglobulin: Analysis by LC–ESI-TOF/MS
    • Cheison, S.C., Schmitt, M., Leeb, E., Letzel, T., Kulozik, U., Influence of temperature and degree of hydrolysis on the peptide composition of trypsin hydrolysates of β-lactoglobulin: Analysis by LC–ESI-TOF/MS. Food Chemistry 121:2 (2010), 457–467.
    • (2010) Food Chemistry , vol.121 , Issue.2 , pp. 457-467
    • Cheison, S.C.1    Schmitt, M.2    Leeb, E.3    Letzel, T.4    Kulozik, U.5
  • 6
    • 77956875053 scopus 로고    scopus 로고
    • Production of antioxidant hydrolyzates from a whey protein concentrate with thermolysin: Optimization by response surface methodology
    • Contreras, M.D.M., Hernández-Ledesma, B., Amigo, L., Martín-Álvarez, P.J., Recio, I., Production of antioxidant hydrolyzates from a whey protein concentrate with thermolysin: Optimization by response surface methodology. LWT - Food Science and Technology 44:1 (2011), 9–15.
    • (2011) LWT - Food Science and Technology , vol.44 , Issue.1 , pp. 9-15
    • Contreras, M.D.M.1    Hernández-Ledesma, B.2    Amigo, L.3    Martín-Álvarez, P.J.4    Recio, I.5
  • 7
    • 33644618433 scopus 로고    scopus 로고
    • The biology of incretin hormones
    • Drucker, D.J., The biology of incretin hormones. Cell Metabolism 3:3 (2006), 153–165.
    • (2006) Cell Metabolism , vol.3 , Issue.3 , pp. 153-165
    • Drucker, D.J.1
  • 9
    • 0002662145 scopus 로고    scopus 로고
    • Protein modification
    • T. Godfrey S. West 2nd ed. Macmillan Press London
    • Godfrey, T., Protein modification. Godfrey, T., West, S., (eds.) Industrial enzymology, 2nd ed., 1996, Macmillan Press, London, 303–325.
    • (1996) Industrial enzymology , pp. 303-325
    • Godfrey, T.1
  • 10
    • 84959370147 scopus 로고    scopus 로고
    • In silico, in vitro and in vivo analyses of dipeptidyl peptidase IV inhibitory activity and the antidiabetic effect of sodium caseinate hydrolysate
    • Hsieh, C.-H., Wang, T.-Y., Hung, C.-C., Jao, C.-L., Hsieh, Y.-L., Wu, S.-X., Hsu, K.-C., In silico, in vitro and in vivo analyses of dipeptidyl peptidase IV inhibitory activity and the antidiabetic effect of sodium caseinate hydrolysate. Food & Function 7:2 (2016), 1122–1128.
    • (2016) Food & Function , vol.7 , Issue.2 , pp. 1122-1128
    • Hsieh, C.-H.1    Wang, T.-Y.2    Hung, C.-C.3    Jao, C.-L.4    Hsieh, Y.-L.5    Wu, S.-X.6    Hsu, K.-C.7
  • 11
    • 0036124772 scopus 로고    scopus 로고
    • Proteolysis of bovine β-lactoglobulin during thermal treatment in subdenaturing conditions highlights some structural features of the temperature-modified protein and yields fragments with low immunoreactivity
    • Iametti, S., Rasmussen, P., Frøkiær, H., Ferranti, P., Addeo, F., Bonomi, F., Proteolysis of bovine β-lactoglobulin during thermal treatment in subdenaturing conditions highlights some structural features of the temperature-modified protein and yields fragments with low immunoreactivity. European Journal of Biochemistry 269:5 (2002), 1362–1372.
    • (2002) European Journal of Biochemistry , vol.269 , Issue.5 , pp. 1362-1372
    • Iametti, S.1    Rasmussen, P.2    Frøkiær, H.3    Ferranti, P.4    Addeo, F.5    Bonomi, F.6
  • 12
    • 84939520179 scopus 로고    scopus 로고
    • The development of bioactive peptides from dietary proteins as a dipeptidyl peptidase IV inhibitor for the management of type 2 diabetes
    • Jao, C.-L., Hung, C.-C., Tung, Y.-S., Lin, P.-Y., Chen, M.-C., Hsu, K.-C., The development of bioactive peptides from dietary proteins as a dipeptidyl peptidase IV inhibitor for the management of type 2 diabetes. Biomedicine 5:3 (2015), 9–15.
