메뉴 건너뛰기




Volumn 58, Issue 8, 2010, Pages 4894-4900

Effect of neutrase, alcalase, and papain hydrolysis of whey protein concentrates on iron uptake by Caco-2 cells

Author keywords

Caco 2 cells; Enzymatic hydrolysates; In vitro digestion; Iron absorption

Indexed keywords

IRON; METALLOPROTEINASE; MICROBIAL METALLOPROTEINASES; PAPAIN; SUBTILISIN;

EID: 77951283238     PISSN: 00218561     EISSN: 15205118     Source Type: Journal    
DOI: 10.1021/jf100055y     Document Type: Article
Times cited : (49)

References (31)
  • 1
    • 62249186740 scopus 로고    scopus 로고
    • Effect of soaking and phytase treatment on phytic acid, calcium, iron and zinc in rice fractions
    • Liang, J.; Han, B.; Nout, M. J. R.; Hamer, R. J. Effect of soaking and phytase treatment on phytic acid, calcium, iron and zinc in rice fractions Food Chem. 2009, 115, 789-794
    • (2009) Food Chem. , vol.115 , pp. 789-794
    • Liang, J.1    Han, B.2    Nout, M.J.R.3    Hamer, R.J.4
  • 2
    • 43449106183 scopus 로고    scopus 로고
    • Effects of soaking, germination and fermentation on phytic acid, total and in vitro soluble zinc in brown rice
    • Liang, J.; Han, B.; Nout, M. J. R.; Hamer, R. J. Effects of soaking, germination and fermentation on phytic acid, total and in vitro soluble zinc in brown rice Food Chem. 2008, 110, 821-828
    • (2008) Food Chem. , vol.110 , pp. 821-828
    • Liang, J.1    Han, B.2    Nout, M.J.R.3    Hamer, R.J.4
  • 3
    • 77951280680 scopus 로고    scopus 로고
    • Attention on iron fortification-the application of NaFeEDTA in food
    • (in Chinese)
    • Yu, B. Attention on iron fortification-the application of NaFeEDTA in food. Sci. Technol. Food Ind. 2007, 4) 34-35 (in Chinese).
    • (2007) Sci. Technol. Food Ind. , Issue.4 , pp. 34-35
    • Yu, B.1
  • 4
    • 34547829763 scopus 로고    scopus 로고
    • Egg yolk protein and egg yolk phosvitin inhibit calcium, magnesium, and iron absorptions in rats
    • Ishikawa, S. I.; Tamaki, S.; Arihara, K.; Itoh, M. Egg yolk protein and egg yolk phosvitin inhibit calcium, magnesium, and iron absorptions in rats J. Food Sci. 2007, 72, S412-S419
    • (2007) J. Food Sci. , vol.72
    • Ishikawa, S.I.1    Tamaki, S.2    Arihara, K.3    Itoh, M.4
  • 5
    • 0347986910 scopus 로고    scopus 로고
    • A low-molecular-weight factor in human milk whey promotes iron uptake by Caco-2 cells
    • Etcheverry, P.; Miller, D. D.; Glahn, R. P. A low-molecular-weight factor in human milk whey promotes iron uptake by Caco-2 cells J. Nutr. 2004, 134, 93-98
    • (2004) J. Nutr. , vol.134 , pp. 93-98
    • Etcheverry, P.1    Miller, D.D.2    Glahn, R.P.3
  • 6
    • 0030747580 scopus 로고    scopus 로고
    • Interaction of iron with other nutrients
    • Lynch, S. R. Interaction of iron with other nutrients Nutr. Rev. 1997, 55, 102-110
    • (1997) Nutr. Rev. , vol.55 , pp. 102-110
    • Lynch, S.R.1
  • 8
    • 59649116856 scopus 로고    scopus 로고
    • Characterisation of binding of iron to sodium caseinate and whey protein isolate
    • Sugiarto, M.; Ye, A.; Singh, H. Characterisation of binding of iron to sodium caseinate and whey protein isolate Food Chem. 2009, 114, 1007-1013
    • (2009) Food Chem. , vol.114 , pp. 1007-1013
    • Sugiarto, M.1    Ye, A.2    Singh, H.3
  • 9
    • 11144238232 scopus 로고    scopus 로고
    • Iron availability from whey protein hydrogels: An in vitro study
    • Remondetto, G. E.; Beyssac, E.; Subirade, M. Iron availability from whey protein hydrogels: an in vitro study J. Agric. Food Chem. 2004, 52, 8137-8143
    • (2004) J. Agric. Food Chem. , vol.52 , pp. 8137-8143
    • Remondetto, G.E.1    Beyssac, E.2    Subirade, M.3
  • 10
    • 33847007267 scopus 로고    scopus 로고
    • Iron-binding properties, amino acid composition, and structure of muscle tissue peptides from in vitro digestion of different meat sources
    • Storcksdieck genannt Bonsmann, S.; Hurrell, R. F. Iron-binding properties, amino acid composition, and structure of muscle tissue peptides from in vitro digestion of different meat sources J. Food Sci. 2007, 72, S019-S029
