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Volumn 54, Issue 4, 2006, Pages 1508-1517

Heat markers and quality indexes of industrially heat-treated [ 15N] milk protein measured in rats

Author keywords

Heat treatments; In vivo assay; Milk protein; Protein quality; Rat

Indexed keywords

DIAGNOSTIC AGENT; MILK PROTEIN; NITROGEN;

EID: 33644865646     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf051304d     Document Type: Article
Times cited : (37)

References (49)
  • 1
    • 0141720797 scopus 로고    scopus 로고
    • Lysinoalanine content of formulas for enteral nutrition
    • Boschin, G.; D'Agostina, A.; Rinaldi, A.; Arnoldi, A. Lysinoalanine content of formulas for enteral nutrition. J. Dairy Sci. 2003, 86 (7), 2283-2287.
    • (2003) J. Dairy Sci. , vol.86 , Issue.7 , pp. 2283-2287
    • Boschin, G.1    D'Agostina, A.2    Rinaldi, A.3    Arnoldi, A.4
  • 2
    • 0028883289 scopus 로고
    • Protein quality of enteral nutrition products is consistent with label claims during shelf life and beyond expiration date
    • Henningfield, M. F.; Smith, S. D.; Reynolds, P. A.; Garcia, S. E.; Baxter, J. H. Protein quality of enteral nutrition products is consistent with label claims during shelf life and beyond expiration date. J. Am. Diet. Assoc. 1995, 95 (1), 46-52.
    • (1995) J. Am. Diet. Assoc. , vol.95 , Issue.1 , pp. 46-52
    • Henningfield, M.F.1    Smith, S.D.2    Reynolds, P.A.3    Garcia, S.E.4    Baxter, J.H.5
  • 3
    • 0026196991 scopus 로고
    • Effect of processing on some chemical and nutritional characteristics of pre-cooked and dehydrated legumes
    • Estevez, A. M.; Castillo, E.; Figuerola, F.; Yanez, E. Effect of processing on some chemical and nutritional characteristics of pre-cooked and dehydrated legumes. Plant Foods Hum. Nutr. 1991, 41 (3), 193-201.
    • (1991) Plant Foods Hum. Nutr. , vol.41 , Issue.3 , pp. 193-201
    • Estevez, A.M.1    Castillo, E.2    Figuerola, F.3    Yanez, E.4
  • 4
    • 0034833829 scopus 로고    scopus 로고
    • Nutritional and health benefits of soy proteins
    • Friedman, M.; Brandon, D. L. Nutritional and health benefits of soy proteins. J. Agric. Food Chem. 2001, 49 (3), 1069-1086.
    • (2001) J. Agric. Food Chem. , vol.49 , Issue.3 , pp. 1069-1086
    • Friedman, M.1    Brandon, D.L.2
  • 5
    • 17644431514 scopus 로고    scopus 로고
    • Nutritional value of the proteins of soybeans roasted at a small-scale unit level in Africa as assessed using growing rats
    • Ouedraogo, C. L.; Combe, E.; Lalles, J. P.; Toullec, R.; Treche, S.; Grongnet, J. F. Nutritional value of the proteins of soybeans roasted at a small-scale unit level in Africa as assessed using growing rats. Reprod. Nutr. Dev. 1999, 39 (2), 201-212.
    • (1999) Reprod. Nutr. Dev. , vol.39 , Issue.2 , pp. 201-212
    • Ouedraogo, C.L.1    Combe, E.2    Lalles, J.P.3    Toullec, R.4    Treche, S.5    Grongnet, J.F.6
  • 6
    • 0032965144 scopus 로고    scopus 로고
    • Chemistry, biochemistry, nutrition, and microbiology of lysinoalanine, lanthionine, and histidinoalanine in food and other proteins
    • Friedman, M. Chemistry, biochemistry, nutrition, and microbiology of lysinoalanine, lanthionine, and histidinoalanine in food and other proteins. J. Agric. Food Chem. 1999, 47 (4), 1295-1319.
    • (1999) J. Agric. Food Chem. , vol.47 , Issue.4 , pp. 1295-1319
    • Friedman, M.1
  • 7
    • 0041885362 scopus 로고    scopus 로고
    • Thermal modifications of structure and co-denaturation of alpha-lactalbumin and beta-lactoglobulin induce changes of solubility and susceptibility to proteases