    • (2015) Biomedicine , vol.5 , Issue.3 , pp. 9-15
    • Jao, C.-L.1    Hung, C.-C.2    Tung, Y.-S.3    Lin, P.-Y.4    Chen, M.-C.5    Hsu, K.-C.6
  • 13
    • 84897390441 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV and its inhibitors: Therapeutics for type 2 diabetes and what else?
    • Juillerat-Jeanneret, L., Dipeptidyl peptidase IV and its inhibitors: Therapeutics for type 2 diabetes and what else?. Journal of Medicinal Chemistry 57:6 (2014), 2197–2212.
    • (2014) Journal of Medicinal Chemistry , vol.57 , Issue.6 , pp. 2197-2212
    • Juillerat-Jeanneret, L.1
  • 14
    • 84860318855 scopus 로고    scopus 로고
    • Evaluation of the potential of dietary proteins as precursors of dipeptidyl peptidase (DPP)-IV inhibitors by an in silico approach
    • Lacroix, I.M.E., Li-Chan, E.C.Y., Evaluation of the potential of dietary proteins as precursors of dipeptidyl peptidase (DPP)-IV inhibitors by an in silico approach. Journal of Functional Foods 4:2 (2012), 403–422.
    • (2012) Journal of Functional Foods , vol.4 , Issue.2 , pp. 403-422
    • Lacroix, I.M.E.1    Li-Chan, E.C.Y.2
  • 15
    • 84893330854 scopus 로고    scopus 로고
    • Isolation and characterization of peptides with dipeptidyl peptidase-IV inhibitory activity from pepsin-treated bovine whey proteins
    • Lacroix, I.M.E., Li-Chan, E.C.Y., Isolation and characterization of peptides with dipeptidyl peptidase-IV inhibitory activity from pepsin-treated bovine whey proteins. Peptides 54 (2014), 39–48.
    • (2014) Peptides , vol.54 , pp. 39-48
    • Lacroix, I.M.E.1    Li-Chan, E.C.Y.2
  • 16
    • 84891428257 scopus 로고    scopus 로고
    • Overview of food products and dietary constituents with antidiabetic properties and their putative mechanisms of action: A natural approach to complement pharmacotherapy in the management of diabetes
    • Lacroix, I.M.E., Li-Chan, E.C.Y., Overview of food products and dietary constituents with antidiabetic properties and their putative mechanisms of action: A natural approach to complement pharmacotherapy in the management of diabetes. Molecular Nutrition & Food Research 58:1 (2014), 61–78.
    • (2014) Molecular Nutrition & Food Research , vol.58 , Issue.1 , pp. 61-78
    • Lacroix, I.M.E.1    Li-Chan, E.C.Y.2
  • 17
    • 84971412805 scopus 로고    scopus 로고
    • Food-derived dipeptidyl-peptidase IV inhibitors as a potential approach for glycemic regulation – Current knowledge and future research considerations
    • Lacroix, I.M.E., Li-Chan, E.C.Y., Food-derived dipeptidyl-peptidase IV inhibitors as a potential approach for glycemic regulation – Current knowledge and future research considerations. Trends in Food Science & Technology 54 (2016), 1–16.
    • (2016) Trends in Food Science & Technology , vol.54 , pp. 1-16
    • Lacroix, I.M.E.1    Li-Chan, E.C.Y.2
  • 18
    • 84915821684 scopus 로고    scopus 로고
    • Analyzing a dipeptide library to identify human dipeptidyl peptidase IV inhibitor
    • Lan, V.T.T., Ito, K., Ohno, M., Motoyama, T., Ito, S., Kawarasaki, Y., Analyzing a dipeptide library to identify human dipeptidyl peptidase IV inhibitor. Food Chemistry 175 (2015), 66–73.
    • (2015) Food Chemistry , vol.175 , pp. 66-73
    • Lan, V.T.T.1    Ito, K.2    Ohno, M.3    Motoyama, T.4    Ito, S.5    Kawarasaki, Y.6
  • 19
    • 84949088240 scopus 로고    scopus 로고
    • Identification of short peptide sequences in the nanofiltration permeate of a bioactive whey protein hydrolysate
    • Le Maux, S., Nongonierma, A.B., Murray, B., Kelly, P.M., FitzGerald, R.J., Identification of short peptide sequences in the nanofiltration permeate of a bioactive whey protein hydrolysate. Food Research International 77 (2015), 534–539.
