메뉴 건너뛰기




Volumn 4, Issue 2-3, 2013, Pages 76-84

In vitro infant digestion of whey protein-dextran glycates

Author keywords

Allergy; Dairy; Food; Glycation; In vitro infant digestion; Maillard

Indexed keywords


EID: 84891610018     PISSN: 18691978     EISSN: 18691986     Source Type: Journal    
DOI: 10.1007/s13228-013-0032-6     Document Type: Article
Times cited : (17)

References (39)
  • 1
    • 84866667012 scopus 로고    scopus 로고
    • Bioactive peptides of buffalo, camel, goat, sheep, mare, and yak milks and milk products
    • 1:CAS:528:DC%2BC38Xhtlyqs73L 10.1080/87559129.2012.692137
    • Abd El-Salam MH, El-Shibiny S (2013) Bioactive peptides of buffalo, camel, goat, sheep, mare, and yak milks and milk products. Food Rev Int 29(1):1-23
    • (2013) Food Rev Int , vol.29 , Issue.1 , pp. 1-23
    • Abd El-Salam, M.H.1    El-Shibiny, S.2
  • 2
    • 33846207960 scopus 로고    scopus 로고
    • Whey protein-maltodextrin conjugates as emulsifying agents: An alternative to gum arabic
    • DOI 10.1016/j.foodhyd.2005.07.014, PII S0268005X06001482
    • Akhtar M, Dickinson E (2007) Whey protein-maltodextrin conjugates as emulsifying agents: an alternative to gum Arabic. Food Hydrocolloids 21(4):607-616 (Pubitemid 46097183)
    • (2007) Food Hydrocolloids , vol.21 , Issue.4 , pp. 607-616
    • Akhtar, M.1    Dickinson, E.2
  • 4
    • 0034877014 scopus 로고    scopus 로고
    • Effect of chemical and genetic attachment of polysaccharides to proteins on the production of IgG and IgE
    • DOI 10.1021/jf001120t
    • Arita K, Babiker EE, Azakami H, Kato A (2001) Effect of chemical and genetic attachment of polysaccharides to proteins on the production of IgG and IgE. J Agric Food Chem 49(4):2030-2036 (Pubitemid 32816855)
    • (2001) Journal of Agricultural and Food Chemistry , vol.49 , Issue.4 , pp. 2030-2036
    • Arita, K.1    Babiker, E.E.2    Azakami, H.3    Kato, A.4
  • 5
    • 84861757630 scopus 로고    scopus 로고
    • Chromatographic purification and characterization of whey protein-dextran glycation products
    • 1:CAS:528:DC%2BC38XotVarsb4%3D 10.1016/j.chroma.2012.04.057
    • Bund T, Allelein S, Arunkumar A, Lucey JA, Etzel MR (2012) Chromatographic purification and characterization of whey protein-dextran glycation products. J Chromatogr A 1244:98-105
    • (2012) J Chromatogr A , vol.1244 , pp. 98-105
    • Bund, T.1    Allelein, S.2    Arunkumar, A.3    Lucey, J.A.4    Etzel, M.R.5
  • 6
    • 0036186189 scopus 로고    scopus 로고
    • Influence of protein source, type, and concentration, and product form on the protein quality of commercial enteral formulas
    • Castillo G, Sanz MA, Serrano MA, Hernandez A (2002) Influence of protein source, type, and concentration, and product form on the protein quality of commercial enteral formulas. J Food Sci 67(1):328-334 (Pubitemid 34190823)
    • (2002) Journal of Food Science , vol.67 , Issue.1 , pp. 328-334
    • Castillo, G.1    Sanz, M.A.2    Serrano, M.A.3    Hernandez, A.4
  • 7
    • 77955510256 scopus 로고    scopus 로고
    • Effect of glycation on the gastrointestinal digestibility and immunoreactivity of bovine beta-lactoglobulin
    • 1:CAS:528:DC%2BC3cXpvVKns7k%3D 10.1016/j.idairyj.2010.04.002
    • Corzo-Martinez M, Soria AC, Belloque J, Villamiel M, Moreno FJ (2010) Effect of glycation on the gastrointestinal digestibility and immunoreactivity of bovine beta-lactoglobulin. Int Dairy J 20(11):742-752
    • (2010) Int Dairy J , vol.20 , Issue.11 , pp. 742-752
