메뉴 건너뛰기




Volumn 63, Issue , 2014, Pages 170-181

Peptidomics for discovery, bioavailability and monitoring of dairy bioactive peptides

Author keywords

Bioactive peptide; Bioavailability; Dairy product; Mass spectrometry; Monitoring; Peptidomics

Indexed keywords

BIOCHEMISTRY; BIOINFORMATICS; DAIRY PRODUCTS; MASS SPECTROMETRY; MOLECULAR BIOLOGY; MONITORING;

EID: 84905049580     PISSN: 09639969     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodres.2014.01.069     Document Type: Review
Times cited : (134)

References (145)
  • 1
    • 78651414246 scopus 로고    scopus 로고
    • Identification of caseinophosphopeptides generated through in vitro gastro-intestinal digestion of Beaufort cheese
    • Adt I., Dupas C., Boutrou R., Oulahal N., Noel C., Mollé D., et al. Identification of caseinophosphopeptides generated through in vitro gastro-intestinal digestion of Beaufort cheese. International Dairy Journal 2011, 21:129-134.
    • (2011) International Dairy Journal , vol.21 , pp. 129-134
    • Adt, I.1    Dupas, C.2    Boutrou, R.3    Oulahal, N.4    Noel, C.5    Mollé, D.6
  • 2
    • 80555125163 scopus 로고    scopus 로고
    • Antibacterial peptides derived from caprine whey proteins, by digestion with human gastrointestinal juice
    • Almaas H., Eriksen E., Sekse C., Comi I., Flengsrud R., Holm H., et al. Antibacterial peptides derived from caprine whey proteins, by digestion with human gastrointestinal juice. British Journal of Nutrition 2011, 106:896-905.
    • (2011) British Journal of Nutrition , vol.106 , pp. 896-905
    • Almaas, H.1    Eriksen, E.2    Sekse, C.3    Comi, I.4    Flengsrud, R.5    Holm, H.6
  • 5
    • 33845961060 scopus 로고    scopus 로고
    • Identification of large phosphopeptides from β-casein that characteristically accumulate during ripening of the semi-hard cheese Herrgård
    • Ardö Y., Lilbæk H., Kristiansen K.R., Zakora M., Otte J. Identification of large phosphopeptides from β-casein that characteristically accumulate during ripening of the semi-hard cheese Herrgård. International Dairy Journal 2007, 17:513-524.
    • (2007) International Dairy Journal , vol.17 , pp. 513-524
    • Ardö, Y.1    Lilbæk, H.2    Kristiansen, K.R.3    Zakora, M.4    Otte, J.5
  • 6
    • 68149150248 scopus 로고    scopus 로고
    • Ussing chamber results for amino acid absorption of protein hydrolysates in porcine jejunum must be corrected for endogenous protein
    • Awati A., Rutherfurd S.M., Plugge W., Reynolds G.W., Marrant H., Kies A.K., et al. Ussing chamber results for amino acid absorption of protein hydrolysates in porcine jejunum must be corrected for endogenous protein. Journal of the Science of Food and Agriculture 2009, 89:1857-1861.
    • (2009) Journal of the Science of Food and Agriculture , vol.89 , pp. 1857-1861
    • Awati, A.1    Rutherfurd, S.M.2    Plugge, W.3    Reynolds, G.W.4    Marrant, H.5    Kies, A.K.6
  • 7
    • 84861857716 scopus 로고    scopus 로고
    • In vitro simulated gastrointestinal digestion of donkeys' milk. Peptide characterization by high performance liquid chromatography-tandem mass spectrometry
    • Bermeosolo-Bidasolo I., Ramos M., Gomez-Ruiz J.A. In vitro simulated gastrointestinal digestion of donkeys' milk. Peptide characterization by high performance liquid chromatography-tandem mass spectrometry. International Dairy Journal 2011, 24:146-152.
    • (2011) International Dairy Journal , vol.24 , pp. 146-152
    • Bermeosolo-Bidasolo, I.1    Ramos, M.2    Gomez-Ruiz, J.A.3
  • 11
    • 38949186542 scopus 로고    scopus 로고
    • Occurrence of the angiotensin-converting enzyme-inhibiting tripeptides Val-Pro-Pro and Ile-Pro-Pro in different cheese varieties of Swiss origin
    • Bütikofer U., Meyer J., Sieber R., Walther B., Wechsler D. Occurrence of the angiotensin-converting enzyme-inhibiting tripeptides Val-Pro-Pro and Ile-Pro-Pro in different cheese varieties of Swiss origin. Journal of Dairy Science 2008, 91:29-38.
    • (2008) Journal of Dairy Science , vol.91 , pp. 29-38
    • Bütikofer, U.1    Meyer, J.2    Sieber, R.3    Walther, B.4    Wechsler, D.5
  • 12
    • 34047274420 scopus 로고    scopus 로고
    • Quantification of the angiotensin-converting enzyme-inhibiting tripeptides Val-Pro-Pro and Ile-Pro-Pro in hard, semi-hard and soft cheeses
    • Bütikofer U., Meyer J., Sieber R., Wechsler D. Quantification of the angiotensin-converting enzyme-inhibiting tripeptides Val-Pro-Pro and Ile-Pro-Pro in hard, semi-hard and soft cheeses. International Dairy Journal 2007, 17:968-975.
    • (2007) International Dairy Journal , vol.17 , pp. 968-975
    • Bütikofer, U.1    Meyer, J.2    Sieber, R.3    Wechsler, D.4
  • 14
    • 78649334104 scopus 로고    scopus 로고
    • Identification of bioactive peptides in hypoallergenic infant milk formulas by capillary electrophoresis-mass spectrometry
    • Català-Clariana S., Benavente F., Giménez E., Barbosa J., Sanz-Nebot V. Identification of bioactive peptides in hypoallergenic infant milk formulas by capillary electrophoresis-mass spectrometry. Analytica Chimica Acta 2010, 683:119-125.
    • (2010) Analytica Chimica Acta , vol.683 , pp. 119-125
    • Català-Clariana, S.1    Benavente, F.2    Giménez, E.3    Barbosa, J.4    Sanz-Nebot, V.5
  • 15
    • 84879818065 scopus 로고    scopus 로고
    • Identification of bioactive peptides in hypoallergenic infant milk formulas by CE-TOF-MS assisted by semiempirical model of electromigration behavior
    • Català-Clariana S., Benavente F., Giménez E., Barbosa J., Sanz-Nebot V. Identification of bioactive peptides in hypoallergenic infant milk formulas by CE-TOF-MS assisted by semiempirical model of electromigration behavior. Electrophoresis 2013, 34:1886-1894.
    • (2013) Electrophoresis , vol.34 , pp. 1886-1894
    • Català-Clariana, S.1    Benavente, F.2    Giménez, E.3    Barbosa, J.4    Sanz-Nebot, V.5
  • 16
    • 0032006448 scopus 로고    scopus 로고
    • Casein peptide release and passage to the blood in humans during digestion of milk or yogurt
    • Chabance B., Marteau P., Rambaud J.C., Migliore-Samour D., Boynard M., Perrotin P., et al. Casein peptide release and passage to the blood in humans during digestion of milk or yogurt. Biochimie 1998, 80:155-165.