    • (2015) Food Research International , vol.77 , pp. 534-539
    • Le Maux, S.1    Nongonierma, A.B.2    Murray, B.3    Kelly, P.M.4    FitzGerald, R.J.5
  • 20
    • 84949571305 scopus 로고    scopus 로고
    • Enzymatic generation of whey protein hydrolysates under pH-controlled and non pH-controlled conditions: Impact on physicochemical and bioactive properties
    • Le Maux, S., Nongonierma, A.B., Barre, C., FitzGerald, R.J., Enzymatic generation of whey protein hydrolysates under pH-controlled and non pH-controlled conditions: Impact on physicochemical and bioactive properties. Food Chemistry 199 (2016), 246–251.
    • (2016) Food Chemistry , vol.199 , pp. 246-251
    • Le Maux, S.1    Nongonierma, A.B.2    Barre, C.3    FitzGerald, R.J.4
  • 21
    • 0000081341 scopus 로고
    • Proteolytic and peptidolytic activities in commercial pancreatic protease preparations and their relationship to some whey protein hydrolyzate characteristics
    • Mullally, M.M., O'Callaghan, D.M., FitzGerald, R.J., Donnelly, W., Dalton, J.P., Proteolytic and peptidolytic activities in commercial pancreatic protease preparations and their relationship to some whey protein hydrolyzate characteristics. Journal of Agricultural and Food Chemistry 42:12 (1994), 2973–2981.
    • (1994) Journal of Agricultural and Food Chemistry , vol.42 , Issue.12 , pp. 2973-2981
    • Mullally, M.M.1    O'Callaghan, D.M.2    FitzGerald, R.J.3    Donnelly, W.4    Dalton, J.P.5
  • 22
    • 84988411849 scopus 로고    scopus 로고
    • Bioactive peptides from Atlantic salmon (Salmo salar) with angiotensin converting enzyme and dipeptidyl peptidase IV inhibitory, and antioxidant activities
    • Neves, A.C., Harnedy, P.A., O'Keeffe, M.B., FitzGerald, R.J., Bioactive peptides from Atlantic salmon (Salmo salar) with angiotensin converting enzyme and dipeptidyl peptidase IV inhibitory, and antioxidant activities. Food Chemistry 218 (2017), 396–405.
    • (2017) Food Chemistry , vol.218 , pp. 396-405
    • Neves, A.C.1    Harnedy, P.A.2    O'Keeffe, M.B.3    FitzGerald, R.J.4
  • 23
    • 84865324339 scopus 로고    scopus 로고
    • Tryptophan-containing milk protein-derived dipeptides inhibit xanthine oxidase
    • Nongonierma, A.B., FitzGerald, R.J., Tryptophan-containing milk protein-derived dipeptides inhibit xanthine oxidase. Peptides 37:2 (2012), 263–272.
    • (2012) Peptides , vol.37 , Issue.2 , pp. 263-272
    • Nongonierma, A.B.1    FitzGerald, R.J.2
  • 24
    • 84871549211 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV inhibitory and antioxidative properties of milk-derived dipeptides and hydrolysates
    • Nongonierma, A.B., FitzGerald, R.J., Dipeptidyl peptidase IV inhibitory and antioxidative properties of milk-derived dipeptides and hydrolysates. Peptides 39 (2013), 157–163.
    • (2013) Peptides , vol.39 , pp. 157-163
    • Nongonierma, A.B.1    FitzGerald, R.J.2
  • 25
    • 84888440672 scopus 로고    scopus 로고
    • Inhibition of dipeptidyl peptidase IV (DPP-IV) by proline containing peptides
    • Nongonierma, A.B., FitzGerald, R.J., Inhibition of dipeptidyl peptidase IV (DPP-IV) by proline containing peptides. Journal of Functional Foods 5:4 (2013), 1909–1917.
    • (2013) Journal of Functional Foods , vol.5 , Issue.4 , pp. 1909-1917
    • Nongonierma, A.B.1    FitzGerald, R.J.2
  • 26
    • 84888165809 scopus 로고    scopus 로고
    • Inhibition of dipeptidyl peptidase IV (DPP-IV) by tryptophan containing dipeptides
    • Nongonierma, A.B., FitzGerald, R.J., Inhibition of dipeptidyl peptidase IV (DPP-IV) by tryptophan containing dipeptides. Food & Function 4 (2013), 1843–1849.