    • Corzo-Martinez, M.1    Soria, A.C.2    Belloque, J.3    Villamiel, M.4    Moreno, F.J.5
  • 10
    • 72449136262 scopus 로고    scopus 로고
    • Combining the dynamic TNO-gastrointestinal tract system with a Caco-2 cell culture model: Application to the assessment of lycopene and alpha-tocopherol bioavailability from a whole food
    • 1:CAS:528:DC%2BD1MXhtlyhtL7M 10.1021/jf902392a
    • Deat E, Blanquet-Diot S, Jarrige JF, Denis S, Beyssac E, Alric M (2009) Combining the dynamic TNO-gastrointestinal tract system with a Caco-2 cell culture model: application to the assessment of lycopene and alpha-tocopherol bioavailability from a whole food. J Agric Food Chem 57(23):11314-11320
    • (2009) J Agric Food Chem , vol.57 , Issue.23 , pp. 11314-11320
    • Deat, E.1    Blanquet-Diot, S.2    Jarrige, J.F.3    Denis, S.4    Beyssac, E.5    Alric, M.6
  • 11
    • 84860738206 scopus 로고    scopus 로고
    • An investigation into the utility of a multi-compartmental, dynamic, system of the upper gastrointestinal tract to support formulation development and establish bioequivalence of poorly soluble drugs
    • 1:CAS:528:DC%2BC38Xlslansb0%3D 10.1208/s12248-012-9333-x
    • Dickinson PA, Abu Rmaileh R, Ashworth L, Barker RA, Burke WM, Patterson CM, Stainforth N, Yasin M (2012) An investigation into the utility of a multi-compartmental, dynamic, system of the upper gastrointestinal tract to support formulation development and establish bioequivalence of poorly soluble drugs. AAPS J 14(2):196-205
    • (2012) AAPS J , vol.14 , Issue.2 , pp. 196-205
    • Dickinson, P.A.1    Abu Rmaileh, R.2    Ashworth, L.3    Barker, R.A.4    Burke, W.M.5    Patterson, C.M.6    Stainforth, N.7    Yasin, M.8
  • 14
    • 84891622176 scopus 로고    scopus 로고
    • Improvement of bioactivity of alpha-lactalbumin through Maillard reaction with dextran
    • Hong S-T, Ha Y-M, Nam M-H, Lee K-W (2012) Improvement of bioactivity of alpha-lactalbumin through Maillard reaction with dextran. FASEB J 26(1-MeetingAbstracts):625-627
    • (2012) FASEB J , vol.26 , Issue.1 , pp. 625-627
    • Hong, S.-T.1    Ha, Y.-M.2    Nam, M.-H.3    Lee, K.-W.4
  • 15
    • 0036980003 scopus 로고    scopus 로고
    • Frequency of cow's milk allergy in childhood
    • Host A (2002) Frequency of cow's milk allergy in childhood. Ann Allergy Asthma Immunol 89(6):33-37 (Pubitemid 36183828)
    • (2002) Annals of Allergy, Asthma and Immunology , vol.89 , Issue.6 SUPPL. 1 , pp. 33-37
    • Host, A.1
  • 16
    • 77956044791 scopus 로고    scopus 로고
    • Comparison of the digestion of caseins and whey proteins in equine, bovine, caprine and human milks by human gastrointestinal enzymes
    • 1:CAS:528:DC%2BC3cXhtlGjs73O 10.1051/dst/2010018
    • Inglingstad RA, Devold TG, Eriksen EK, Holm H, Jacobsen M, Liland KH, Rukke EO, Vegarud GE (2010) Comparison of the digestion of caseins and whey proteins in equine, bovine, caprine and human milks by human gastrointestinal enzymes. Dairy Sci Technol 90(5):549-563
    • (2010) Dairy Sci Technol , vol.90 , Issue.5 , pp. 549-563
    • Inglingstad, R.A.1    Devold, T.G.2    Eriksen, E.K.3    Holm, H.4    Jacobsen, M.5    Liland, K.H.6    Rukke, E.O.7    Vegarud, G.E.8
  • 17
    • 0020287591 scopus 로고
    • In vitro digestion of cowês milk proteins by duodenal juice from infants with various gastrointestinal disorders
    • 1:STN:280:DyaL3s3ptlylsg%3D%3D 10.1097/00005176-198201020-00006
    • Jakobsson I, Lindberg T, Benediktsson B (1982) In vitro digestion of cowês milk proteins by duodenal juice from infants with various gastrointestinal disorders. J Pediatr Gastroenterol Nutr 1(2):183-192