    • (2007) J. Food Sci. , vol.72
    • Storcksdieck Genannt Bonsmann, S.1    Hurrell, R.F.2
  • 11
    • 0028856041 scopus 로고
    • Iron absorption and intestinal solubility in rats are influenced by dietary proteins
    • Kim, M.; Lee, D. T.; Lee, Y. S. Iron absorption and intestinal solubility in rats are influenced by dietary proteins Nutr. Res. (N.Y.) 1995, 15, 1705-1716
    • (1995) Nutr. Res. (N.Y.) , vol.15 , pp. 1705-1716
    • Kim, M.1    Lee, D.T.2    Lee, Y.S.3
  • 12
    • 0031954579 scopus 로고    scopus 로고
    • Influence of the sulphydryl content of animal proteins on in vitro bioavailability of non-haem iron
    • DOI 10.1016/S0308-8146(97)00127-1, PII S0308814697001271
    • Mulvihill, B.; Morrissey, P. A. Influence of the sulphydryl content of animal proteins on in vitro bioavailability of non-haem iron Food Chem. 1998, 61, 1-7 (Pubitemid 28152149)
    • (1998) Food Chemistry , vol.61 , Issue.1-2 , pp. 1-7
    • Mulvihill, B.1    Morrissey, P.A.2
  • 13
    • 33847028271 scopus 로고    scopus 로고
    • Separation of iron-binding protein from whey through enzymatic hydrolysis
    • Kim, S. B.; Seo, I. S.; Khan, M. A.; Ki, K. S.; Nam, M. S.; Kim, H. S. Separation of iron-binding protein from whey through enzymatic hydrolysis Int. Dairy J. 2007, 17, 625-631
    • (2007) Int. Dairy J. , vol.17 , pp. 625-631
    • Kim, S.B.1    Seo, I.S.2    Khan, M.A.3    Ki, K.S.4    Nam, M.S.5    Kim, H.S.6
  • 14
    • 58249140350 scopus 로고    scopus 로고
    • Purification of an iron-binding nona-peptide from hydrolysates of porcine blood plasma protein
    • Lee, S. H.; Song, K. B. Purification of an iron-binding nona-peptide from hydrolysates of porcine blood plasma protein Process Biochem. 2009, 44, 378-381
    • (2009) Process Biochem. , vol.44 , pp. 378-381
    • Lee, S.H.1    Song, K.B.2
  • 15
    • 34848867314 scopus 로고    scopus 로고
    • Enzymatic hydrolysis of heated whey: Iron-binding ability of peptides and antigenic protein fractions
    • Kim, S. B.; Seo, I. S.; Khan, M. A.; Ki, K. S.; Lee, W. S.; Lee, H. J.; Shin, H. S.; Kim, H. S. Enzymatic hydrolysis of heated whey: Iron-binding ability of peptides and antigenic protein fractions J. Dairy Sci. 2007, 90, 4033-4042
    • (2007) J. Dairy Sci. , vol.90 , pp. 4033-4042
    • Kim, S.B.1    Seo, I.S.2    Khan, M.A.3    Ki, K.S.4    Lee, W.S.5    Lee, H.J.6    Shin, H.S.7    Kim, H.S.8
  • 16
    • 44549084148 scopus 로고    scopus 로고
    • Whey and whey proteins-from 'gutter-to-gold'
    • Smithers, G. W. Whey and whey proteins-from 'gutter-to-gold' Int. Dairy J. 2008, 18, 695-704
    • (2008) Int. Dairy J. , vol.18 , pp. 695-704
    • Smithers, G.W.1
  • 17
    • 0018536145 scopus 로고
    • Determination of the degree of hydrolysis of food protein hydrolysates by trinitrobenzenesulfonic acid
    • Adler-Nissen, J. Determination of the degree of hydrolysis of food protein hydrolysates by trinitrobenzenesulfonic acid J. Agric. Food Chem. 1979, 27, 1256-1262
    • (1979) J. Agric. Food Chem. , vol.27 , pp. 1256-1262
    • Adler-Nissen, J.1
  • 19
    • 0031658047 scopus 로고    scopus 로고
    • Caco-2 cell ferritin formation predicts nonradiolabeled food iron availability in an in vitro digestion/Caco-2 cell culture model
    • Glahn, R. P.; Lee, O. A.; Yeung, A.; Goldman, M. I.; Miller, D. D. Caco-2 cell ferritin formation predicts nonradiolabeled food iron availability in an in vitro digestion/Caco-2 cell culture model J. Nutr. 1998, 128, 1555-1561
    • (1998) J. Nutr. , vol.128 , pp. 1555-1561
    • Glahn, R.P.1    Lee, O.A.2    Yeung, A.3    Goldman, M.I.4    Miller, D.D.5
  • 20
    • 0029027292 scopus 로고
    • Bathophenanthrolene disulfonic acid and sodium dithionite effectively remove surface-bound iron from Caco-2 cell monolayers
    • Glahn, R. P.; Gangloff, M. B.; van Campen, D. R.; Miller, D. D.; Wien, E. M.; Norvell, W. A. Bathophenanthrolene disulfonic acid and sodium dithionite effectively remove surface-bound iron from Caco-2 cell monolayers J. Nutr. 1995, 125, 1833-1840
    • (1995) J. Nutr. , vol.125 , pp. 1833-1840
