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Volumn 58, Issue 9, 2018, Pages 1468-1477

Bioactive whey peptide particles: An emerging class of nutraceutical carriers

Author keywords

ACE inhibitory; nanofibril; nanoparticle; nanotube; whey protein isolate

Indexed keywords

BIOACTIVITY; DRUG DELIVERY; ENCAPSULATION; GELATION; NANOPARTICLES; NANOTUBES; SUPRAMOLECULAR CHEMISTRY; YARN;

EID: 85020440949     PISSN: 10408398     EISSN: 15497852     Source Type: Journal    
DOI: 10.1080/10408398.2016.1264064     Document Type: Article
Times cited : (34)

References (89)
  • 1
    • 84942040082 scopus 로고    scopus 로고
    • Niosome-loaded cold-set whey protein hydrogels
    • Abaee, A., and Madadlou, A., (2016). Niosome-loaded cold-set whey protein hydrogels. Food Chem. 196:106–113.
    • (2016) Food Chem. , vol.196 , pp. 106-113
    • Abaee, A.1    Madadlou, A.2
  • 2
    • 84884782467 scopus 로고    scopus 로고
    • Whey protein peptides as components of nanoemulsions: A review of emulsifying and biological functionalities
    • Adjonu, R., Doran, G., Torley, P., and Agboola, S., (2014). Whey protein peptides as components of nanoemulsions: A review of emulsifying and biological functionalities. J. Food Eng. 122:15–27.
    • (2014) J. Food Eng. , vol.122 , pp. 15-27
    • Adjonu, R.1    Doran, G.2    Torley, P.3    Agboola, S.4
  • 3
    • 84867895162 scopus 로고    scopus 로고
    • Screening of whey protein isolate hydrolysates for their dual functionality: Influence of heat pre-treatment and enzyme specificity
    • Adjonu, R., Doran, G., Torley, P., and Agboola, S., (2013). Screening of whey protein isolate hydrolysates for their dual functionality: Influence of heat pre-treatment and enzyme specificity. Food Chem. 136:1435–1443.
    • (2013) Food Chem. , vol.136 , pp. 1435-1443
    • Adjonu, R.1    Doran, G.2    Torley, P.3    Agboola, S.4
  • 4
    • 44449138916 scopus 로고    scopus 로고
    • Akkermans, C., Venema, P., van der Goot, A. J., Gruppen, H., Bakx, E. J., Boom, R. M., and van der Linden, E. (2008). Peptides are building blocks of heat-induced fibrillar protein aggregates of β-lactoglobulin formed at pH 2., Biomacromolecules, :1474–1479
    • Akkermans, C., Venema, P., van der Goot, A. J., Gruppen, H., Bakx, E. J., Boom, R. M., and van der Linden, E. (2008). Peptides are building blocks of heat-induced fibrillar protein aggregates of β-lactoglobulin formed at pH 2. Biomacromolecules 9:1474–1479.
  • 5
    • 84895069902 scopus 로고    scopus 로고
    • Potentially bioactive and caffeine-loaded peptidic sub-micron and nanoscalar particles
    • Bagheri, L., Madadlou, A., Yarmand, M., and Mousavi, M. E., (2014a). Potentially bioactive and caffeine-loaded peptidic sub-micron and nanoscalar particles. J. Funct. Foods. 6:462–469.
    • (2014) J. Funct. Foods. , vol.6 , pp. 462-469
    • Bagheri, L.1    Madadlou, A.2    Yarmand, M.3    Mousavi, M.E.4
  • 6
    • 84902578961 scopus 로고    scopus 로고
    • Spray-dried alginate microparticles carrying caffeine-loaded and potentially bioactive nanoparticles
    • Bagheri, L., Madadlou, A., Yarmand, M., and Mousavi, M. E., (2014b). Spray-dried alginate microparticles carrying caffeine-loaded and potentially bioactive nanoparticles. Food Res. Int. 62:1113–1119.
    • (2014) Food Res. Int. , vol.62 , pp. 1113-1119
    • Bagheri, L.1    Madadlou, A.2    Yarmand, M.3    Mousavi, M.E.4
  • 7
    • 84905050245 scopus 로고    scopus 로고
    • Tracking the in vivo release of bioactive peptides in the gut during digestion: Mass spectrometry peptidomic characterization of effluents collected in the gut of dairy matrices fed mini-pigs
    • Barbé, F., Le Feunteun, S., Rémond, D., Ménard, O., Jardin, J., Henry, G., Laroche, B., and Dupont, D., (2014). Tracking the in vivo release of bioactive peptides in the gut during digestion: Mass spectrometry peptidomic characterization of effluents collected in the gut of dairy matrices fed mini-pigs. Food Res. Int. 63:147–156.
    • (2014) Food Res. Int. , vol.63 , pp. 147-156
    • Barbé, F.1    Le Feunteun, S.2    Rémond, D.3    Ménard, O.4    Jardin, J.5    Henry, G.6    Laroche, B.7    Dupont, D.8
  • 9
    • 0033091317 scopus 로고    scopus 로고
    • Proposing sequences for peptides derived from whey fermentation with potential bioactive sites
    • Belem, M. A. F., Gibbs, B. F., and Lee, B. H., (1999). Proposing sequences for peptides derived from whey fermentation with potential bioactive sites. J. Dairy Sci. 82:486–493.