    • (2013) Food & Function , vol.4 , pp. 1843-1849
    • Nongonierma, A.B.1    FitzGerald, R.J.2
  • 27
    • 84903131059 scopus 로고    scopus 로고
    • An in silico model to predict the potential of dietary proteins as sources of dipeptidyl peptidase IV (DPP-IV) inhibitory peptides
    • Nongonierma, A.B., FitzGerald, R.J., An in silico model to predict the potential of dietary proteins as sources of dipeptidyl peptidase IV (DPP-IV) inhibitory peptides. Food Chemistry 165 (2014), 489–498.
    • (2014) Food Chemistry , vol.165 , pp. 489-498
    • Nongonierma, A.B.1    FitzGerald, R.J.2
  • 28
    • 84884510206 scopus 로고    scopus 로고
    • Susceptibility of milk protein-derived peptides to dipeptidyl peptidase IV (DPP-IV) hydrolysis
    • Nongonierma, A.B., FitzGerald, R.J., Susceptibility of milk protein-derived peptides to dipeptidyl peptidase IV (DPP-IV) hydrolysis. Food Chemistry 145:15 (2014), 845–852.
    • (2014) Food Chemistry , vol.145 , Issue.15 , pp. 845-852
    • Nongonierma, A.B.1    FitzGerald, R.J.2
  • 29
    • 84940380637 scopus 로고    scopus 로고
    • Bioactive properties of milk proteins in humans: A review
    • Nongonierma, A.B., FitzGerald, R.J., Bioactive properties of milk proteins in humans: A review. Peptides 73 (2015), 20–34.
    • (2015) Peptides , vol.73 , pp. 20-34
    • Nongonierma, A.B.1    FitzGerald, R.J.2
  • 30
    • 84938833523 scopus 로고    scopus 로고
    • The scientific evidence for the role of milk protein-derived bioactive peptides in humans: A review
    • Nongonierma, A.B., FitzGerald, R.J., The scientific evidence for the role of milk protein-derived bioactive peptides in humans: A review. Journal of Functional Foods 640 (2015), 640–656.
    • (2015) Journal of Functional Foods , vol.640 , pp. 640-656
    • Nongonierma, A.B.1    FitzGerald, R.J.2
  • 31
    • 84928102730 scopus 로고    scopus 로고
    • Utilisation of the isobole methodology to study dietary peptide–drug and peptide–peptide interactive effects on dipeptidyl peptidase IV (DPP-IV) inhibition
    • Nongonierma, A.B., FitzGerald, R.J., Utilisation of the isobole methodology to study dietary peptide–drug and peptide–peptide interactive effects on dipeptidyl peptidase IV (DPP-IV) inhibition. Food & Function 6:1 (2015), 312–319.
    • (2015) Food & Function , vol.6 , Issue.1 , pp. 312-319
    • Nongonierma, A.B.1    FitzGerald, R.J.2
  • 32
    • 84982162235 scopus 로고    scopus 로고
    • Learnings from quantitative structure-activity relationship (QSAR) studies with respect to food protein-derived bioactive peptides: A review
    • Nongonierma, A.B., FitzGerald, R.J., Learnings from quantitative structure-activity relationship (QSAR) studies with respect to food protein-derived bioactive peptides: A review. RSC Advances 6:79 (2016), 75400–75413.
    • (2016) RSC Advances , vol.6 , Issue.79 , pp. 75400-75413
    • Nongonierma, A.B.1    FitzGerald, R.J.2
  • 33
    • 84957875650 scopus 로고    scopus 로고
    • Prospects for the management of type 2 diabetes using food protein-derived peptides with dipeptidyl peptidase IV (DPP-IV) inhibitory activity
    • Nongonierma, A.B., FitzGerald, R.J., Prospects for the management of type 2 diabetes using food protein-derived peptides with dipeptidyl peptidase IV (DPP-IV) inhibitory activity. Current Opinion in Food Science 8 (2016), 19–24.
    • (2016) Current Opinion in Food Science , vol.8 , pp. 19-24
    • Nongonierma, A.B.1    FitzGerald, R.J.2
  • 34
    • 84961782662 scopus 로고    scopus 로고
    • Structure activity relationship modelling of milk protein-derived peptides with dipeptidyl peptidase IV (DPP-IV) inhibitory activity
    • Nongonierma, A.B., FitzGerald, R.J., Structure activity relationship modelling of milk protein-derived peptides with dipeptidyl peptidase IV (DPP-IV) inhibitory activity. Peptides 79 (2016), 1–7.