    • Glahn, R.P.1    Gangloff, M.B.2    Van Campen, D.R.3    Miller, D.D.4    Wien, E.M.5    Norvell, W.A.6
  • 21
    • 33747708760 scopus 로고    scopus 로고
    • Effect of retinol on iron bioavailability from Iranian bread in a Caco-2 cell culture model
    • Gargari, B. P.; Razavieh, S. V.; Mahboob, S.; Niknafs, B.; Kooshavar, H. Effect of retinol on iron bioavailability from Iranian bread in a Caco-2 cell culture model Nutrition 2006, 22, 638-644
    • (2006) Nutrition , vol.22 , pp. 638-644
    • Gargari, B.P.1    Razavieh, S.V.2    Mahboob, S.3    Niknafs, B.4    Kooshavar, H.5
  • 22
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schagger, H.; Von Jagow, G. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa Anal. Biochem. 1987, 166, 368-379
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schagger, H.1    Von Jagow, G.2
  • 23
    • 0028856041 scopus 로고
    • Iron absorption and intestinal solubility in rats are influenced by dietary proteins
    • Kim, M.; Lee, D. T.; Lee, Y. S. Iron absorption and intestinal solubility in rats are influenced by dietary proteins Nutr. Res. (N.Y.) 1995, 15, 1705-1716
    • (1995) Nutr. Res. (N.Y.) , vol.15 , pp. 1705-1716
    • Kim, M.1    Lee, D.T.2    Lee, Y.S.3
  • 25
    • 33846644075 scopus 로고    scopus 로고
    • Availability of iron from milk-based formulas and fruit juices containing milk and cereals estimated by in vitro methods (solubility, dialysability) and uptake and transport by Caco-2 cells
    • Perales, S.; Barber, R.; Lagarda, M. J.; Farr, R. Availability of iron from milk-based formulas and fruit juices containing milk and cereals estimated by in vitro methods (solubility, dialysability) and uptake and transport by Caco-2 cells Food Chem. 2007, 102, 1296-1303
    • (2007) Food Chem. , vol.102 , pp. 1296-1303
    • Perales, S.1    Barber, R.2    Lagarda, M.J.3    Farr, R.4
  • 26
    • 33847028271 scopus 로고    scopus 로고
    • Separation of iron-binding protein from whey through enzymatic hydrolysis
    • Kim, S. B.; Seo, I. S.; Khan, M. A.; Ki, K. S.; Nam, M. S.; Kim, H. S. Separation of iron-binding protein from whey through enzymatic hydrolysis Int. Dairy J. 2007, 17, 625-631
    • (2007) Int. Dairy J. , vol.17 , pp. 625-631
    • Kim, S.B.1    Seo, I.S.2    Khan, M.A.3    Ki, K.S.4    Nam, M.S.5    Kim, H.S.6
  • 27
    • 84974224136 scopus 로고
    • Application to the plastein reaction to casein and skim-milk powder
    • Sukan, G.; Andrews, A. T. Application to the plastein reaction to casein and skim-milk powder J. Dairy Res 1982, 49, 265-78
    • (1982) J. Dairy Res , vol.49 , pp. 265-78
    • Sukan, G.1    Andrews, A.T.2
  • 28
    • 0037070051 scopus 로고    scopus 로고
    • Iron derivatives from casein hydrolysates as a potential source in the treatment of iron deficiency
    • Chaud, M. V.; Izumi, C.; Nahaal, Z.; Shuhama, T.; Bianchi, M.; Freitas, O. Iron derivatives from casein hydrolysates as a potential source in the treatment of iron deficiency J. Agric. Food Chem. 2002, 50, 871-877
    • (2002) J. Agric. Food Chem. , vol.50 , pp. 871-877
    • Chaud, M.V.1    Izumi, C.2    Nahaal, Z.3    Shuhama, T.4    Bianchi, M.5    Freitas, O.6
  • 29
    • 38049008013 scopus 로고    scopus 로고
    • Peptides isolated from in vitro digests of milk enhance iron uptake by Caco-2 cells
    • Argyri, K.; Miller, D. D.; Glahn, R. P.; Zhu, L.; Kapsokefalou, M. Peptides isolated from in vitro digests of milk enhance iron uptake by Caco-2 cells J. Agric. Food Chem. 2007, 55, 10221-10225
    • (2007) J. Agric. Food Chem. , vol.55 , pp. 10221-10225
    • Argyri, K.1    Miller, D.D.2    Glahn, R.P.3    Zhu, L.4    Kapsokefalou, M.5
  • 31
    • 0027439867 scopus 로고
    • Proline-dependent structural and biological properties of peptides and proteins
    • Yaron, A.; Naider, F.; Scharpe, S. Proline-dependent structural and biological properties of peptides and proteins Crit. Rev. Biochem. Mol. Biol. 1993, 28, 31-81
    • (1993) Crit. Rev. Biochem. Mol. Biol. , vol.28 , pp. 31-81
    • Yaron, A.1    Naider, F.2    Scharpe, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.