    • (1999) J. Dairy Sci. , vol.82 , pp. 486-493
    • Belem, M.A.F.1    Gibbs, B.F.2    Lee, B.H.3
  • 10
    • 84960800820 scopus 로고    scopus 로고
    • Encapsulation and controlled release of bioactive compounds in lactoferrin-glycomacropeptide nanohydrogels: Curcumin and caffeine as model compounds
    • Bourbon, A. I., Cerqueira, M. A., and Vicente, A. A., (2016). Encapsulation and controlled release of bioactive compounds in lactoferrin-glycomacropeptide nanohydrogels: Curcumin and caffeine as model compounds. J. Food Eng. 180:110–119.
    • (2016) J. Food Eng. , vol.180 , pp. 110-119
    • Bourbon, A.I.1    Cerqueira, M.A.2    Vicente, A.A.3
  • 11
    • 84938834357 scopus 로고    scopus 로고
    • On the trail of milk bioactive peptides in human and animal intestinal tracts during digestion: A review
    • Boutrou, R., Henry, G., and Sanchez-Rivera, L., (2015). On the trail of milk bioactive peptides in human and animal intestinal tracts during digestion: A review. Dairy Sci. Technol. 95:815–829.
    • (2015) Dairy Sci. Technol. , vol.95 , pp. 815-829
    • Boutrou, R.1    Henry, G.2    Sanchez-Rivera, L.3
  • 12
    • 84930182842 scopus 로고    scopus 로고
    • Whey as a source of peptides with remarkable biological activities
    • Brandelli, A., Dariot, D. J., and Corrêa, A. P. F., (2015). Whey as a source of peptides with remarkable biological activities. Food Res. Int. 73:149–161.
    • (2015) Food Res. Int. , vol.73 , pp. 149-161
    • Brandelli, A.1    Dariot, D.J.2    Corrêa, A.P.F.3
  • 13
    • 0037122727 scopus 로고    scopus 로고
    • Designing peptide-based scaffolds as drug delivery vehicles
    • Brokx, R. D., Bisland, S. K., and Gariépy, J., (2002). Designing peptide-based scaffolds as drug delivery vehicles. J. Control. Release. 17:115–123.
    • (2002) J. Control. Release. , vol.17 , pp. 115-123
    • Brokx, R.D.1    Bisland, S.K.2    Gariépy, J.3
  • 15
    • 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-M., El-Zahar, K., Sitohy, M., Dalgalarrondo, M., Métro, F., Choiset, Y., and Haertlé, T., (2005). Angiotensin I-converting-enzyme (ACE)-inhibitory activity of tryptic peptides of ovine β-lactoglobulin and of milk yoghurts obtained by using different starters. Lait 85:141–152.
    • (2005) Lait , vol.85 , pp. 141-152
    • Chobert, J.-M.1    El-Zahar, K.2    Sitohy, M.3    Dalgalarrondo, M.4    Métro, F.5    Choiset, Y.6    Haertlé, T.7
  • 16
    • 0034199281 scopus 로고    scopus 로고
    • Bioactive milk peptides: A prospectus
    • Clare, D. A., and Swaisgood, H. E., (2000). Bioactive milk peptides: A prospectus. J. Dairy Sci. 83:1187–1195.
    • (2000) J. Dairy Sci. , vol.83 , pp. 1187-1195
    • Clare, D.A.1    Swaisgood, H.E.2
  • 17
    • 84857117570 scopus 로고    scopus 로고
    • Milk clotting activity and production of bioactive peptides from whey using Maclura pomifera proteases
    • Corrons, M. A., Bertucci, J. I., Liggieri, C. S., López, L. M. I., and Bruno, M. A., (2012). Milk clotting activity and production of bioactive peptides from whey using Maclura pomifera proteases. LWT-Food Sci. Technol. 47:103–109.
    • (2012) LWT-Food Sci. Technol. , vol.47 , pp. 103-109
    • Corrons, M.A.1    Bertucci, J.I.2    Liggieri, C.S.3    López, L.M.I.4    Bruno, M.A.5
  • 19
    • 84908519080 scopus 로고    scopus 로고
    • Self-assembly of b-lactoglobulin and egg white lysozyme as a potential carrier for nutraceuticals
    • Diarrassouba, F., Remondetto, G., Garrait, G., Alvarez, P., Beyssac, E., and Subirade, M., (2015). Self-assembly of b-lactoglobulin and egg white lysozyme as a potential carrier for nutraceuticals. Food Chem. 173:203–209.
    • (2015) Food Chem. , vol.173 , pp. 203-209
    • Diarrassouba, F.1    Remondetto, G.2    Garrait, G.3    Alvarez, P.4    Beyssac, E.5    Subirade, M.6
  • 20
    • 33747501826 scopus 로고    scopus 로고
    • Preparation of angiotensin-I-converting enzyme inhibitory hydrolysate from unsupplemented caprine whey fermentation by various cheese microflora
    • Didelot, S., Bordenave-Juchereau, S., Rosenfeld, E., Fruitier-Arnaudin, I., Piot, J.-M., and Sannier, F., (2006). Preparation of angiotensin-I-converting enzyme inhibitory hydrolysate from unsupplemented caprine whey fermentation by various cheese microflora. Int. Dairy J. 16:976–983.
    • (2006) Int. Dairy J. , vol.16 , pp. 976-983
    • Didelot, S.1    Bordenave-Juchereau, S.2    Rosenfeld, E.3    Fruitier-Arnaudin, I.4    Piot, J.-M.5    Sannier, F.6
  • 21
    • 78649865389 scopus 로고    scopus 로고
    • Solid peptide nanoparticles–Structural characterization and quantification of cargo encapsulation
    • Dittrich, C., and Meier, W., (2010). Solid peptide nanoparticles–Structural characterization and quantification of cargo encapsulation. Macromolec. Biosci. 10:1406–1415.