    • (2016) Peptides , vol.79 , pp. 1-7
    • Nongonierma, A.B.1    FitzGerald, R.J.2
  • 35
    • 84884602268 scopus 로고    scopus 로고
    • Inhibition of dipeptidyl peptidase IV and xanthine oxidase by amino acids and dipeptides
    • Nongonierma, A.B., Mooney, C., Shields, D.C., FitzGerald, R.J., Inhibition of dipeptidyl peptidase IV and xanthine oxidase by amino acids and dipeptides. Food Chemistry 141 (2013), 644–653.
    • (2013) Food Chemistry , vol.141 , pp. 644-653
    • Nongonierma, A.B.1    Mooney, C.2    Shields, D.C.3    FitzGerald, R.J.4
  • 36
    • 84979020963 scopus 로고    scopus 로고
    • Response surface methodology (RSM) applied to the generation of casein hydrolysates with antioxidant and dipeptidyl peptidase IV (DPP-IV) inhibitory properties
    • (In Press)
    • Nongonierma, A.B., Le Maux, S., Esteveny, C., FitzGerald, R.J., Response surface methodology (RSM) applied to the generation of casein hydrolysates with antioxidant and dipeptidyl peptidase IV (DPP-IV) inhibitory properties. Journal of the Science of Food and Agriculture, 2016 (In Press) 10.1002/jsfa.7834.
    • (2016) Journal of the Science of Food and Agriculture
    • Nongonierma, A.B.1    Le Maux, S.2    Esteveny, C.3    FitzGerald, R.J.4
  • 37
    • 84894242430 scopus 로고    scopus 로고
    • Characterisation of the hydrolytic specificity of Aspergillus niger derived prolyl endoproteinase on bovine β-casein and determination of ACE inhibitory activity
    • Norris, R., Poyarkov, A., O'Keeffe, M.B., FitzGerald, R.J., Characterisation of the hydrolytic specificity of Aspergillus niger derived prolyl endoproteinase on bovine β-casein and determination of ACE inhibitory activity. Food Chemistry 156 (2014), 29–36.
    • (2014) Food Chemistry , vol.156 , pp. 29-36
    • Norris, R.1    Poyarkov, A.2    O'Keeffe, M.B.3    FitzGerald, R.J.4
  • 38
    • 84926168802 scopus 로고    scopus 로고
    • Identification of short peptide sequences in complex milk protein hydrolysates
    • O'Keeffe, M.B., FitzGerald, R.J., Identification of short peptide sequences in complex milk protein hydrolysates. Food Chemistry 184 (2015), 140–146.
    • (2015) Food Chemistry , vol.184 , pp. 140-146
    • O'Keeffe, M.B.1    FitzGerald, R.J.2
  • 39
    • 0032911654 scopus 로고    scopus 로고
    • Fractionation of whey protein hydrolysates using charged UF/NF membranes
    • Pouliot, Y., Wijers, M.C., Gauthier, S.F., Nadeau, L., Fractionation of whey protein hydrolysates using charged UF/NF membranes. Journal of Membrane Science 158:1–2 (1999), 105–114.
    • (1999) Journal of Membrane Science , vol.158 , Issue.1-2 , pp. 105-114
    • Pouliot, Y.1    Wijers, M.C.2    Gauthier, S.F.3    Nadeau, L.4
  • 40
    • 84878313919 scopus 로고    scopus 로고
    • Dipeptidyl peptidase-IV inhibitory peptides generated by tryptic hydrolysis of a whey protein concentrate rich in β-lactoglobulin
    • Silveira, S.T., Martínez-Maqueda, D., Recio, I., Hernández-Ledesma, B., Dipeptidyl peptidase-IV inhibitory peptides generated by tryptic hydrolysis of a whey protein concentrate rich in β-lactoglobulin. Food Chemistry 141:15 (2013), 1072–1077.
    • (2013) Food Chemistry , vol.141 , Issue.15 , pp. 1072-1077
    • Silveira, S.T.1    Martínez-Maqueda, D.2    Recio, I.3    Hernández-Ledesma, B.4
  • 41
    • 58749101498 scopus 로고    scopus 로고
    • Bitterness in Bacillus proteinase hydrolysates of whey proteins
    • Spellman, D., O'Cuinn, G., FitzGerald, R.J., Bitterness in Bacillus proteinase hydrolysates of whey proteins. Food Chemistry 114:2 (2009), 440–446.