    • (1982) J Pediatr Gastroenterol Nutr , vol.1 , Issue.2 , pp. 183-192
    • Jakobsson, I.1    Lindberg, T.2    Benediktsson, B.3
  • 18
    • 33750956935 scopus 로고    scopus 로고
    • Glycosylation of individual whey proteins by Maillard reaction using dextran of different molecular mass
    • DOI 10.1016/j.foodhyd.2006.05.006, PII S0268005X06001032
    • Jimenez-Castano L, Villamiel M, Lopez-Fandino R (2007) Glycosylation of individual whey proteins by Maillard reaction using dextran of different molecular mass. Food Hydrocolloids 21(3):433-443 (Pubitemid 44739138)
    • (2007) Food Hydrocolloids , vol.21 , Issue.3 , pp. 433-443
    • Jimenez-Castano, L.1    Villamiel, M.2    Lopez-Fandino, R.3
  • 19
    • 80053093893 scopus 로고    scopus 로고
    • Human immunoglobulin e (IgE) binding to heated and glycated ovalbumin and ovomucoid before and after in vitro digestion
    • 1:CAS:528:DC%2BC3MXhtVOktrvI 10.1021/jf2014638
    • Jimenez-Saiz R, Belloque J, Molina E, Lopez-Fandino R (2011) Human immunoglobulin E (IgE) binding to heated and glycated ovalbumin and ovomucoid before and after in vitro digestion. J Agric Food Chem 59(18):10044-10051
    • (2011) J Agric Food Chem , vol.59 , Issue.18 , pp. 10044-10051
    • Jimenez-Saiz, R.1    Belloque, J.2    Molina, E.3    Lopez-Fandino, R.4
  • 21
    • 0035117504 scopus 로고    scopus 로고
    • Reduced immunogenicity of β-lactoglobulin by conjugation with carboxymethyl dextran differing in molecular weight
    • DOI 10.1021/jf000926q
    • Kobayashi K, Hirano A, Ohta A, Yoshida T, Takahashi K, Hattori M (2001) Reduced immunogenicity of beta-lactoglobulin by conjugation with carboxymethyl dextran differing in molecular weight. J Agric Food Chem 49(2):823-831 (Pubitemid 32172634)
    • (2001) Journal of Agricultural and Food Chemistry , vol.49 , Issue.2 , pp. 823-831
    • Kobayashi, K.1    Hirano, A.2    Ohta, A.3    Yoshida, T.4    Takahashi, K.5    Hattori, M.6
  • 22
    • 84858237139 scopus 로고    scopus 로고
    • Validation of an in vitro figestive system for studying macronutrient decomposition in humans
    • 1:CAS:528:DC%2BC38XhsFyjtrk%3D 10.3945/jn.111.148635
    • Kopf-Bolanz KA, Schwander F, Gijs M, Vergeres G, Portmann R, Egger L (2012) Validation of an in vitro figestive system for studying macronutrient decomposition in humans. J Nutr 142(2):245-250
    • (2012) J Nutr , vol.142 , Issue.2 , pp. 245-250
    • Kopf-Bolanz, K.A.1    Schwander, F.2    Gijs, M.3    Vergeres, G.4    Portmann, R.5    Egger, L.6
  • 23
    • 79961171984 scopus 로고    scopus 로고
    • Controlling lipid digestibility: Response of lipid droplets coated by beta-lactoglobulin-dextran Maillard conjugates to simulated gastrointestinal conditions
    • 1:CAS:528:DC%2BC3MXhtVWjsrbJ 10.1016/j.foodhyd.2011.05.011
    • Lesmes U, McClements DJ (2012) Controlling lipid digestibility: response of lipid droplets coated by beta-lactoglobulin-dextran Maillard conjugates to simulated gastrointestinal conditions. Food Hydrocolloids 26(1):221-230
    • (2012) Food Hydrocolloids , vol.26 , Issue.1 , pp. 221-230
    • Lesmes, U.1    McClements, D.J.2
  • 24
    • 84860395576 scopus 로고    scopus 로고
    • Effects of Maillard reaction conditions on the antigenicity of alpha-lactalbumin and beta-lactoglobulin in whey protein conjugated with maltose
    • 1:CAS:528:DC%2BC3MXhtVCrtr3P 10.1007/s00217-011-1532-7