    • (2010) Macromolec. Biosci. , vol.10 , pp. 1406-1415
    • Dittrich, C.1    Meier, W.2
  • 23
    • 45849129818 scopus 로고    scopus 로고
    • Antioxidant activity of proteins and peptides
    • Elias, R. J., Kellerby, S. S., and Decker, E. A., (2008). Antioxidant activity of proteins and peptides. Cr. Rev. Food Sci. 48:430–441.
    • (2008) Cr. Rev. Food Sci. , vol.48 , pp. 430-441
    • Elias, R.J.1    Kellerby, S.S.2    Decker, E.A.3
  • 24
    • 51049097278 scopus 로고    scopus 로고
    • Erdmann, K., Cheung, B. W. Y., and Schröder, H. (2008). The possible roles of food-derived bioactive peptides in reducing the risk of cardiovascular disease., J. Nutr. Biochem., :643–654
    • Erdmann, K., Cheung, B. W. Y., and Schröder, H. (2008). The possible roles of food-derived bioactive peptides in reducing the risk of cardiovascular disease. J. Nutr. Biochem. 19:643–654.
  • 25
    • 84888072817 scopus 로고    scopus 로고
    • The effect of limited proteolysis by different proteases on the formation of whey protein fibrils
    • Gao, Y.-Z., Xu, H.-H., Ju, T.-T., and Zhao, X.-H., (2013). The effect of limited proteolysis by different proteases on the formation of whey protein fibrils. J. Dairy Sci. 96:7383–7392.
    • (2013) J. Dairy Sci. , vol.96 , pp. 7383-7392
    • Gao, Y.-Z.1    Xu, H.-H.2    Ju, T.-T.3    Zhao, X.-H.4
  • 26
    • 84880940415 scopus 로고    scopus 로고
    • Influence of whey protein and its hydrolysate on prehypertension and postprandial hyperglycaemia in adult men
    • Goudarzi, M., and Madadlou, A., (2013). Influence of whey protein and its hydrolysate on prehypertension and postprandial hyperglycaemia in adult men. Int. Dairy J. 33:62–66.
    • (2013) Int. Dairy J. , vol.33 , pp. 62-66
    • Goudarzi, M.1    Madadlou, A.2
  • 27
    • 84921556530 scopus 로고    scopus 로고
    • Formulation of apple juice beverages containing whey protein isolate or whey protein hydrolysate based on sensory and physicochemical analysis
    • Goudarzi, M., Madadlou, A., Mousavi, M. E., and Emam-Djomeh, Z., (2015). Formulation of apple juice beverages containing whey protein isolate or whey protein hydrolysate based on sensory and physicochemical analysis. Int. J. Dairy Technol. 68:70–78.
    • (2015) Int. J. Dairy Technol. , vol.68 , pp. 70-78
    • Goudarzi, M.1    Madadlou, A.2    Mousavi, M.E.3    Emam-Djomeh, Z.4
  • 28
    • 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., and Belloque, J., (2004). 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. J. Agric. Food Chem. 52:6315–6319.
    • (2004) J. Agric. Food Chem. , vol.52 , pp. 6315-6319
    • Gómez-Ruiz, J.A.1    Recio, I.2    Belloque, J.3
  • 30
    • 4043078473 scopus 로고    scopus 로고
    • Influence of calcium on the self-assembly of partially hydrolyzed a-lactalbumin
    • Graveland-Bikker, J. F., Ipsen, R., Otte, J., and de Kruif, C. G., (2004). Influence of calcium on the self-assembly of partially hydrolyzed a-lactalbumin. Langmuir 20:6841–6846.
    • (2004) Langmuir , vol.20 , pp. 6841-6846
    • Graveland-Bikker, J.F.1    Ipsen, R.2    Otte, J.3    de Kruif, C.G.4
  • 31
    • 34249039632 scopus 로고    scopus 로고
    • Use of whey proteins for encapsulation and controlled delivery applications
    • Gunasekaran, S., Ko, S., and Xiao, L., (2007). Use of whey proteins for encapsulation and controlled delivery applications. J. Food Eng. 83:31–40.
    • (2007) J. Food Eng. , vol.83 , pp. 31-40
    • Gunasekaran, S.1    Ko, S.2    Xiao, L.3
  • 32
    • 0038045562 scopus 로고    scopus 로고
    • Ha, E., and Zemel, M. B. (2003). Functional properties of whey, whey components, and essential amino acids: mechanisms underlying health benefits for active people., J. Nutr. Biochem., :251–258
    • Ha, E., and Zemel, M. B. (2003). Functional properties of whey, whey components, and essential amino acids: mechanisms underlying health benefits for active people. J. Nutr. Biochem. 14:251–258.
  • 33
    • 34147123803 scopus 로고    scopus 로고
    • Food-derived peptides with biological activity: From research to food applications
    • Hartmann, R., and Meisel, H., (2007). Food-derived peptides with biological activity: From research to food applications. Curr. Opin. Biotech. 18:163–169.
    • (2007) Curr. Opin. Biotech. , vol.18 , pp. 163-169
    • Hartmann, R.1    Meisel, H.2
  • 34
    • 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., and Amigo, L., (2005). Preparation of antioxidant enzymatic hydrolysates from α-lactalbumin and β-lactoglobulin. Identification of active peptides by HPLC-MS/MS. J. Agric. Food Chem. 53:588–593.