    • (2009) Food Chemistry , vol.114 , Issue.2 , pp. 440-446
    • Spellman, D.1    O'Cuinn, G.2    FitzGerald, R.J.3
  • 42
    • 84937977214 scopus 로고    scopus 로고
    • Characterisation of the potential of β-lactoglobulin and α-lactalbumin as sources of bioactive peptides affecting incretin function: In silico and in vitro comparative studies
    • Tulipano, G., Faggi, L., Nardone, A., Cocchi, D., Caroli, A.M., Characterisation of the potential of β-lactoglobulin and α-lactalbumin as sources of bioactive peptides affecting incretin function: In silico and in vitro comparative studies. International Dairy Journal 48 (2015), 62–72.
    • (2015) International Dairy Journal , vol.48 , pp. 62-72
    • Tulipano, G.1    Faggi, L.2    Nardone, A.3    Cocchi, D.4    Caroli, A.M.5
  • 43
    • 80052897910 scopus 로고    scopus 로고
    • Novel dipeptidyl peptidase-4-inhibiting peptide derived from β-lactoglobulin
    • Uchida, M., Ohshiba, Y., Mogami, O., Novel dipeptidyl peptidase-4-inhibiting peptide derived from β-lactoglobulin. Journal of Pharmacological Sciences 117:1 (2011), 63–66.
    • (2011) Journal of Pharmacological Sciences , vol.117 , Issue.1 , pp. 63-66
    • Uchida, M.1    Ohshiba, Y.2    Mogami, O.3
  • 44
    • 82655173852 scopus 로고    scopus 로고
    • Isolation and identification of casein-derived dipeptidyl-peptidase 4 (DPP-4)-inhibitory peptide LPQNIPPL from gouda-type cheese and its effect on plasma glucose in rats
    • Uenishi, H., Kabuki, T., Seto, Y., Serizawa, A., Nakajima, H., Isolation and identification of casein-derived dipeptidyl-peptidase 4 (DPP-4)-inhibitory peptide LPQNIPPL from gouda-type cheese and its effect on plasma glucose in rats. International Dairy Journal 22:1 (2012), 24–30.
    • (2012) International Dairy Journal , vol.22 , Issue.1 , pp. 24-30
    • Uenishi, H.1    Kabuki, T.2    Seto, Y.3    Serizawa, A.4    Nakajima, H.5
  • 45
    • 0021230368 scopus 로고
    • Diprotins A and B, inhibitors of dipeptidyl aminopeptidase IV, produced by bacteria
    • Umezawa, H., Aoyagi, T., Ogawa, K., Naganawa, H., Hamada, M., Takeuchi, T., Diprotins A and B, inhibitors of dipeptidyl aminopeptidase IV, produced by bacteria. Journal of Antibiotics 37:4 (1984), 422–425.
    • (1984) Journal of Antibiotics , vol.37 , Issue.4 , pp. 422-425
    • Umezawa, H.1    Aoyagi, T.2    Ogawa, K.3    Naganawa, H.4    Hamada, M.5    Takeuchi, T.6
  • 46
    • 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, 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 12:10 (2002), 813–820.
    • (2002) International Dairy Journal , vol.12 , Issue.10 , pp. 813-820
    • van der Ven, C.1    Gruppen, H.2    de Bont, D.B.A.3    Voragen, A.G.J.4
  • 48
    • 84944189069 scopus 로고    scopus 로고
    • Isolation and identification of dipeptidyl peptidase IV-inhibitory peptides from trypsin/chymotrypsin-treated goat milk casein hydrolysates by 2D-TLC and LC–MS/MS
    • Zhang, Y., Chen, R., Ma, H., Chen, S., Isolation and identification of dipeptidyl peptidase IV-inhibitory peptides from trypsin/chymotrypsin-treated goat milk casein hydrolysates by 2D-TLC and LC–MS/MS. Journal of Agricultural and Food Chemistry 63:40 (2015), 8819–8828.
    • (2015) Journal of Agricultural and Food Chemistry , vol.63 , Issue.40 , pp. 8819-8828
    • Zhang, Y.1    Chen, R.2    Ma, H.3    Chen, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.