    • (1998) Biochimie , vol.80 , pp. 155-165
    • Chabance, B.1    Marteau, P.2    Rambaud, J.C.3    Migliore-Samour, D.4    Boynard, M.5    Perrotin, P.6
  • 17
    • 34047215914 scopus 로고    scopus 로고
    • Production of lactoferricin and other cationic peptides from food grade bovine lactoferrin with various iron saturation levels
    • Chan J.C.K., Li-Chan E.C.Y. Production of lactoferricin and other cationic peptides from food grade bovine lactoferrin with various iron saturation levels. Journal of Agricultural and Food Chemistry 2007, 55:493-501.
    • (2007) Journal of Agricultural and Food Chemistry , vol.55 , pp. 493-501
    • Chan, J.C.K.1    Li-Chan, E.C.Y.2
  • 18
    • 20844439071 scopus 로고    scopus 로고
    • Angiotensin I-converting-enzyme (ACE)-inhibitory activity of tryptic peptides of ovine β-lactoglobulin and of milk yoghurts obtained by using different starters
    • Chobert J.-, El-Zahar K., Sitohy M., Dalgalarrondo M., Métro F., Choiset Y., et al. Angiotensin I-converting-enzyme (ACE)-inhibitory activity of tryptic peptides of ovine β-lactoglobulin and of milk yoghurts obtained by using different starters. Le Lait 2005, 85:141-152.
    • (2005) Le Lait , vol.85 , pp. 141-152
    • Chobert J.-1    El-Zahar, K.2    Sitohy, M.3    Dalgalarrondo, M.4    Métro, F.5    Choiset, Y.6
  • 21
    • 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 2011, 44:9-15.
    • (2011) LWT-Food Science and Technology , vol.44 , pp. 9-15
    • Contreras, M.D.M.1    Hernández-Ledesma, B.2    Amigo, L.3    Martín-Álvarez, P.J.4    Recio, I.5
  • 23
    • 84871745882 scopus 로고    scopus 로고
    • Absorption of casein antihypertensive peptides through an in vitro model of intestinal epithelium
    • Contreras M.D.M., Sancho A., Recio I., Mills C. Absorption of casein antihypertensive peptides through an in vitro model of intestinal epithelium. Food Digestion 2012, 3:16-24.
    • (2012) Food Digestion , vol.3 , pp. 16-24
    • Contreras, M.D.M.1    Sancho, A.2    Recio, I.3    Mills, C.4
  • 24
    • 79955549808 scopus 로고    scopus 로고
    • Food-grade production of an antihypertensive casein hydrolysate and resistance of active peptides to drying and storage
    • Contreras M., Sevilla M., Monroy-Ruiz J., Amigo L., Gómez-Sala B., Molina E., et al. Food-grade production of an antihypertensive casein hydrolysate and resistance of active peptides to drying and storage. International Dairy Journal 2011, 21:470-476.
    • (2011) International Dairy Journal , vol.21 , pp. 470-476
    • Contreras, M.1    Sevilla, M.2    Monroy-Ruiz, J.3    Amigo, L.4    Gómez-Sala, B.5    Molina, E.6
  • 26
    • 84877136049 scopus 로고    scopus 로고
    • Extensive in vivo human milk peptidomics reveals specific proteolysis yielding protective antimicrobial peptides
    • Dallas D.C., Guerrero A., Khaldi N., Castillo P.A., Martin W.F., Smilowitz J.T., et al. Extensive in vivo human milk peptidomics reveals specific proteolysis yielding protective antimicrobial peptides. Journal of Proteome Research 2013, 12:2295-2304.
    • (2013) Journal of Proteome Research , vol.12 , pp. 2295-2304
    • Dallas, D.C.1    Guerrero, A.2    Khaldi, N.3    Castillo, P.A.4    Martin, W.F.5    Smilowitz, J.T.6
  • 27
    • 70350573378 scopus 로고    scopus 로고
    • Occurrence of β-casomorphins 5 and 7 in commercial dairy products and their digests following in vitro simulated gastro-intestinal digestion
    • De Noni I., Cattaneo S. Occurrence of β-casomorphins 5 and 7 in commercial dairy products and their digests following in vitro simulated gastro-intestinal digestion. Food Chemistry 2010, 119:560-566.
    • (2010) Food Chemistry , vol.119 , pp. 560-566
    • De Noni, I.1    Cattaneo, S.2
  • 28
  • 29
    • 33747501826 scopus 로고    scopus 로고
    • Preparation of angiotensin-I-converting enzyme inhibitory hydrolysates from unsupplemented caprine whey fermentation by various cheese microflora
    • Didelot S., Bordenave-Juchereau S., Rosenfeld E., Fruitier-Arnaudin I., Piot J.-, Sannier F. Preparation of angiotensin-I-converting enzyme inhibitory hydrolysates from unsupplemented caprine whey fermentation by various cheese microflora. International Dairy Journal 2006, 16:976-983.
    • (2006) International Dairy Journal , vol.16 , pp. 976-983
    • Didelot, S.1    Bordenave-Juchereau, S.2    Rosenfeld, E.3    Fruitier-Arnaudin, I.4    Piot J.-5    Sannier, F.6
  • 33
    • 1642301670 scopus 로고    scopus 로고
    • Casein proteolysis in human milk: Tracing the pattern of casein breakdown and the formation of potential bioactive peptides
    • Ferranti P., Traisci M.V., Picariello G., Nasi A., Boschi V., Siervo M., et al. Casein proteolysis in human milk: Tracing the pattern of casein breakdown and the formation of potential bioactive peptides. Journal of Dairy Research 2004, 71:74-87.
    • (2004) Journal of Dairy Research , vol.71 , pp. 74-87
    • Ferranti, P.1    Traisci, M.V.2    Picariello, G.3    Nasi, A.4    Boschi, V.5    Siervo, M.6
  • 34
    • 47649099423 scopus 로고    scopus 로고
    • The angiotensin converting enzyme inhibitory tripeptides Ile-Pro-Pro and Val-Pro-Pro show increasing permeabilities with increasing physiological relevance of absorption models
    • Foltz M., Cerstiaens A., van Meensel A., Mols R., van der Pijl P.C., Duchateau G.S.M.J.E., et al. The angiotensin converting enzyme inhibitory tripeptides Ile-Pro-Pro and Val-Pro-Pro show increasing permeabilities with increasing physiological relevance of absorption models. Peptides 2008, 29:1312-1320.
    • (2008) Peptides , vol.29 , pp. 1312-1320
    • Foltz, M.1    Cerstiaens, A.2    van Meensel, A.3    Mols, R.4    van der Pijl, P.C.5    Duchateau, G.S.M.J.E.6
  • 35
    • 34247153806 scopus 로고    scopus 로고
    • Angiotensin converting enzyme inhibitory peptides from a lactotripeptide-enriched milk beverage are absorbed intact into the circulation
    • Foltz M., Meynen E.E., Bianco V., van Platerink C., Koning T.M.M.G., Kloek J. Angiotensin converting enzyme inhibitory peptides from a lactotripeptide-enriched milk beverage are absorbed intact into the circulation. Journal of Nutrition 2007, 137:953-958.