    • (2005) J. Agric. Food Chem. , vol.53 , pp. 588-593
    • Hernández-Ledesma, B.1    Dávalos, A.2    Bartolomé, B.3    Amigo, L.4
  • 36
    • 84899428110 scopus 로고    scopus 로고
    • Associations between dairy foods, diabetes, and metabolic health: Potential mechanisms and future directions
    • Hirahatake, K. M., Slavin, J. L., Maki, K. C., and Adams, S. H., (2014). Associations between dairy foods, diabetes, and metabolic health: Potential mechanisms and future directions. Metabolism 63:618–627.
    • (2014) Metabolism , vol.63 , pp. 618-627
    • Hirahatake, K.M.1    Slavin, J.L.2    Maki, K.C.3    Adams, S.H.4
  • 37
    • 41149177461 scopus 로고    scopus 로고
    • Peptide amphiphile nanofibers with conjugated polydiacetylene backbones in their core
    • Hsu, L., Cvetanovich, G. L., and Stupp, S. I., (2008). Peptide amphiphile nanofibers with conjugated polydiacetylene backbones in their core. J. AOCS 130:3892–3899.
    • (2008) J. AOCS , vol.130 , pp. 3892-3899
    • Hsu, L.1    Cvetanovich, G.L.2    Stupp, S.I.3
  • 39
    • 0034987131 scopus 로고    scopus 로고
    • Impact of different dietary protein on rat growth, blood serum lipids and protein and liver cholesterol
    • Jacobucci, H. B., Sgarbieri, V. C., Dias, N. F. G. P., Borges, P., and Tanikawa, C., (2001). Impact of different dietary protein on rat growth, blood serum lipids and protein and liver cholesterol. Nutr. Res. 21:905–915.
    • (2001) Nutr. Res. , vol.21 , pp. 905-915
    • Jacobucci, H.B.1    Sgarbieri, V.C.2    Dias, N.F.G.P.3    Borges, P.4    Tanikawa, C.5
  • 40
    • 84870441206 scopus 로고    scopus 로고
    • Biochemical and metabolic mechanisms by which dietary whey protein may combat obesity and Type 2 diabetes
    • Jakubowicz, D., and Froy, O., (2013). Biochemical and metabolic mechanisms by which dietary whey protein may combat obesity and Type 2 diabetes. J. Nutr. Biochem. 24:1–5.
    • (2013) J. Nutr. Biochem. , vol.24 , pp. 1-5
    • Jakubowicz, D.1    Froy, O.2
  • 41
    • 84872807864 scopus 로고    scopus 로고
    • Characterization of reducible peptide oligomers as carriers for gene delivery
    • Kiselev, A., Egorova, A., Laukkanen, A., Baranov, V., and Urtti, A., (2013). Characterization of reducible peptide oligomers as carriers for gene delivery. Int. J. Pharm. 441:736–747.
    • (2013) Int. J. Pharm. , vol.441 , pp. 736-747
    • Kiselev, A.1    Egorova, A.2    Laukkanen, A.3    Baranov, V.4    Urtti, A.5
  • 42
    • 75849156917 scopus 로고    scopus 로고
    • Milk proteins as vehicles for bioactives
    • Livney, Y. D., (2010). Milk proteins as vehicles for bioactives. Cur. Opin. Colloid Interface Sci. 15:73–83.
    • (2010) Cur. Opin. Colloid Interface Sci. , vol.15 , pp. 73-83
    • Livney, Y.D.1
  • 44
    • 79960093689 scopus 로고    scopus 로고
    • ACE-inhibitory peptides from casein hydrolyzed with nanoencapsulated protease
    • Madadlou, A., Sheehan, D., Emam-Djomeh, Z., and Mousavi, M. E., (2011). ACE-inhibitory peptides from casein hydrolyzed with nanoencapsulated protease. J. Sci. Food Agric. 91:2112–2116.
    • (2011) J. Sci. Food Agric. , vol.91 , pp. 2112-2116
    • Madadlou, A.1    Sheehan, D.2    Emam-Djomeh, Z.3    Mousavi, M.E.4
  • 46
    • 84961743132 scopus 로고    scopus 로고
    • Characterization of fibrillated antioxidant whey protein hydrolysate and comparison with fibrillated protein solution
    • Mohammadian, M., and Madadlou, A., (2016). Characterization of fibrillated antioxidant whey protein hydrolysate and comparison with fibrillated protein solution. Food Hydrocolloid. 52:221–230.
    • (2016) Food Hydrocolloid. , vol.52 , pp. 221-230
    • Mohammadian, M.1    Madadlou, A.2
  • 47
    • 77955675378 scopus 로고    scopus 로고
    • Comparison of different sources and degrees of hydrolysis of dietary protein: Effect on plasma amino acids, dipeptides, and insulin responses in human subjects
    • et al
    • Morifuji, M., Ishizaka, M., Baba, S., Fukuda, K., Matsumoto, H., Koga, J., et al. (2010). Comparison of different sources and degrees of hydrolysis of dietary protein: Effect on plasma amino acids, dipeptides, and insulin responses in human subjects. J. Agric. Food Chem. 58:8788–8797.
    • (2010) J. Agric. Food Chem. , vol.58 , pp. 8788-8797
    • Morifuji, M.1    Ishizaka, M.2    Baba, S.3    Fukuda, K.4    Matsumoto, H.5    Koga, J.6
  • 48
  • 49
    • 0031464182 scopus 로고    scopus 로고
    • Angiotensin-I-converting enzyme inhibitory activities of gastric and pancreatic proteinase digests of whey proteins
    • Mullally, M. M., Meisel, H., and FitzGerald, R. J., (1997). Angiotensin-I-converting enzyme inhibitory activities of gastric and pancreatic proteinase digests of whey proteins. Int. Dairy J. 7:299–303.