    • Bertrand-Harb, C.; Baday, A.; Dalgalarrondo, M.; Chobert, J. M.; Haertle, T. Thermal modifications of structure and co-denaturation of alpha-lactalbumin and beta-lactoglobulin induce changes of solubility and susceptibility to proteases. Nahrung 2002, 46 (4), 283-289.
    • (2002) Nahrung , vol.46 , Issue.4 , pp. 283-289
    • Bertrand-Harb, C.1    Baday, A.2    Dalgalarrondo, M.3    Chobert, J.M.4    Haertle, T.5
  • 8
    • 0021161497 scopus 로고
    • Protein-alkali reactions: Chemistry, toxicology, and nutritional consequences
    • Friedman, M.; Gumbmann, M. R.; Masters, P. M. Protein-alkali reactions: Chemistry, toxicology, and nutritional consequences. Adv. Exp. Med. Biol. 1984, 177, 367-412.
    • (1984) Adv. Exp. Med. Biol. , vol.177 , pp. 367-412
    • Friedman, M.1    Gumbmann, M.R.2    Masters, P.M.3
  • 9
    • 0036209392 scopus 로고    scopus 로고
    • Effect of heat-treated proteins on selected parameters of the biotransformation system in the rat
    • Wenzel, E.; Tasto, S.; Erbersdobler, H. F.; Faist, V. Effect of heat-treated proteins on selected parameters of the biotransformation system in the rat. Ann. Nutr. Metab. 2002, 46 (1), 9-16.
    • (2002) Ann. Nutr. Metab. , vol.46 , Issue.1 , pp. 9-16
    • Wenzel, E.1    Tasto, S.2    Erbersdobler, H.F.3    Faist, V.4
  • 10
    • 0001219012 scopus 로고
    • Denaturation and aggregation of serum proteins and caseins in heated milk
    • Dalgleish, D. G. Denaturation and aggregation of serum proteins and caseins in heated milk. J. Agric. Food Chem. 1990, 38 (11), 1995-1999.
    • (1990) J. Agric. Food Chem. , vol.38 , Issue.11 , pp. 1995-1999
    • Dalgleish, D.G.1
  • 11
    • 0034824293 scopus 로고    scopus 로고
    • Changes in protein nutritional quality in fresh and recombined ultrahigh-temperature treated milk during storage
    • al Kanhal, H. A.; al-Othman, A. A.; Hewedi, F. M. Changes in protein nutritional quality in fresh and recombined ultrahigh-temperature treated milk during storage. Int. J. Food Sci. Nutr. 2001, 52 (6), 509-514.
    • (2001) Int. J. Food Sci. Nutr. , vol.52 , Issue.6 , pp. 509-514
    • Al Kanhal, H.A.1    Al-Othman, A.A.2    Hewedi, F.M.3
  • 12
    • 0030890025 scopus 로고    scopus 로고
    • Available lysine in dried milk after processing
    • El, S. N.; Kavas, A. Available lysine in dried milk after processing. Int. J. Food Sci. Nutr. 1997, 48 (2), 109-111.
    • (1997) Int. J. Food Sci. Nutr. , vol.48 , Issue.2 , pp. 109-111
    • El, S.N.1    Kavas, A.2
  • 13
    • 0037228809 scopus 로고    scopus 로고
    • Protein digestibility and quality in products containing antinutritional factors are adversely affected by old age in rats
    • Gilani, G. S.; Sepehr, E. Protein digestibility and quality in products containing antinutritional factors are adversely affected by old age in rats. J. Nutr. 2003, 133 (1), 220-225.
    • (2003) J. Nutr. , vol.133 , Issue.1 , pp. 220-225
    • Gilani, G.S.1    Sepehr, E.2
  • 14
    • 0037386648 scopus 로고    scopus 로고
    • Updating on the lysinoalanine content of commercial infant formulae and beicost products
    • D'Agostina, A.; Boschin, G.; Rinaldi, A.; Arnoldi, A. Updating on the lysinoalanine content of commercial infant formulae and beicost products. Food Chem. 2003, 80, 483-488.
    • (2003) Food Chem. , vol.80 , pp. 483-488
    • D'Agostina, A.1    Boschin, G.2    Rinaldi, A.3    Arnoldi, A.4
  • 15
    • 0040285405 scopus 로고    scopus 로고