    • (2007) Journal of Nutrition , vol.137 , pp. 953-958
    • Foltz, M.1    Meynen, E.E.2    Bianco, V.3    van Platerink, C.4    Koning, T.M.M.G.5    Kloek, J.6
  • 36
    • 69749111280 scopus 로고    scopus 로고
    • Modeling of the relationship between dipeptide structure and dipeptide stability, permeability, and ACE inhibitory activity
    • Foltz M., van Buren L., Klaffke W., Duchateau G.S.M.J.E. Modeling of the relationship between dipeptide structure and dipeptide stability, permeability, and ACE inhibitory activity. Journal of Food Science 2009, 74:243-251.
    • (2009) Journal of Food Science , vol.74 , pp. 243-251
    • Foltz, M.1    van Buren, L.2    Klaffke, W.3    Duchateau, G.S.M.J.E.4
  • 38
    • 61449163906 scopus 로고    scopus 로고
    • Invited review: Proteomics of milk and bacteria used in fermented dairy products: From qualitative to quantitative advances
    • Gagnaire V., Jardin J., Jan G., Lortal S. Invited review: Proteomics of milk and bacteria used in fermented dairy products: From qualitative to quantitative advances. Journal of Dairy Science 2009, 92:811-825.
    • (2009) Journal of Dairy Science , vol.92 , pp. 811-825
    • Gagnaire, V.1    Jardin, J.2    Jan, G.3    Lortal, S.4
  • 39
    • 77649231781 scopus 로고    scopus 로고
    • Milk versus caseinophosphopeptides added to fruit beverage: Resistance and release from simulated gastrointestinal digestion
    • García-Nebot M.J., Alegría A., Barberá R., Contreras M.M., Recio I. Milk versus caseinophosphopeptides added to fruit beverage: Resistance and release from simulated gastrointestinal digestion. Peptides 2010, 31:555-561.
    • (2010) Peptides , vol.31 , pp. 555-561
    • García-Nebot, M.J.1    Alegría, A.2    Barberá, R.3    Contreras, M.M.4    Recio, I.5
  • 40
    • 4544317465 scopus 로고    scopus 로고
    • Angiotensin converting enzyme-inhibitory activity of peptides isolated from Manchego cheese. Stability under simulated gastrointestinal digestion
    • Gómez-Ruiz J.Á., Ramos M., Recio I. Angiotensin converting enzyme-inhibitory activity of peptides isolated from Manchego cheese. Stability under simulated gastrointestinal digestion. International Dairy Journal 2004, 14:1075-1080.
    • (2004) International Dairy Journal , vol.14 , pp. 1075-1080
    • Gómez-Ruiz, J.Á.1    Ramos, M.2    Recio, I.3
  • 41
    • 7444220586 scopus 로고    scopus 로고
    • Identification and formation of angiotensin-converting enzyme-inhibitory peptides in Manchego cheese by high-performance liquid chromatography-tandem mass spectrometry
    • Gómez-Ruiz J.A., Ramos M., Recio I. Identification and formation of angiotensin-converting enzyme-inhibitory peptides in Manchego cheese by high-performance liquid chromatography-tandem mass spectrometry. Journal of Chromatography. A 2004, 1054:269-277.
    • (2004) Journal of Chromatography. A , vol.1054 , pp. 269-277
    • Gómez-Ruiz, J.A.1    Ramos, M.2    Recio, I.3
  • 42
    • 36549086043 scopus 로고    scopus 로고
    • Identification of novel angiotensin-converting enzyme-inhibitory peptides from ovine milk proteins by CE-MS and chromatographic techniques
    • Gómez-Ruiz J.Á., Ramos M., Recio I. Identification of novel angiotensin-converting enzyme-inhibitory peptides from ovine milk proteins by CE-MS and chromatographic techniques. Electrophoresis 2007, 28:4202-4211.
    • (2007) Electrophoresis , vol.28 , pp. 4202-4211
    • Gómez-Ruiz, J.Á.1    Ramos, M.2    Recio, I.3
  • 43
    • 4744361004 scopus 로고    scopus 로고
    • ACE-inhibitory activity and structural properties of peptide Asp-Lys-Ile-His-Pro [β-CN f(47-51)]. Study of the peptide forms synthesized by different methods
    • Gómez-Ruiz J.A., Recio I., Belloque J. ACE-inhibitory activity and structural properties of peptide Asp-Lys-Ile-His-Pro [β-CN f(47-51)]. Study of the peptide forms synthesized by different methods. Journal of Agricultural and Food Chemistry 2004, 52:6315-6319.
    • (2004) Journal of Agricultural and Food Chemistry , vol.52 , pp. 6315-6319
    • Gómez-Ruiz, J.A.1    Recio, I.2    Belloque, J.3
  • 45
    • 80051558901 scopus 로고    scopus 로고
    • QSAR-aided in silico approach in evaluation of food proteins as precursors of ACE inhibitory peptides
    • Gu Y., Majumder K., Wu J. QSAR-aided in silico approach in evaluation of food proteins as precursors of ACE inhibitory peptides. Food Research International 2011, 44:2465-2474.
    • (2011) Food Research International , vol.44 , pp. 2465-2474
    • Gu, Y.1    Majumder, K.2    Wu, J.3
  • 46
    • 34147123803 scopus 로고    scopus 로고
    • Food-derived peptides with biological activity: From research to food applications
    • Hartmann R., Meisel H. Food-derived peptides with biological activity: From research to food applications. Current Opinion in Biotechnology 2007, 18:163-169.
    • (2007) Current Opinion in Biotechnology , vol.18 , pp. 163-169
    • Hartmann, R.1    Meisel, H.2
  • 49
    • 34547150556 scopus 로고    scopus 로고
    • Casein fermentate of Lactobacillus animalis DPC6134 contains a range of novel propeptide angiotensin-converting enzyme inhibitors
    • Hayes M., Stanton C., Slattery H., O'Sullivan O., Hill C., Fitzgerald G.F., et al. Casein fermentate of Lactobacillus animalis DPC6134 contains a range of novel propeptide angiotensin-converting enzyme inhibitors. Applied and Environmental Microbiology 2007, 73:4658-4667.
    • (2007) Applied and Environmental Microbiology , vol.73 , pp. 4658-4667
    • Hayes, M.1    Stanton, C.2    Slattery, H.3    O'Sullivan, O.4    Hill, C.5    Fitzgerald, G.F.6
  • 51
    • 13244277961 scopus 로고    scopus 로고
    • Preparation of antioxidant enzymatic hydrolysates from α-lactalbumin and β-lactoglobulin. Identification of active peptides by HPLC-MS/MS
    • Hernández-Ledesma B., Dávalos A., Bartolomé B., Amigo L. Preparation of antioxidant enzymatic hydrolysates from α-lactalbumin and β-lactoglobulin. Identification of active peptides by HPLC-MS/MS. Journal of Agricultural and Food Chemistry 2005, 53:588-593.
