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Volumn 199, Issue , 2016, Pages 246-251

Enzymatic generation of whey protein hydrolysates under pH-controlled and non pH-controlled conditions: Impact on physicochemical and bioactive properties

Author keywords

DPP IV inhibition; ORAC; Peptide profile; pH stat; Whey proteins

Indexed keywords

HYDROLYSIS; MASS SPECTROMETRY; PAPAIN; PEPTIDES; PH; PROTEINS;

EID: 84949571305     PISSN: 03088146     EISSN: 18737072     Source Type: Journal    
DOI: 10.1016/j.foodchem.2015.12.021     Document Type: Article
Times cited : (80)

References (28)
  • 1
    • 0018536145 scopus 로고
    • Determination of the degree of hydrolysis of food protein hydrolysates by trinitrobenzenesulfonic acid
    • J. Adler-Nissen 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
    • 78649318542 scopus 로고    scopus 로고
    • Hydrolysis of β-lactoglobulin by trypsin under acidic pH and analysis of the hydrolysates with MALDI-TOF-MS/MS
    • S.C. Cheison, M.-Y. Lai, E. Leeb, and U. Kulozik Hydrolysis of β-lactoglobulin by trypsin under acidic pH and analysis of the hydrolysates with MALDI-TOF-MS/MS Food Chemistry 125 2011 1241 1248
    • (2011) Food Chemistry , vol.125 , pp. 1241-1248
    • Cheison, S.C.1    Lai, M.-Y.2    Leeb, E.3    Kulozik, U.4
  • 3
    • 78651438046 scopus 로고    scopus 로고
    • Influence of hydrolysis temperature and pH on the selective hydrolysis of whey proteins by trypsin and potential recovery of native alpha-lactalbumin
    • S.C. Cheison, E. Leeb, J. Toro-Sierra, and U. Kulozik Influence of hydrolysis temperature and pH on the selective hydrolysis of whey proteins by trypsin and potential recovery of native alpha-lactalbumin International Dairy Journal 21 2011 166 171
    • (2011) International Dairy Journal , vol.21 , pp. 166-171
    • Cheison, S.C.1    Leeb, E.2    Toro-Sierra, J.3    Kulozik, U.4
  • 4
    • 84896888595 scopus 로고    scopus 로고
    • Antioxidant activity of bovine casein hydrolysates produced by Ficus carica L.-derived proteinase
    • G. Di Pierro, M.B. O'Keeffe, A. Poyarkov, G. Lomolino, and R.J. FitzGerald Antioxidant activity of bovine casein hydrolysates produced by Ficus carica L.-derived proteinase Food Chemistry 156 2014 305 311
    • (2014) Food Chemistry , vol.156 , pp. 305-311
    • Di Pierro, G.1    O'Keeffe, M.B.2    Poyarkov, A.3    Lomolino, G.4    FitzGerald, R.J.5
  • 7
    • 84897390441 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV and its inhibitors: Therapeutics for type 2 diabetes and what else?
    • L. Juillerat-Jeanneret Dipeptidyl peptidase IV and its inhibitors: Therapeutics for type 2 diabetes and what else? Journal of Medicinal Chemistry 57 2014 2197 2212
    • (2014) Journal of Medicinal Chemistry , vol.57 , pp. 2197-2212
    • Juillerat-Jeanneret, L.1
  • 8
    • 33747503962 scopus 로고    scopus 로고
    • Bioactive peptides: Production and functionality
    • H. Korhonen, and A. Pihlanto Bioactive peptides: Production and functionality International Dairy Journal 16 2006 945 960
    • (2006) International Dairy Journal , vol.16 , pp. 945-960
    • Korhonen, H.1    Pihlanto, A.2
  • 9
    • 84893330854 scopus 로고    scopus 로고
    • Isolation and characterization of peptides with dipeptidyl peptidase-IV Inhibitory activity from pepsin-treated bovine whey proteins
    • I.M.E. Lacroix, and E.C.Y. Li-Chan 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
  • 10
    • 84949088240 scopus 로고    scopus 로고
    • Identification of short peptide sequences in the nanofiltration permeate of a bioactive whey protein hydrolysate
    • S. Le Maux, A.B. Nongonierma, B.A. Murray, P.M. Kelly, and R.J. FitzGerald 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.A.3    Kelly, P.M.4    FitzGerald, R.J.5
  • 11
    • 84961290278 scopus 로고    scopus 로고
    • Bioactive peptides and protein hydrolysates: Research trends and challenges for application as nutraceuticals and functional food ingredients
    • E.C. Li-Chan Bioactive peptides and protein hydrolysates: Research trends and challenges for application as nutraceuticals and functional food ingredients Current Opinion in Food Science 1 2015 28 37
    • (2015) Current Opinion in Food Science , vol.1 , pp. 28-37
    • Li-Chan, E.C.1
  • 12
    • 84865324339 scopus 로고    scopus 로고
    • Tryptophan-containing milk protein-derived dipeptides inhibit xanthine oxidase
    • A.B. Nongonierma, and R.J. FitzGerald Tryptophan-containing milk protein-derived dipeptides inhibit xanthine oxidase Peptides 37 2012 263 272
    • (2012) Peptides , vol.37 , pp. 263-272
    • Nongonierma, A.B.1    FitzGerald, R.J.2
  • 13
    • 84871549211 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV inhibitory and antioxidative properties of milk-derived dipeptides and hydrolysates
    • A.B. Nongonierma, and R.J. FitzGerald 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
  • 14