    • (1997) Int. Dairy J. , vol.7 , pp. 299-303
    • Mullally, M.M.1    Meisel, H.2    FitzGerald, R.J.3
  • 50
    • 84877836950 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV inhibitory properties of a whey protein hydrolysate: Influence of fractionation, stability to simulated gastrointestinal digestion and foodedrug interaction
    • Nongonierma, A. B., and FitzGerald, R. J., (2013). Dipeptidyl peptidase IV inhibitory properties of a whey protein hydrolysate: Influence of fractionation, stability to simulated gastrointestinal digestion and foodedrug interaction. Int. Dairy J. 32:33–39.
    • (2013) Int. Dairy J. , vol.32 , pp. 33-39
    • Nongonierma, A.B.1    FitzGerald, R.J.2
  • 51
    • 84879481214 scopus 로고    scopus 로고
    • Insulinotropic properties of whey protein hydrolysates and impact of peptide fractionation on insulinotropic response
    • Nongonierma, A. B., Gaudel, C., Murray, B. A., Flynn, S., Kelly, P. M., Newsholme, P., and FitzGerlad, R. J., (2013). Insulinotropic properties of whey protein hydrolysates and impact of peptide fractionation on insulinotropic response. Int. Dairy J. 32:163–168.
    • (2013) Int. Dairy J. , vol.32 , pp. 163-168
    • Nongonierma, A.B.1    Gaudel, C.2    Murray, B.A.3    Flynn, S.4    Kelly, P.M.5    Newsholme, P.6    FitzGerlad, R.J.7
  • 52
    • 84937774232 scopus 로고    scopus 로고
    • Maillard conjugation of lactulose with potentially bioactive peptides
    • Nooshkam, M., and Madadlou, A., (2016). Maillard conjugation of lactulose with potentially bioactive peptides. Food Chem. 192:831–836.
    • (2016) Food Chem. , vol.192 , pp. 831-836
    • Nooshkam, M.1    Madadlou, A.2
  • 53
    • 84952837225 scopus 로고    scopus 로고
    • Microwave-assisted isomerisation of lactose to lactulose and Maillard conjugation of lactulose and lactose with whey proteins and peptides
    • Nooshkam, M., and Madadlou, A., (2016). Microwave-assisted isomerisation of lactose to lactulose and Maillard conjugation of lactulose and lactose with whey proteins and peptides. Food Chem. 200:1–9.
    • (2016) Food Chem. , vol.200 , pp. 1-9
    • Nooshkam, M.1    Madadlou, A.2
  • 54
    • 85011552145 scopus 로고    scopus 로고
    • Nourbakhsh, H., Emam-Djomeh, Z., Madadlou, A., Mousavi, M. E., Moosavi-Movahedi, A. A., and Gunasekaran, S. (2017). Antioxidant peptidic particles for delivery of gallic acid., J. Food Process. Preserv., (1):e12767
    • Nourbakhsh, H., Emam-Djomeh, Z., Madadlou, A., Mousavi, M. E., Moosavi-Movahedi, A. A., and Gunasekaran, S. (2017). Antioxidant peptidic particles for delivery of gallic acid. J. Food Process. Preserv. 41(1):e12767. doi:10.1111/jfpp.12767.
  • 55
    • 84964579577 scopus 로고    scopus 로고
    • One-pot nanoparticulation of potentially bioactive peptides and gallic acid encapsulation
    • Nourbakhsh, H., Madadlou, A., Emam-Djomeh, Z., Wang, Y.-C., and Gunasekaran, S., (2016a). One-pot nanoparticulation of potentially bioactive peptides and gallic acid encapsulation. Food Chem. 210:317–324.
    • (2016) Food Chem. , vol.210 , pp. 317-324
    • Nourbakhsh, H.1    Madadlou, A.2    Emam-Djomeh, Z.3    Wang, Y.-C.4    Gunasekaran, S.5
  • 56
    • 84959255132 scopus 로고    scopus 로고
    • One-Pot procedure for recovery of gallic acid from wastewater and encapsulation within protein particles
    • Nourbakhsh, H., Madadlou, A., Emam-Djomeh, Z., Wang, Y.-C., Gunasekaran, S., and Mousavi, M. E., (2016b). One-Pot procedure for recovery of gallic acid from wastewater and encapsulation within protein particles. J. Agric. Food Chem. 64:1575–1582.
    • (2016) J. Agric. Food Chem. , vol.64 , pp. 1575-1582
    • Nourbakhsh, H.1    Madadlou, A.2    Emam-Djomeh, Z.3    Wang, Y.-C.4    Gunasekaran, S.5    Mousavi, M.E.6
  • 58
    • 79961042019 scopus 로고    scopus 로고
    • Hierarchical organization of purely peptidic amphiphiles into peptide beads
    • Ouboter, D. B., Schuster, T. B., Mantion, A., and Meier, W., (2011). Hierarchical organization of purely peptidic amphiphiles into peptide beads. J. Phys. Chem. 115:14583–14590.