    • (2005) Journal of Agricultural and Food Chemistry , vol.53 , pp. 588-593
    • Hernández-Ledesma, B.1    Dávalos, A.2    Bartolomé, B.3    Amigo, L.4
  • 54
    • 33846015834 scopus 로고    scopus 로고
    • Identification of bioactive peptides after digestion of human milk and infant formula with pepsin and pancreatin
    • Hernández-Ledesma B., Quiros A., Amigo L., Recio I. Identification of bioactive peptides after digestion of human milk and infant formula with pepsin and pancreatin. International Dairy Journal 2007, 17:42-49.
    • (2007) International Dairy Journal , vol.17 , pp. 42-49
    • Hernández-Ledesma, B.1    Quiros, A.2    Amigo, L.3    Recio, I.4
  • 55
    • 44649132121 scopus 로고    scopus 로고
    • Capillary electrophoresis-electrospray-mass spectrometry in peptide analysis and peptidomics
    • Herrero M., Ibañez E., Cifuentes A. Capillary electrophoresis-electrospray-mass spectrometry in peptide analysis and peptidomics. Electrophoresis 2008, 29:2148-2160.
    • (2008) Electrophoresis , vol.29 , pp. 2148-2160
    • Herrero, M.1    Ibañez, E.2    Cifuentes, A.3
  • 56
    • 0033973754 scopus 로고    scopus 로고
    • Caco-2 versus Caco-2/HT29-MTX co-cultured cell lines: Permeabilities via diffusion, inside- and outside-directed carrier-mediated transport
    • Hilgendorf C., Spahn-Langguth H., Regårdh Carl G., Lipka Elke, Amidon G.L., Langguth P. Caco-2 versus Caco-2/HT29-MTX co-cultured cell lines: Permeabilities via diffusion, inside- and outside-directed carrier-mediated transport. Journal of Pharmaceutical Sciences 2000, 89:63-75.
    • (2000) Journal of Pharmaceutical Sciences , vol.89 , pp. 63-75
    • Hilgendorf, C.1    Spahn-Langguth, H.2    Regårdh, C.G.3    Lipka, E.4    Amidon, G.L.5    Langguth, P.6
  • 60
    • 59649101292 scopus 로고    scopus 로고
    • Separation, detection and quantitation of peptides by liquid chromatography and capillary electrochromatography
    • Issaq H.J., Chan K.C., Blonder J., Ye X., Veenstra T.D. Separation, detection and quantitation of peptides by liquid chromatography and capillary electrochromatography. Journal of Chromatography. A 2009, 1216:1825-1837.
    • (2009) Journal of Chromatography. A , vol.1216 , pp. 1825-1837
    • Issaq, H.J.1    Chan, K.C.2    Blonder, J.3    Ye, X.4    Veenstra, T.D.5
  • 61
    • 43049162813 scopus 로고    scopus 로고
    • Transport of micro-opioid receptor agonists and antagonist peptides across Caco-2 monolayer
    • Iwan M.G., JarmoÅ'owska B., Bielikowicz K., Kostyra E., Kostyra H., Kaczmarski M. Transport of micro-opioid receptor agonists and antagonist peptides across Caco-2 monolayer. Peptides 2008, 29:1042-1047.
    • (2008) Peptides , vol.29 , pp. 1042-1047
    • Iwan, M.G.1    Jarmoa'owska, B.2    Bielikowicz, K.3    Kostyra, E.4    Kostyra, H.5    Kaczmarski, M.6
  • 62
    • 84860249243 scopus 로고    scopus 로고
    • The influence of storage on contents of selected antagonist and agonist opioid peptides in fermented milk drinks
    • Jarmołowska B., Krawczuk S. The influence of storage on contents of selected antagonist and agonist opioid peptides in fermented milk drinks. Milchwissenschaft 2012, 67:130-133.
    • (2012) Milchwissenschaft , vol.67 , pp. 130-133
    • Jarmołowska, B.1    Krawczuk, S.2
  • 63
    • 33846953603 scopus 로고    scopus 로고
    • Yak milk casein as a functional ingredient: Preparation and identification of angiotensin-I-converting enzyme inhibitory peptides
    • Jiang J., Chen S., Ren F., Luo Z., Zeng S.S. Yak milk casein as a functional ingredient: Preparation and identification of angiotensin-I-converting enzyme inhibitory peptides. Journal of Dairy Research 2007, 74:18-25.
    • (2007) Journal of Dairy Research , vol.74 , pp. 18-25
    • Jiang, J.1    Chen, S.2    Ren, F.3    Luo, Z.4    Zeng, S.S.5
  • 64
    • 70349232247 scopus 로고    scopus 로고
    • Nanoelectrospray with ion-trap mass spectrometry for the determination of beta-casomorphins in derived milk products
    • Juan-García A., Font G., Juan C., Picó Y. Nanoelectrospray with ion-trap mass spectrometry for the determination of beta-casomorphins in derived milk products. Talanta 2009, 80:294-306.
    • (2009) Talanta , vol.80 , pp. 294-306
    • Juan-García, A.1    Font, G.2    Juan, C.3    Picó, Y.4
  • 66
    • 84555178067 scopus 로고    scopus 로고
    • Recent developments in CE and CEC of peptides (2009-2011)
    • Kašička V. Recent developments in CE and CEC of peptides (2009-2011). Electrophoresis 2012, 33:48-73.
    • (2012) Electrophoresis , vol.33 , pp. 48-73
    • Kašička, V.1
  • 68
    • 84857142045 scopus 로고    scopus 로고
    • Identification of bioactive peptides in a functional yogurt by micro liquid chromatography time-of-flight mass spectrometry assisted by retention time prediction
    • Kunda P.B., Benavente F., Catalá-Clariana S., Giménez E., Barbosa J., Sanz-Nebot V. Identification of bioactive peptides in a functional yogurt by micro liquid chromatography time-of-flight mass spectrometry assisted by retention time prediction. Journal of Chromatography. A 2012, 1229:121-128.
    • (2012) Journal of Chromatography. A , vol.1229 , pp. 121-128
    • Kunda, P.B.1    Benavente, F.2    Catalá-Clariana, S.3    Giménez, E.4    Barbosa, J.5    Sanz-Nebot, V.6
  • 69
    • 77957360551 scopus 로고    scopus 로고
    • Proteomics in nutrition: Status quo and outlook for biomarkers and bioactives
    • Kussmann M., Panchaud A., Affolter M. Proteomics in nutrition: Status quo and outlook for biomarkers and bioactives. Journal of Proteome Research 2010, 9:4876-4887.
    • (2010) Journal of Proteome Research , vol.9 , pp. 4876-4887
    • Kussmann, M.1    Panchaud, A.2    Affolter, M.3
  • 70
    • 84859950630 scopus 로고    scopus 로고
    • Nanostructure-assisted laser desorption/ionization (NALDI) for analysis of peptides in milk and colostrum
    • Kütt M.-, Malbe M., Stagsted J. Nanostructure-assisted laser desorption/ionization (NALDI) for analysis of peptides in milk and colostrum. Agronomy Research 2011, 9:415-420.