    • Li Z, Luo YK, Feng LG (2011) Effects of Maillard reaction conditions on the antigenicity of alpha-lactalbumin and beta-lactoglobulin in whey protein conjugated with maltose. Eur Food Res Technol 233(3):387-394
    • (2011) Eur Food Res Technol , vol.233 , Issue.3 , pp. 387-394
    • Li, Z.1    Luo, Y.K.2    Feng, L.G.3
  • 25
    • 0031944894 scopus 로고    scopus 로고
    • Validation of a three-stage compound continuous culture system for investigating the effect of retention time on the ecology and metabolism of bacteria in the human colon
    • DOI 10.1007/s002489900072
    • Macfarlane GT, Macfarlane S, Gibson GR (1998) Validation of a three-stage compound continuous culture system for investigating the effect of retention time on the ecology and metabolism of bacteria in the human colon. Microb Ecol 35(2):180-187 (Pubitemid 28190244)
    • (1998) Microbial Ecology , vol.35 , Issue.2 , pp. 180-187
    • Macfarlane, G.T.1    Macfarlane, S.2    Gibson, G.R.3
  • 26
    • 67649939005 scopus 로고    scopus 로고
    • Emulsification alters simulated gastrointestinal proteolysis of beta-casein and beta-lactoglobulin
    • 1:CAS:528:DC%2BD1MXht1yjtL8%3D 10.1039/b811233a
    • Macierzanka A, Sancho AI, Mills ENC, Rigby NM, Mackie AR (2009) Emulsification alters simulated gastrointestinal proteolysis of beta-casein and beta-lactoglobulin. Soft Matter 5(3):538-550
    • (2009) Soft Matter , vol.5 , Issue.3 , pp. 538-550
    • MacIerzanka, A.1    Sancho, A.I.2    Mills, E.N.C.3    Rigby, N.M.4    MacKie, A.R.5
  • 28
    • 67649909210 scopus 로고    scopus 로고
    • Physiological phosphatidylcholine protects bovine beta-lactoglobulin from simulated gastrointestinal proteolysis
    • 10.1002/mnfr.200800321
    • Mandalari G, Mackie AM, Rigby NM, Wickham MSJ, Mills ENC (2009) Physiological phosphatidylcholine protects bovine beta-lactoglobulin from simulated gastrointestinal proteolysis. Mol Nutr Food Res 53:S131-S139
    • (2009) Mol Nutr Food Res , vol.53
    • Mandalari, G.1    MacKie, A.M.2    Rigby, N.M.3    Wickham, M.S.J.4    Mills, E.N.C.5
  • 29
    • 29744451337 scopus 로고    scopus 로고
    • Phospholipid interactions protect the milk allergen α-lactalbumin from proteolysis during in vitro digestion
    • DOI 10.1021/jf0515227
    • Moreno FJ, Mackie AR, Mills ENC (2005) Phospholipid interactions protect the milk allergen alpha-lactalbumin from proteolysis during in vitro digestion. J Agric Food Chem 53(25):9810-9816 (Pubitemid 43027191)
    • (2005) Journal of Agricultural and Food Chemistry , vol.53 , Issue.25 , pp. 9810-9816
    • Moreno, F.J.1    Mackie, A.R.2    Mills, E.N.C.3
  • 30
    • 77951566643 scopus 로고    scopus 로고
    • Reduction of the immunogenicity of beta-lactoglobulin from cow's milk by conjugation with a dextran derivative
    • 1:CAS:528:DC%2BC3cXnt1Kqsrg%3D 10.1271/bbb.90767
    • Nodake Y, Fukumoto S, Fukasawa M, Sakakibara R, Yamasaki N (2010) Reduction of the immunogenicity of beta-lactoglobulin from cow's milk by conjugation with a dextran derivative. Biosci Biotechnol Biochem 74(4):721-726
    • (2010) Biosci Biotechnol Biochem , vol.74 , Issue.4 , pp. 721-726
    • Nodake, Y.1    Fukumoto, S.2    Fukasawa, M.3    Sakakibara, R.4    Yamasaki, N.5
  • 31
    • 33646377677 scopus 로고    scopus 로고
    • Creating proteins with novel functionality via the Maillard reaction: A review
    • 1:CAS:528:DC%2BD28XjsFanu78%3D 10.1080/10408690590957250
    • Oliver CM, Melton LD, Stanley RA (2006) Creating proteins with novel functionality via the Maillard reaction: a review. Crit Rev Food Sci Nutr 46(4):337-350