    • (2011) J. Phys. Chem. , vol.115 , pp. 14583-14590
    • Ouboter, D.B.1    Schuster, T.B.2    Mantion, A.3    Meier, W.4
  • 59
    • 84887015748 scopus 로고    scopus 로고
    • Self-assembled peptide beads used as a template for ordered gold nanoparticle superstructures
    • Ouboter, D. B., Schuster, T. B., Sigg, S. J., and Meier, W. P., (2013). Self-assembled peptide beads used as a template for ordered gold nanoparticle superstructures. Colloid Surface B. 112:542–547.
    • (2013) Colloid Surface B. , vol.112 , pp. 542-547
    • Ouboter, D.B.1    Schuster, T.B.2    Sigg, S.J.3    Meier, W.P.4
  • 60
    • 0035755659 scopus 로고    scopus 로고
    • Antioxidative activity of whey protein hydrolysates in a liposomal system
    • Peña-Ramos, E. A., and Xiong, Y. L., (2001). Antioxidative activity of whey protein hydrolysates in a liposomal system. J. Dairy Sci., 84:2577–2583.
    • (2001) J. Dairy Sci. , vol.84 , pp. 2577-2583
    • Peña-Ramos, E.A.1    Xiong, Y.L.2
  • 61
    • 0038640588 scopus 로고    scopus 로고
    • Whey and soy protein hydrolysates inhibit lipid oxidation in cooked pork patties
    • Peña-Ramos, E. A., and Xiong, Y. L., (2003). Whey and soy protein hydrolysates inhibit lipid oxidation in cooked pork patties. Meat Sci. 64:259–263.
    • (2003) Meat Sci. , vol.64 , pp. 259-263
    • Peña-Ramos, E.A.1    Xiong, Y.L.2
  • 62
    • 7044286379 scopus 로고    scopus 로고
    • Fractionation and characterisation for antioxidant activity of hydrolysed whey protein
    • Peña-Ramos, E. A., Xiong, Y. L., and Arteaga, G. E., (2003). Fractionation and characterisation for antioxidant activity of hydrolysed whey protein. J. Sci. Food Agric. 84:1908–1918.
    • (2003) J. Sci. Food Agric. , vol.84 , pp. 1908-1918
    • Peña-Ramos, E.A.1    Xiong, Y.L.2    Arteaga, G.E.3
  • 63
    • 52949091925 scopus 로고    scopus 로고
    • Antioxidant activity of peptide fractions from whey protein hydrolysates as measured by electron spin resonance
    • Peng, X., Xiong, Y. L., and Kong, B., (2009). Antioxidant activity of peptide fractions from whey protein hydrolysates as measured by electron spin resonance. Food Chem. 113:196–201.
    • (2009) Food Chem. , vol.113 , pp. 196-201
    • Peng, X.1    Xiong, Y.L.2    Kong, B.3
  • 64
    • 0034633086 scopus 로고    scopus 로고
    • Bioactive peptides derived from bovine whey proteins: opioid and ace-inhibitory peptides
    • Pihlanto-Leppälä, A., (2001). Bioactive peptides derived from bovine whey proteins: opioid and ace-inhibitory peptides. Trends Food Sci. Tech. 11:347–356.
    • (2001) Trends Food Sci. Tech. , vol.11 , pp. 347-356
    • Pihlanto-Leppälä, A.1
  • 65
    • 33646496790 scopus 로고    scopus 로고
    • Physical performance of exercising young rats fed hydrolysed whey protein at a sub-optimal level
    • Pimenta, F. M. V., Abecia-Soria, M. I., Flá via Auler, F., and Amaya-Farfan, J., (2006). Physical performance of exercising young rats fed hydrolysed whey protein at a sub-optimal level. Int. Dairy J. 16:984–991.
    • (2006) Int. Dairy J. , vol.16 , pp. 984-991
    • Pimenta, F.M.V.1    Abecia-Soria, M.I.2    Flá via Auler, F.3    Amaya-Farfan, J.4
  • 66
    • 84930936669 scopus 로고    scopus 로고
    • Insulin/poly(ethylene glycol)-block-poly(L-lysine) complexes: Physicochemical properties and protein encapsulation
    • Pippa, N., Kalinova, R., Dimitrov, I., Pispas, S., and Demetzos, C., (2015). Insulin/poly(ethylene glycol)-block-poly(L-lysine) complexes: Physicochemical properties and protein encapsulation. J. Phys. Chem. B. 119:6813–6819.
    • (2015) J. Phys. Chem. B. , vol.119 , pp. 6813-6819
    • Pippa, N.1    Kalinova, R.2    Dimitrov, I.3    Pispas, S.4    Demetzos, C.5
  • 67
    • 85027944546 scopus 로고    scopus 로고
    • Oxidized forms of dietary antioxidants: Friends or foes?
    • Poljsak, B., and Milisav, I., (2014). Oxidized forms of dietary antioxidants: Friends or foes?. Trends Food Sci. Tech. 39:156–166.
    • (2014) Trends Food Sci. Tech. , vol.39 , pp. 156-166
    • Poljsak, B.1    Milisav, I.2
  • 68
    • 84939148835 scopus 로고    scopus 로고
    • Stimuli-responsive protamine-based biodegradable nanocapsules for enhanced bioavailability and intracellular delivery of anticancer agents
    • Radhakrishnan, K., Thomas, M. B., Pulakkat, S., Gnanadhas, D. P., Chakravortty, D., and Raichur, A. M., (2015). Stimuli-responsive protamine-based biodegradable nanocapsules for enhanced bioavailability and intracellular delivery of anticancer agents. J. Nanopart. Res. 17:341.