    • (2011) Agronomy Research , vol.9 , pp. 415-420
    • Kütt M.-1    Malbe, M.2    Stagsted, J.3
  • 71
    • 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 2012, 4:403-422.
    • (2012) Journal of Functional Foods , vol.4 , pp. 403-422
    • Lacroix, I.M.E.1    Li-Chan, E.C.Y.2
  • 73
    • 84878379489 scopus 로고    scopus 로고
    • Quantification of lactosylation of whey proteins in stored milk powder using multiple reaction monitoring
    • Le T.T., Deeth H.C., Bhandari B., Alewood P.F., Holland J.W. Quantification of lactosylation of whey proteins in stored milk powder using multiple reaction monitoring. Food Chemistry 2013, 141:1203-1210.
    • (2013) Food Chemistry , vol.141 , pp. 1203-1210
    • Le, T.T.1    Deeth, H.C.2    Bhandari, B.3    Alewood, P.F.4    Holland, J.W.5
  • 74
    • 77949293684 scopus 로고    scopus 로고
    • Phosphopeptide enrichment using metal oxide affinity chromatography
    • Leitner A. Phosphopeptide enrichment using metal oxide affinity chromatography. Trends in Analytical Chemistry 2010, 29:177-185.
    • (2010) Trends in Analytical Chemistry , vol.29 , pp. 177-185
    • Leitner, A.1
  • 75
    • 84870322164 scopus 로고    scopus 로고
    • Characterization of structure-antioxidant activity relationship of peptides in free radical systems using QSAR models: Key sequence positions and their amino acid properties
    • Li Y.-, Li B. Characterization of structure-antioxidant activity relationship of peptides in free radical systems using QSAR models: Key sequence positions and their amino acid properties. Journal of Theoretical Biology 2013, 318:29-43.
    • (2013) Journal of Theoretical Biology , vol.318 , pp. 29-43
    • Li Y.-1    Li, B.2
  • 76
    • 79955913588 scopus 로고    scopus 로고
    • Structure-activity relationship study of antioxidative peptides by QSAR modeling: The amino acid next to C-terminus affects the activity
    • Li Y.-, Li B., He J., Qian P. Structure-activity relationship study of antioxidative peptides by QSAR modeling: The amino acid next to C-terminus affects the activity. Journal of Peptide Science 2011, 17:454-462.
    • (2011) Journal of Peptide Science , vol.17 , pp. 454-462
    • Li Y.-1    Li, B.2    He, J.3    Qian, P.4
  • 77
    • 33847374660 scopus 로고    scopus 로고
    • Rapid enrichment of phosphopeptides from tryptic digests of proteins using iron oxide nanocomposites of magnetic particles coated with zirconia as the concentrating probes
    • Lo C.-, Chen W.-, Chen C.-, Chen Y.- Rapid enrichment of phosphopeptides from tryptic digests of proteins using iron oxide nanocomposites of magnetic particles coated with zirconia as the concentrating probes. Journal of Proteome Research 2007, 6:887-893.
    • (2007) Journal of Proteome Research , vol.6 , pp. 887-893
    • Lo C.-1    Chen W.-2    Chen C.-3    Chen Y.-4
  • 78
    • 84872044172 scopus 로고    scopus 로고
    • A mini-review on health and nutritional aspects of cheese with a focus on bioactive peptides
    • López-Expósito I., Amigo L., Recio I. A mini-review on health and nutritional aspects of cheese with a focus on bioactive peptides. Dairy Science and Technology 2012, 92:419-438.
    • (2012) Dairy Science and Technology , vol.92 , pp. 419-438
    • López-Expósito, I.1    Amigo, L.2    Recio, I.3
  • 81
    • 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. International Dairy Journal 2006, 16:1277-1293.
    • (2006) International Dairy Journal , vol.16 , pp. 1277-1293
    • López-Fandiño, R.1    Otte, J.2    van Camp, J.3
  • 82
    • 32044438646 scopus 로고    scopus 로고
    • Identification of peptides in antimicrobial fractions of cheese extracts by electrospray ionization ion trap mass spectrometry coupled to a two-dimensional liquid chromatographic separation
    • Losito I., Carbonara T., De Bari M.D., Gobbetti M., Palmisano F., Rizzello C.G., et al. Identification of peptides in antimicrobial fractions of cheese extracts by electrospray ionization ion trap mass spectrometry coupled to a two-dimensional liquid chromatographic separation. Rapid Communications in Mass Spectrometry 2006, 20:447-455.
    • (2006) Rapid Communications in Mass Spectrometry , vol.20 , pp. 447-455
    • Losito, I.1    Carbonara, T.2    De Bari, M.D.3    Gobbetti, M.4    Palmisano, F.5    Rizzello, C.G.6
  • 83
    • 0030202780 scopus 로고    scopus 로고
    • Identification of an antihypertensive peptide from casein hydrolysates produced by a proteinase from Lactobacillus helveticus CP790
    • Maeno M., Yamamoto N., Takano T. Identification of an antihypertensive peptide from casein hydrolysates produced by a proteinase from Lactobacillus helveticus CP790. Journal of Dairy Science 1996, 79:1316-1321.
    • (1996) Journal of Dairy Science , vol.79 , pp. 1316-1321
    • Maeno, M.1    Yamamoto, N.2    Takano, T.3
  • 84
    • 0024522775 scopus 로고
    • Absorption of intact morphiceptin by diisopropylfluorophosphate-treated rabbit ileum
    • Mahé S., Tomé D., Dumontier A.M., Desjeux J.F. Absorption of intact morphiceptin by diisopropylfluorophosphate-treated rabbit ileum. Peptides 1989, 10:45-52.
    • (1989) Peptides , vol.10 , pp. 45-52
    • Mahé, S.1    Tomé, D.2    Dumontier, A.M.3    Desjeux, J.F.4
  • 88
    • 84886262835 scopus 로고    scopus 로고
    • Effect of β-lactoglobulin hydrolysate and β-lactorphin on intestinal mucin secretion and gene expression in human goblet cells
    • Martínez-Maqueda D., Miralles B., Ramos M., Recio I. Effect of β-lactoglobulin hydrolysate and β-lactorphin on intestinal mucin secretion and gene expression in human goblet cells. Food Research International 2013, 54:1287-1291.
    • (2013) Food Research International , vol.54 , pp. 1287-1291
    • Martínez-Maqueda, D.1    Miralles, B.2    Ramos, M.3    Recio, I.4
  • 90
    • 11844268066 scopus 로고    scopus 로고
    • Isolation and characterisation of antibacterial peptides derived from the f(164-207) region of bovine α s2-casein
    • McCann K.B., Shiell B.J., Michalski W.P., Lee A., Wan J., Roginski H., et al. Isolation and characterisation of antibacterial peptides derived from the f(164-207) region of bovine α s2-casein. International Dairy Journal 2005, 15:133-143.