    • (2006) Crit Rev Food Sci Nutr , vol.46 , Issue.4 , pp. 337-350
    • Oliver, C.M.1    Melton, L.D.2    Stanley, R.A.3
  • 32
    • 58149494410 scopus 로고    scopus 로고
    • Structural analysis and properties of dextran produced by Leuconostoc mesenteroides NRRL B-640
    • 1:CAS:528:DC%2BD1MXpsVamsw%3D%3D 10.1016/j.carbpol.2008.09.018
    • Purama RK, Goswami P, Khan AT, Goyal A (2009) Structural analysis and properties of dextran produced by Leuconostoc mesenteroides NRRL B-640. Carbohydr Polym 76(1):30-35
    • (2009) Carbohydr Polym , vol.76 , Issue.1 , pp. 30-35
    • Purama, R.K.1    Goswami, P.2    Khan, A.T.3    Goyal, A.4
  • 33
    • 0028863589 scopus 로고
    • Dextran hydrogels for colon-specific drug delivery.5. Degradation in human intestinal incubation models
    • 1:CAS:528:DyaK2MXpvVyqtbg%3D 10.1016/0928-0987(95)00023-6
    • Simonsen L, Hovgaard L, Mortensen PB, Brondsted H (1995) Dextran hydrogels for colon-specific drug delivery.5. Degradation in human intestinal incubation models. Eur J Pharm Sci 3(6):329-337
    • (1995) Eur J Pharm Sci , vol.3 , Issue.6 , pp. 329-337
    • Simonsen, L.1    Hovgaard, L.2    Mortensen, P.B.3    Brondsted, H.4
  • 34
    • 84859944275 scopus 로고    scopus 로고
    • Dextran conjugates in drug delivery
    • 1:CAS:528:DC%2BC38XlvVGrtLs%3D 10.1517/17425247.2012.673580
    • Varshosaz J (2012) Dextran conjugates in drug delivery. Expert Opin Drug Deliv 9(5):509-523
    • (2012) Expert Opin Drug Deliv , vol.9 , Issue.5 , pp. 509-523
    • Varshosaz, J.1
  • 36
    • 84861330638 scopus 로고    scopus 로고
    • Effect of Maillard-induced glycosylation on the nutritional quality, solubility, thermal stability and molecular configuration of whey protein
    • 10.1016/j.idairyj.2012.02.009
    • Wang Q, Ismail B (2012) Effect of Maillard-induced glycosylation on the nutritional quality, solubility, thermal stability and molecular configuration of whey protein. Int Dairy J 25(2):112-122
    • (2012) Int Dairy J , vol.25 , Issue.2 , pp. 112-122
    • Wang, Q.1    Ismail, B.2
  • 37
    • 79954511312 scopus 로고    scopus 로고
    • Oral tolerance
    • 1:CAS:528:DC%2BC3MXlsFOjsLg%3D 10.1111/j.1600-065X.2011.01017.x
    • Weiner HL, da Cunha AP, Quintana F, Wu H (2011) Oral tolerance. Immunol Rev 241(1):241-259
    • (2011) Immunol Rev , vol.241 , Issue.1 , pp. 241-259
    • Weiner, H.L.1    Da Cunha, A.P.2    Quintana, F.3    Wu, H.4
  • 38
    • 51649086473 scopus 로고    scopus 로고
    • Formation of whey protein isolate (WPI)-dextran conjugates in aqueous solutions
    • 1:CAS:528:DC%2BD1cXptVagt7k%3D 10.1021/jf800909w
    • Zhu D, Damodaran S, Lucey JA (2008) Formation of whey protein isolate (WPI)-dextran conjugates in aqueous solutions. J Agric Food Chem 56(16):7113-7118
    • (2008) J Agric Food Chem , vol.56 , Issue.16 , pp. 7113-7118
    • Zhu, D.1    Damodaran, S.2    Lucey, J.A.3
  • 39
    • 77949404014 scopus 로고    scopus 로고
    • Physicochemical and emulsifying properties of whey protein isolate (WPI)-dextran conjugates produced in aqueous solution
    • 1:CAS:528:DC%2BC3cXhslSgtLc%3D 10.1021/jf903643p
    • Zhu D, Damodaran S, Lucey JA (2010) Physicochemical and emulsifying properties of whey protein isolate (WPI)-dextran conjugates produced in aqueous solution. J Agric Food Chem 58(5):2988-2994
    • (2010) J Agric Food Chem , vol.58 , Issue.5 , pp. 2988-2994
    • Zhu, D.1    Damodaran, S.2    Lucey, J.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.