    • (2015) J. Nanopart. Res. , vol.17 , pp. 341
    • Radhakrishnan, K.1    Thomas, M.B.2    Pulakkat, S.3    Gnanadhas, D.P.4    Chakravortty, D.5    Raichur, A.M.6
  • 69
    • 84883542204 scopus 로고    scopus 로고
    • Immunomodulatory activities of whey b-lactoglobulin tryptic-digested fractions
    • Rodríguez-Carrio, J., Fernández, A., Riera, F. A., and Suárez, A., (2014). Immunomodulatory activities of whey b-lactoglobulin tryptic-digested fractions. Int. Dairy J. 34:65–73.
    • (2014) Int. Dairy J. , vol.34 , pp. 65-73
    • Rodríguez-Carrio, J.1    Fernández, A.2    Riera, F.A.3    Suárez, A.4
  • 70
    • 84886246769 scopus 로고    scopus 로고
    • Microemulsification—Cold gelation of whey proteins for nanoencapsulation of date palm pit extract
    • Sadeghi, S., Madadlou, A., and Yarmand, M., (2014). Microemulsification—Cold gelation of whey proteins for nanoencapsulation of date palm pit extract. Food Hydrocolloid. 35:590–596.
    • (2014) Food Hydrocolloid. , vol.35 , pp. 590-596
    • Sadeghi, S.1    Madadlou, A.2    Yarmand, M.3
  • 71
    • 84878313919 scopus 로고    scopus 로고
    • Dipeptidyl peptidase-IV inhibitory peptides generated by tryptic hydrolysis of a whey protein concentrate rich in b-lactoglobulin
    • Silveira, S. T., Martínez-Maqueda, D., Recio, I., and Hernández-Ledesma, B., (2013). Dipeptidyl peptidase-IV inhibitory peptides generated by tryptic hydrolysis of a whey protein concentrate rich in b-lactoglobulin. Food Chem. 141:1072–1077.
    • (2013) Food Chem. , vol.141 , pp. 1072-1077
    • Silveira, S.T.1    Martínez-Maqueda, D.2    Recio, I.3    Hernández-Ledesma, B.4
  • 72
    • 44549084148 scopus 로고    scopus 로고
    • Whey and whey proteins—From ‘gutter-to-gold’
    • Smithers, G. W., (2008). Whey and whey proteins—From ‘gutter-to-gold’. Int. Dairy J. 18:695–704.
    • (2008) Int. Dairy J. , vol.18 , pp. 695-704
    • Smithers, G.W.1
  • 73
    • 33947309536 scopus 로고    scopus 로고
    • Whey protein hydrolysate: Functional properties, nutritional quality and utilization in beverage formulation
    • Sinha, R., Radha, C., Prakash, J., and Kaul, P., (2007). Whey protein hydrolysate: Functional properties, nutritional quality and utilization in beverage formulation. Food Chem. 101:1484–1491.
    • (2007) Food Chem. , vol.101 , pp. 1484-1491
    • Sinha, R.1    Radha, C.2    Prakash, J.3    Kaul, P.4
  • 75
    • 84927675042 scopus 로고    scopus 로고
    • Whey protein preloads are more beneficial than soy protein preloads in regulating appetite, calorie intake, anthropometry, and body composition of overweight and obese men
    • Tahavorgar, A., Vafa, M., Shidfar, F., Gohari, M., and Heydari, I., (2014). Whey protein preloads are more beneficial than soy protein preloads in regulating appetite, calorie intake, anthropometry, and body composition of overweight and obese men. Nutr. Res. 34:856–861.
    • (2014) Nutr. Res. , vol.34 , pp. 856-861
    • Tahavorgar, A.1    Vafa, M.2    Shidfar, F.3    Gohari, M.4    Heydari, I.5
  • 76
    • 84866010946 scopus 로고    scopus 로고
    • An antioxidant peptide derived from Ostrich (Struthio camelus) egg white protein hydrolysates
    • Tanzadehpanah, H., Asoodeh, A., and Chamani, J., (2012). An antioxidant peptide derived from Ostrich (Struthio camelus) egg white protein hydrolysates. Food Res. Int. 49:105–111.
    • (2012) Food Res. Int. , vol.49 , pp. 105-111
    • Tanzadehpanah, H.1    Asoodeh, A.2    Chamani, J.3
  • 77
    • 84856993467 scopus 로고    scopus 로고
    • Manufacture of bioactive peptide-rich concentrates from whey: Characterization of pilot process
    • Tavares, T., Amorim, M., Gomes, D., Pintado, M. E., Pereira, C. D., and Malcata, F. X., (2012). Manufacture of bioactive peptide-rich concentrates from whey: Characterization of pilot process. J. Food Eng. 110:547–552.
    • (2012) J. Food Eng. , vol.110 , pp. 547-552
    • Tavares, T.1    Amorim, M.2    Gomes, D.3    Pintado, M.E.4    Pereira, C.D.5    Malcata, F.X.6
  • 78
    • 80755143648 scopus 로고    scopus 로고
    • The Portuguese Paradox: Why do some inhabitants of Portugal appear to live so long when their diet is based on whey cheese?
    • Tavares, T., and Malacta, F. X., (2012). The Portuguese Paradox: Why do some inhabitants of Portugal appear to live so long when their diet is based on whey cheese?. Food Chem. 131:727–729.
    • (2012) Food Chem. , vol.131 , pp. 727-729
    • Tavares, T.1    Malacta, F.X.2
  • 79
    • 84928320966 scopus 로고    scopus 로고
    • Beta-lactoglobulin-based encapsulating systems as emerging bioavailability enhancers for nutraceuticals: a review
    • Teng, Z., Xu, R., and Wang, Q., (2015). Beta-lactoglobulin-based encapsulating systems as emerging bioavailability enhancers for nutraceuticals: a review. RSC Adv. 5:35138–35154.