    • (2005) International Dairy Journal , vol.15 , pp. 133-143
    • McCann, K.B.1    Shiell, B.J.2    Michalski, W.P.3    Lee, A.4    Wan, J.5    Roginski, H.6
  • 92
    • 0033165880 scopus 로고    scopus 로고
    • Mucus as a barrier to the permeability of hydrophilic and lipophilic compounds in the absence and presence of sodium taurocholate micellar systems using cell culture models
    • Meaney C., O'Driscoll C. Mucus as a barrier to the permeability of hydrophilic and lipophilic compounds in the absence and presence of sodium taurocholate micellar systems using cell culture models. European Journal of Pharmaceutical Sciences 1999, 8:167-175.
    • (1999) European Journal of Pharmaceutical Sciences , vol.8 , pp. 167-175
    • Meaney, C.1    O'Driscoll, C.2
  • 93
    • 0032076817 scopus 로고    scopus 로고
    • Overview on milk protein-derived peptides
    • Meisel H. Overview on milk protein-derived peptides. International Dairy Journal 1998, 8:363-373.
    • (1998) International Dairy Journal , vol.8 , pp. 363-373
    • Meisel, H.1
  • 94
    • 61449192388 scopus 로고    scopus 로고
    • Hot topic: Changes in angiotensin-converting enzyme inhibition and concentrations of the tripeptides Val-Pro-Pro and Ile-Pro-Pro during ripening of different Swiss cheese varieties
    • Meyer J., Bütikofer U., Walther B., Wechsler D., Sieber R. Hot topic: Changes in angiotensin-converting enzyme inhibition and concentrations of the tripeptides Val-Pro-Pro and Ile-Pro-Pro during ripening of different Swiss cheese varieties. Journal of Dairy Science 2009, 92:826-836.
    • (2009) Journal of Dairy Science , vol.92 , pp. 826-836
    • Meyer, J.1    Bütikofer, U.2    Walther, B.3    Wechsler, D.4    Sieber, R.5
  • 95
    • 0141816841 scopus 로고    scopus 로고
    • Angiotensin I-converting-enzyme-inhibitory and antibacterial peptides from Lactobacillus helveticus PR4 proteinase-hydrolyzed caseins of milk from six species
    • Minervini F., Algaron F., Rizzello C.G., Fox P.F., Monnet V., Gobbetti M. Angiotensin I-converting-enzyme-inhibitory and antibacterial peptides from Lactobacillus helveticus PR4 proteinase-hydrolyzed caseins of milk from six species. Applied and Environmental Microbiology 2003, 69:5297-5305.
    • (2003) Applied and Environmental Microbiology , vol.69 , pp. 5297-5305
    • Minervini, F.1    Algaron, F.2    Rizzello, C.G.3    Fox, P.F.4    Monnet, V.5    Gobbetti, M.6
  • 100
    • 47649096199 scopus 로고    scopus 로고
    • Release and identification of angiotensin-converting enzyme-inhibitory peptides as influenced by ripening temperatures and probiotic adjuncts in Cheddar cheeses
    • Ong L., Shah N.P. Release and identification of angiotensin-converting enzyme-inhibitory peptides as influenced by ripening temperatures and probiotic adjuncts in Cheddar cheeses. Food Science and Technology 2008, 41:1555-1566.
    • (2008) Food Science and Technology , vol.41 , pp. 1555-1566
    • Ong, L.1    Shah, N.P.2
  • 101
    • 33846024711 scopus 로고    scopus 로고
    • Angiotensin-converting enzyme inhibitory activity of milk protein hydrolysates: Effect of substrate, enzyme and time of hydrolysis
    • Otte J., Shalaby S.M., Zakora M., Pripp A.H., El-Shabrawy S.A. Angiotensin-converting enzyme inhibitory activity of milk protein hydrolysates: Effect of substrate, enzyme and time of hydrolysis. International Dairy Journal 2007, 17:488-503.
    • (2007) International Dairy Journal , vol.17 , pp. 488-503
    • Otte, J.1    Shalaby, S.M.2    Zakora, M.3    Pripp, A.H.4    El-Shabrawy, S.A.5
  • 102
    • 77950864272 scopus 로고    scopus 로고
    • Optimization of sour milk fermentation for the production of ACE-inhibitory peptides and purification of a novel peptide from whey protein hydrolysate
    • Pan D., Guo Y. Optimization of sour milk fermentation for the production of ACE-inhibitory peptides and purification of a novel peptide from whey protein hydrolysate. International Dairy Journal 2010, 20:472-479.
    • (2010) International Dairy Journal , vol.20 , pp. 472-479
    • Pan, D.1    Guo, Y.2
  • 103
    • 84862189137 scopus 로고    scopus 로고
    • Mass spectrometry for nutritional peptidomics: How to analyze food bioactives and their health effects
    • Panchaud A., Affolter M., Kussmann M. Mass spectrometry for nutritional peptidomics: How to analyze food bioactives and their health effects. Journal of Proteomics 2012, 75:3546-3559.
    • (2012) Journal of Proteomics , vol.75 , pp. 3546-3559
    • Panchaud, A.1    Affolter, M.2    Kussmann, M.3
  • 104
    • 68849084346 scopus 로고    scopus 로고
    • Degradation of milk-based bioactive peptides by yogurt fermentation bacteria
    • Paul M., Somkuti G.A. Degradation of milk-based bioactive peptides by yogurt fermentation bacteria. Letters in Applied Microbiology 2009, 49:345-350.
    • (2009) Letters in Applied Microbiology , vol.49 , pp. 345-350
    • Paul, M.1    Somkuti, G.A.2
  • 105
    • 74049126072 scopus 로고    scopus 로고
    • Peptides surviving the simulated gastrointestinal digestion of milk proteins: Biological and toxicological implications
    • Picariello G., Ferranti P., Fierro O., Mamone G., Caira S., Di Luccia A., et al. Peptides surviving the simulated gastrointestinal digestion of milk proteins: Biological and toxicological implications. Journal of Chromatography. B 2010, 878:295-308.
    • (2010) Journal of Chromatography. B , vol.878 , pp. 295-308
    • Picariello, G.1    Ferranti, P.2    Fierro, O.3    Mamone, G.4    Caira, S.5    Di Luccia, A.6
  • 106
    • 84875951488 scopus 로고    scopus 로고
    • Transport across Caco-2 monolayers of peptides arising from in vitro digestion of bovine milk proteins
    • Picariello G., Iacomino G., Mamone G., Ferranti P., Fierro O., Gianfrani C., et al. Transport across Caco-2 monolayers of peptides arising from in vitro digestion of bovine milk proteins. Food Chemistry 2013, 139:203-212.
    • (2013) Food Chemistry , vol.139 , pp. 203-212
    • Picariello, G.1    Iacomino, G.2    Mamone, G.3    Ferranti, P.4    Fierro, O.5    Gianfrani, C.6
  • 107
    • 84867450906 scopus 로고    scopus 로고
    • Novel mass spectrometry-based applications of the 'omic': Sciences in food technology and biotechnology
    • Picariello G., Mamone G., Addeo F., Ferranti P. Novel mass spectrometry-based applications of the 'omic': Sciences in food technology and biotechnology. Food Technology and Biotechnology 2012, 50:286-305.
    • (2012) Food Technology and Biotechnology , vol.50 , pp. 286-305
    • Picariello, G.1    Mamone, G.2    Addeo, F.3    Ferranti, P.4
  • 108
    • 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. International Dairy Journal 2010, 20:3-10.