    • 84877836950 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV inhibitory properties of a whey protein hydrolysate: Influence of fractionation, stability to simulated gastrointestinal digestion and food-drug interaction
    • A.B. Nongonierma, and R.J. FitzGerald Dipeptidyl peptidase IV inhibitory properties of a whey protein hydrolysate: Influence of fractionation, stability to simulated gastrointestinal digestion and food-drug interaction International Dairy Journal 32 2013 33 39
    • (2013) International Dairy Journal , vol.32 , pp. 33-39
    • Nongonierma, A.B.1    FitzGerald, R.J.2
  • 15
    • 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
    • A.B. Nongonierma, and R.J. FitzGerald 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
  • 16
    • 84938833523 scopus 로고    scopus 로고
    • The scientific evidence for the role of milk protein-derived bioactive peptides in humans: A review
    • A.B. Nongonierma, and R.J. FitzGerald 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
  • 18
    • 84942574100 scopus 로고    scopus 로고
    • Quinoa (Chenopodium quinoa Willd.) protein hydrolysates with in vitro dipeptidyl peptidase IV (DPP-IV) inhibitory and antioxidant properties
    • A.B. Nongonierma, S. Le Maux, C. Dubrulle, C. Barre, and R.J. FitzGerald Quinoa (Chenopodium quinoa Willd.) protein hydrolysates with in vitro dipeptidyl peptidase IV (DPP-IV) inhibitory and antioxidant properties Journal of Cereal Science 65 2015 112 118
    • (2015) Journal of Cereal Science , vol.65 , pp. 112-118
    • Nongonierma, A.B.1    Le Maux, S.2    Dubrulle, C.3    Barre, C.4    FitzGerald, R.J.5
  • 19
    • 33748319573 scopus 로고    scopus 로고
    • Antioxidative peptides derived from milk proteins
    • A. Pihlanto Antioxidative peptides derived from milk proteins International Dairy Journal 16 2006 1306 1314
    • (2006) International Dairy Journal , vol.16 , pp. 1306-1314
    • Pihlanto, A.1
  • 21
    • 84878368347 scopus 로고    scopus 로고
    • Antioxidative peptides: Enzymatic production, in vitro and in vivo antioxidant activity and potential applications of milk-derived antioxidative peptides
    • O. Power, P. Jakeman, and R.J. FitzGerald Antioxidative peptides: enzymatic production, in vitro and in vivo antioxidant activity and potential applications of milk-derived antioxidative peptides Amino Acids 44 2013 797 820
    • (2013) Amino Acids , vol.44 , pp. 797-820
    • Power, O.1    Jakeman, P.2    FitzGerald, R.J.3
  • 22
    • 84896480172 scopus 로고    scopus 로고
    • Study on total antioxidant status in relation to oxidative stress in type 2 diabetes mellitus
    • A.J. Rani, and S. Mythili Study on total antioxidant status in relation to oxidative stress in type 2 diabetes mellitus Journal of Clinical and Diagnostic Research 8 2014 108 110
    • (2014) Journal of Clinical and Diagnostic Research , vol.8 , pp. 108-110
    • Rani, A.J.1    Mythili, S.2
  • 23
    • 0038029531 scopus 로고    scopus 로고
    • Proteinase and exopeptidase hydrolysis of whey protein: Comparison of the TNBS, OPA and pH stat methods for quantification of degree of hydrolysis
    • D. Spellman, E. McEvoy, G. O'Cuinn, and R.J. FitzGerald Proteinase and exopeptidase hydrolysis of whey protein: Comparison of the TNBS, OPA and pH stat methods for quantification of degree of hydrolysis International Dairy Journal 13 2003 447 453
    • (2003) International Dairy Journal , vol.13 , pp. 447-453
    • Spellman, D.1    McEvoy, E.2    O'Cuinn, G.3    FitzGerald, R.J.4
  • 24
    • 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
    • G. Tulipano, L. Faggi, A. Nardone, D. Cocchi, and A.M. Caroli 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 66 72
    • (2015) International Dairy Journal , vol.48 , pp. 66-72
    • Tulipano, G.1    Faggi, L.2    Nardone, A.3    Cocchi, D.4    Caroli, A.M.5
  • 25
    • 0036397541 scopus 로고    scopus 로고
    • Optimisation of the angiotensin converting enzyme inhibition by whey protein hydrolysates using response surface methodology
    • C. van der Ven, H. Gruppen, D.B.A. de Bont, and A.G.J. Voragen 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
    • Van Der Ven, C.1    Gruppen, H.2    De Bont, D.B.A.3    Voragen, A.G.J.4
  • 26
    • 33749342431 scopus 로고    scopus 로고
    • Enzymatic hydrolysis of protein: Mechanism and kinetic model
    • Q. Wei, and H. Zhimin Enzymatic hydrolysis of protein: Mechanism and kinetic model Frontiers of Chemistry in China 1 2006 308 314
    • (2006) Frontiers of Chemistry in China , vol.1 , pp. 308-314
    • Wei, Q.1    Zhimin, H.2
  • 28
    • 58149503993 scopus 로고    scopus 로고
    • ORAC and TEAC assays comparison to measure the antioxidant capacity of food products
    • A. Zulueta, M.J. Esteve, and A. Frígola ORAC and TEAC assays comparison to measure the antioxidant capacity of food products Food Chemistry 114 2009 310 316
    • (2009) Food Chemistry , vol.114 , pp. 310-316
    • Zulueta, A.1    Esteve, M.J.2    Frígola, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.