    • (2015) RSC Adv. , vol.5 , pp. 35138-35154
    • Teng, Z.1    Xu, R.2    Wang, Q.3
  • 80
    • 0000870154 scopus 로고
    • Interfacial properties of tryptic peptides of β-lactoglobulin
    • Turgeon, S. L., Gauthier, S. F., Mollé, D., and Léonil, J., (1992). Interfacial properties of tryptic peptides of β-lactoglobulin. J. Agric. Food Chem. 40:669–675.
    • (1992) J. Agric. Food Chem. , vol.40 , pp. 669-675
    • Turgeon, S.L.1    Gauthier, S.F.2    Mollé, D.3    Léonil, J.4
  • 81
    • 80052897910 scopus 로고    scopus 로고
    • Novel dipeptidyl peptidase-4-inhibiting peptide derived from β-lactoglobulin
    • Uchida, M., Ohshiba, Y., and Mogami, O., (2011). Novel dipeptidyl peptidase-4-inhibiting peptide derived from β-lactoglobulin. J. Pharmacol. Sci. 117:63–66.
    • (2011) J. Pharmacol. Sci. , vol.117 , pp. 63-66
    • Uchida, M.1    Ohshiba, Y.2    Mogami, O.3
  • 82
    • 2342569607 scopus 로고    scopus 로고
    • A quantitative in silico analysis calculates the angiotensin I converting enzyme (ACE) inhibitory activity in pea and whey protein digests
    • Vermeirssen, V., van der Bent, A., Camp, J. V., van Amerongen, A., and Verstraete, W., (2004). A quantitative in silico analysis calculates the angiotensin I converting enzyme (ACE) inhibitory activity in pea and whey protein digests. Biochimie 86:231–239.
    • (2004) Biochimie , vol.86 , pp. 231-239
    • Vermeirssen, V.1    van der Bent, A.2    Camp, J.V.3    van Amerongen, A.4    Verstraete, W.5
  • 83
    • 53849092685 scopus 로고    scopus 로고
    • Will all Americans become overweight or obese? Estimating the progression and cost of the US obesity epidemic
    • Wang, Y., Beydoun, M. A., Liang, L., Caballero, B., and Kumanyika, S. K., (2008). Will all Americans become overweight or obese? Estimating the progression and cost of the US obesity epidemic. Obesity 16:2323–2330.
    • (2008) Obesity , vol.16 , pp. 2323-2330
    • Wang, Y.1    Beydoun, M.A.2    Liang, L.3    Caballero, B.4    Kumanyika, S.K.5
  • 84
    • 0008334620 scopus 로고    scopus 로고
    • Nutraceuticals: A brief review of historical and teleological aspects
    • Wildman R.E.C., (ed), CRC Press, New York:. Chapter 1, Ed
    • Wildman, R. E. C., (2001). Nutraceuticals: A brief review of historical and teleological aspects. In: Handbook of Nutraceuticals and Functional Foods. Chapter 1, Wildman, R. E. C., Ed., CRC Press, New York.
    • (2001) Handbook of Nutraceuticals and Functional Foods
    • Wildman, R.E.C.1
  • 86
    • 84878855642 scopus 로고    scopus 로고
    • Nanoparticles for oral delivery: Targeted nanoparticles with peptidic ligands for oral protein delivery
    • Yun, Y., Cho, Y. W., & Park, K., (2013). Nanoparticles for oral delivery: Targeted nanoparticles with peptidic ligands for oral protein delivery. Adv. Drug Deliver. Rev. 65:822–832.
    • (2013) Adv. Drug Deliver. Rev. , vol.65 , pp. 822-832
    • Yun, Y.1    Cho, Y.W.2    Park, K.3
  • 87
    • 84961340941 scopus 로고    scopus 로고
    • Caffeine-loaded whey protein hydrogels reinforced with gellan and enriched with calcium chloride
    • Zand-Rajabi, H., and Madadlou, A., (2016). Caffeine-loaded whey protein hydrogels reinforced with gellan and enriched with calcium chloride. Int. Dairy J. 56:38–44.
    • (2016) Int. Dairy J. , vol.56 , pp. 38-44
    • Zand-Rajabi, H.1    Madadlou, A.2
  • 88
    • 70349895279 scopus 로고    scopus 로고
    • Microemulsions as nanoreactors to produce whey protein nanoparticles with enhanced heat stability by sequential enzymatic cross-linking and thermal pretreatments
    • Zhang, W., and Zhong, Q., (2009). Microemulsions as nanoreactors to produce whey protein nanoparticles with enhanced heat stability by sequential enzymatic cross-linking and thermal pretreatments. J. Agric. Food Chem. 57:9181–9189.
    • (2009) J. Agric. Food Chem. , vol.57 , pp. 9181-9189
    • Zhang, W.1    Zhong, Q.2
  • 89
    • 70449651755 scopus 로고    scopus 로고
    • Microemulsions as nanoreactors to produce whey protein nanoparticles with enhanced heat stability by thermal pretreatment
    • Zhang, W., and Zhong, Q., (2010). Microemulsions as nanoreactors to produce whey protein nanoparticles with enhanced heat stability by thermal pretreatment. Food Chem. 119:1318–1325
    • (2010) Food Chem. , vol.119 , pp. 1318-1325
    • Zhang, W.1    Zhong, Q.2


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