    • (2010) International Dairy Journal , vol.20 , pp. 3-10
    • Pihlanto, A.1    Virtanen, T.2    Korhonen, H.3
  • 109
    • 84870470724 scopus 로고    scopus 로고
    • A novel bioactive peptide from yoghurts modulates expression of the gel-forming MUC2 mucin as well as population of goblet cells and Paneth cells along the small intestine
    • Plaisancié P., Claustre J., Estienne M., Henry G., Boutrou R., Paquet A., et al. A novel bioactive peptide from yoghurts modulates expression of the gel-forming MUC2 mucin as well as population of goblet cells and Paneth cells along the small intestine. Journal of Nutritional Biochemistry 2013, 24:213-221.
    • (2013) Journal of Nutritional Biochemistry , vol.24 , pp. 213-221
    • Plaisancié, P.1    Claustre, J.2    Estienne, M.3    Henry, G.4    Boutrou, R.5    Paquet, A.6
  • 110
    • 59249085496 scopus 로고    scopus 로고
    • Sample pretreatment techniques for oligopeptide analysis from natural sources
    • Poliwoda A., Wieczorek P.P. Sample pretreatment techniques for oligopeptide analysis from natural sources. Analytical and Bioanalytical Chemistry 2009, 393:885-897.
    • (2009) Analytical and Bioanalytical Chemistry , vol.393 , pp. 885-897
    • Poliwoda, A.1    Wieczorek, P.P.2
  • 111
    • 70349333712 scopus 로고    scopus 로고
    • Stability to gastrointestinal enzymes and structure-activity relationship of β-casein-peptides with antihypertensive properties
    • Quirós A., Contreras M.M., Ramos M., Amigo L., Recio I. Stability to gastrointestinal enzymes and structure-activity relationship of β-casein-peptides with antihypertensive properties. Peptides 2009, 30:1848-1853.
    • (2009) Peptides , vol.30 , pp. 1848-1853
    • Quirós, A.1    Contreras, M.M.2    Ramos, M.3    Amigo, L.4    Recio, I.5
  • 113
  • 115
    • 84872679078 scopus 로고    scopus 로고
    • Angiotensin I-converting enzyme-inhibitory activity of the Norwegian authocthonus cheeses Gamalost and Norvegia after in vitro human gastrointestinal digestion
    • Qureshi T.M., Vegarud G.E., Abrahamsen R.K., Skeie S. Angiotensin I-converting enzyme-inhibitory activity of the Norwegian authocthonus cheeses Gamalost and Norvegia after in vitro human gastrointestinal digestion. Journal of Dairy Science 2013, 96:838-853.
    • (2013) Journal of Dairy Science , vol.96 , pp. 838-853
    • Qureshi, T.M.1    Vegarud, G.E.2    Abrahamsen, R.K.3    Skeie, S.4
  • 119
    • 8444246337 scopus 로고    scopus 로고
    • Identification of angiotensin-I-converting enzyme inhibitory peptides derived from sodium caseinate hydrolysates produced by Lactobacillus helveticus NCC 2765
    • Robert M.-, Razaname A., Mutter M., Juillerat M.A. Identification of angiotensin-I-converting enzyme inhibitory peptides derived from sodium caseinate hydrolysates produced by Lactobacillus helveticus NCC 2765. Journal of Agricultural and Food Chemistry 2004, 52:6923-6931.
    • (2004) Journal of Agricultural and Food Chemistry , vol.52 , pp. 6923-6931
    • Robert M.-1    Razaname, A.2    Mutter, M.3    Juillerat, M.A.4
  • 120
    • 0033007311 scopus 로고    scopus 로고
    • Effect of chain length on absorption of biologically active peptides from the gastrointestinal tract
    • Roberts P.R., Burney J.D., Black K.W., Zaloga G.P. 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
  • 121
    • 80054040698 scopus 로고    scopus 로고
    • Antihypertensive effect of a bovine lactoferrin pepsin hydrolysate: Identification of novel active peptides
    • Ruiz-Giménez P., Salom J.B., Marcos J.F., Vallés S., Martínez-Maqueda D., Recio I., et al. Antihypertensive effect of a bovine lactoferrin pepsin hydrolysate: Identification of novel active peptides. Food Chemistry 2012, 131:266-273.
    • (2012) Food Chemistry , vol.131 , pp. 266-273
    • Ruiz-Giménez, P.1    Salom, J.B.2    Marcos, J.F.3    Vallés, S.4    Martínez-Maqueda, D.5    Recio, I.6
  • 122
    • 84868123294 scopus 로고    scopus 로고
    • Food proteins as a source of bioactive peptides with diverse functions
    • Rutherfurd-Markwick K.J. Food proteins as a source of bioactive peptides with diverse functions. British Journal of Nutrition 2012, 108:149-157.
    • (2012) British Journal of Nutrition , vol.108 , pp. 149-157
    • Rutherfurd-Markwick, K.J.1
  • 123
    • 84886307863 scopus 로고    scopus 로고
    • An overview of "omic" analytical methods applied in bioactive peptide studies
    • Saavedra L., Hebert E.M., Minahk C., Ferranti P. An overview of "omic" analytical methods applied in bioactive peptide studies. Food Research International 2013, 54:925-934.
    • (2013) Food Research International , vol.54 , pp. 925-934
    • Saavedra, L.1    Hebert, E.M.2    Minahk, C.3    Ferranti, P.4
  • 124
    • 84882838844 scopus 로고    scopus 로고
    • Quantitative structure-activity relationship based screening of bioactive peptides identified in ripened cheese
    • Sagardia I., Iloro I., Elortza F., Bald C. Quantitative structure-activity relationship based screening of bioactive peptides identified in ripened cheese. International Dairy Journal 2013, 33:184-190.
    • (2013) International Dairy Journal , vol.33 , pp. 184-190
    • Sagardia, I.1    Iloro, I.2    Elortza, F.3    Bald, C.4
  • 125
    • 84867894628 scopus 로고    scopus 로고
    • A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides
    • Sagardia I., Roa-Ureta R.H., Bald C. A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides. Food Chemistry 2013, 136:1370-1376.
    • (2013) Food Chemistry , vol.136 , pp. 1370-1376
    • Sagardia, I.1    Roa-Ureta, R.H.2    Bald, C.3
  • 126
    • 84901928728 scopus 로고    scopus 로고
    • Peptidomic study of Spanish blue cheese (Valdeón) and changes after simulated gastrointestinal digestión
    • (in press)
    • Sánchez-Rivera L., Diezhandino I., Gómez-Ruiz J.A., Fresno J.M., Miralles B., Recio I. Peptidomic study of Spanish blue cheese (Valdeón) and changes after simulated gastrointestinal digestión. Electrophoresis 2014, (in press). 10.1002/elps.201300510.
    • (2014) Electrophoresis
    • Sánchez-Rivera, L.1    Diezhandino, I.2    Gómez-Ruiz, J.A.3    Fresno, J.M.4    Miralles, B.5    Recio, I.6
  • 127
    • 84878122215 scopus 로고    scopus 로고
    • Short communication: Peptide profiling in cheeses packed using different technologies
    • Sánchez-Rivera L., Recio I., Ramos M., Gómez-Ruiz J.Á. Short communication: Peptide profiling in cheeses packed using different technologies. Journal of Dairy Science 2013, 96:3551-3557.
    • (2013) Journal of Dairy Science , vol.96 , pp. 3551-3557
    • Sánchez-Rivera, L.1    Recio, I.2    Ramos, M.3    Gómez-Ruiz, J.Á.4
  • 129
    • 84862567709 scopus 로고    scopus 로고
    • Cheese peptidomics: A detailed study on the evolution of the oligopeptide fraction in Parmigiano-Reggiano cheese from curd to 24months of aging
    • Sforza S., Cavatorta V., Lambertini F., Galaverna G., Dossena A., Marchelli R. Cheese peptidomics: A detailed study on the evolution of the oligopeptide fraction in Parmigiano-Reggiano cheese from curd to 24months of aging. Journal of Dairy Science 2012, 95:3514-3526.
    • (2012) Journal of Dairy Science , vol.95 , pp. 3514-3526
    • Sforza, S.1    Cavatorta, V.2    Lambertini, F.3    Galaverna, G.4    Dossena, A.5    Marchelli, R.6
  • 130
    • 0030759649 scopus 로고    scopus 로고
    • Transepithelial transport of oligopeptides in the human intestinal cell, Caco-2
    • Shimizu M., Tsunogai M., Arai S. Transepithelial transport of oligopeptides in the human intestinal cell, Caco-2. Peptides 1997, 18:681-687.
    • (1997) Peptides , vol.18 , pp. 681-687
    • Shimizu, M.1    Tsunogai, M.2    Arai, S.3
  • 131
    • 84874050250 scopus 로고    scopus 로고
    • Predicting the activity of antimicrobial peptides with amino acid topological information
    • Shu M., Yu R., Zhang Y., Wang J., Yang L., Wang L., et al. Predicting the activity of antimicrobial peptides with amino acid topological information. Medicinal Chemistry 2013, 9:32-44.
    • (2013) Medicinal Chemistry , vol.9 , pp. 32-44
    • Shu, M.1    Yu, R.2    Zhang, Y.3    Wang, J.4    Yang, L.5    Wang, L.6
  • 133
    • 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 2013, 141:1072-1077.
    • (2013) Food Chemistry , vol.141 , pp. 1072-1077
    • Silveira, S.T.1    Martínez-Maqueda, D.2    Recio, I.3    Hernández-Ledesma, B.4
  • 134
    • 77952892222 scopus 로고    scopus 로고
    • Enzymatic fragmentation of the antimicrobial peptides casocidin and isracidin by Streptococcus thermophilus and Lactobacillus delbrueckii ssp. bulgaricus
    • Somkuti G., Paul M. Enzymatic fragmentation of the antimicrobial peptides casocidin and isracidin by Streptococcus thermophilus and Lactobacillus delbrueckii ssp. bulgaricus. Applied Microbiology and Biotechnology 2010, 87:235-242.
    • (2010) Applied Microbiology and Biotechnology , vol.87 , pp. 235-242
    • Somkuti, G.1    Paul, M.2
  • 135
    • 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 M.D.M., Amorim M., Pintado M., Recio I., Malcata F.X. 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
  • 136
    • 84872017263 scopus 로고    scopus 로고
    • QSAR models for ACE-inhibitor activity of tri-peptides based on representation of the molecular structure by graph of atomic orbitals and SMILES
    • Toropova A.P., Toropov A.A., Rasulev B.F., Benfenati E., Gini G., Leszczynska D., et al. QSAR models for ACE-inhibitor activity of tri-peptides based on representation of the molecular structure by graph of atomic orbitals and SMILES. Structural Chemistry 2012, 23:1873-1878.
    • (2012) Structural Chemistry , vol.23 , pp. 1873-1878
    • Toropova, A.P.1    Toropov, A.A.2    Rasulev, B.F.3    Benfenati, E.4    Gini, G.5    Leszczynska, D.6
  • 139
    • 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 2012, 22:24-30.
    • (2012) International Dairy Journal , vol.22 , pp. 24-30
    • Uenishi, H.1    Kabuki, T.2    Seto, Y.3    Serizawa, A.4    Nakajima, H.5
  • 141
    • 33846463451 scopus 로고    scopus 로고
    • Development of an at-line method for the identification of angiotensin-I inhibiting peptides in protein hydrolysates
    • van Platerink C.J., Janssen H.-M., Haverkamp J. Development of an at-line method for the identification of angiotensin-I inhibiting peptides in protein hydrolysates. Journal of Chromatography. B 2007, 846:147-154.
    • (2007) Journal of Chromatography. B , vol.846 , pp. 147-154
    • van Platerink, C.J.1    Janssen, H.-M.2    Haverkamp, J.3
  • 142
    • 29244477860 scopus 로고    scopus 로고
    • Quantification of ACE inhibiting peptides in human plasma using high performance liquid chromatography-mass spectrometry
    • van Platerink C., Janssen H.-G.M., Horsten R., Haverkamp J. Quantification of ACE inhibiting peptides in human plasma using high performance liquid chromatography-mass spectrometry. Journal of Chromatography. B 2006, 830:151-157.
    • (2006) Journal of Chromatography. B , vol.830 , pp. 151-157
    • van Platerink, C.1    Janssen, H.-G.M.2    Horsten, R.3    Haverkamp, J.4
  • 143
    • 34447621600 scopus 로고    scopus 로고
    • Highly efficient and selective enrichment of phosphopeptides using porous anodic alumina membrane for MALDI-TOF MS analysis
    • Wang Y., Chen W., Wu J., Guo Y., Xia X. Highly efficient and selective enrichment of phosphopeptides using porous anodic alumina membrane for MALDI-TOF MS analysis. Journal of the American Society for Mass Spectrometry 2007, 18:1387-1395.
    • (2007) Journal of the American Society for Mass Spectrometry , vol.18 , pp. 1387-1395
    • Wang, Y.1    Chen, W.2    Wu, J.3    Guo, Y.4    Xia, X.5
  • 144
    • 69149106437 scopus 로고    scopus 로고
    • In vitro digestion methods for assessing the effect of food structure on allergen breakdown
    • Wickham M., Faulks R., Mills C. In vitro digestion methods for assessing the effect of food structure on allergen breakdown. Molecular Nutrition & Food Research 2009, 53:952-958.
    • (2009) Molecular Nutrition & Food Research , vol.53 , pp. 952-958
    • Wickham, M.1    Faulks, R.2    Mills, C.3
  • 145
    • 77954621834 scopus 로고    scopus 로고
    • Direct nanoHPLC-ESI-QTOF MS/MS analysis of tryptic caseinophosphopeptides
    • Zhu Y.-, FitzGerald R.J. Direct nanoHPLC-ESI-QTOF MS/MS analysis of tryptic caseinophosphopeptides. Food Chemistry 2010, 123:753-759.
    • (2010) Food Chemistry , vol.123 , pp. 753-759
    • Zhu Y.-1    FitzGerald, R.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.