    • Application of a new method for determining digestible reactive lysine to variably heated protein sources
    • Rutherfurd, S. M.; Moughan, P. J. Application of a new method for determining digestible reactive lysine to variably heated protein sources. J. Agric. Food Chem. 1997, 45 (5), 1582-1586.
    • (1997) J. Agric. Food Chem. , vol.45 , Issue.5 , pp. 1582-1586
    • Rutherfurd, S.M.1    Moughan, P.J.2
  • 17
    • 0033858993 scopus 로고    scopus 로고
    • A high-protein meal exceeds anabolic and catabolic capacities in rats adapted to a normal protein diet
    • Morens, C.; Gaudichon, C.; Metges, C. C.; Fromentin, G.; Baglieri, A.; Even, P. C.; Huneau, J. F.; Tome, D. A high-protein meal exceeds anabolic and catabolic capacities in rats adapted to a normal protein diet. J. Nutr. 2000, 130 (9), 2312-2321.
    • (2000) J. Nutr. , vol.130 , Issue.9 , pp. 2312-2321
    • Morens, C.1    Gaudichon, C.2    Metges, C.C.3    Fromentin, G.4    Baglieri, A.5    Even, P.C.6    Huneau, J.F.7    Tome, D.8
  • 19
    • 0038671678 scopus 로고    scopus 로고
    • Postprandial kinetics of dietary amino acids are the main determinant of their metabolism after soy or milk protein ingestion in humans
    • Bos, C.; Metges, C. C.; Gaudichon, C.; Petzke, K. J.; Pueyo, M. E.; Morens, C.; Everwand, J.; Benamouzig, R.; Tome, D. Postprandial kinetics of dietary amino acids are the main determinant of their metabolism after soy or milk protein ingestion in humans. J. Nutr. 2003, 133 (5), 1308-1315.
    • (2003) J. Nutr. , vol.133 , Issue.5 , pp. 1308-1315
    • Bos, C.1    Metges, C.C.2    Gaudichon, C.3    Petzke, K.J.4    Pueyo, M.E.5    Morens, C.6    Everwand, J.7    Benamouzig, R.8    Tome, D.9
  • 20
    • 0030912476 scopus 로고    scopus 로고
    • Components of the AIN-93 diets as improvements in the AIN-76A diet
    • Reeves, P. G. Components of the AIN-93 diets as improvements in the AIN-76A diet. J. Nutr. 1997, 127 (5 Suppl.), 838S-841S.
    • (1997) J. Nutr. , vol.127 , Issue.5 SUPPL.
    • Reeves, P.G.1
  • 23
    • 0010581394 scopus 로고
    • Automatic recording apparatus for use in the chromatography of amino acids
    • Spackman, D. H.; Stein, W. H.; Moore, S. Automatic recording apparatus for use in the chromatography of amino acids. Anal. Chem. 1958, 30, 1190-1206.
    • (1958) Anal. Chem. , vol.30 , pp. 1190-1206
    • Spackman, D.H.1    Stein, W.H.2    Moore, S.3
  • 24
    • 0031253029 scopus 로고    scopus 로고
    • Characterization by ionization mass spectrometry of lactosyl beta-lactoglobulin conjugates formed during heat treatment of milk and whey and identification of one lactose-binding site
    • Leonil, J.; Molle, D.; Fauquant, J.; Maubois, J. L.; Pearce, R. J.; Bouhallab, S. Characterization by ionization mass spectrometry of lactosyl beta-lactoglobulin conjugates formed during heat treatment of milk and whey and identification of one lactose-binding site. J. Dairy Sci. 1997, 80 (10), 2270-2281.
    • (1997) J. Dairy Sci. , vol.80 , Issue.10 , pp. 2270-2281
    • Leonil, J.1    Molle, D.2    Fauquant, J.3    Maubois, J.L.4    Pearce, R.J.5    Bouhallab, S.6
  • 26
    • 0030610423 scopus 로고    scopus 로고
    • [15N]-labeled pea flour protein nitrogen exhibits good ileal digestibility and postprandial retention in humans
    • Gausseres, N.; Mahe, S.; Benamouzig, R.; Luengo, C.; Ferriere, F.; Rautureau, J.; Tome, D. [15N]-labeled pea flour protein nitrogen exhibits good ileal digestibility and postprandial retention in humans. J. Nutr. 1997, 127 (6), 1160-1165.
    • (1997) J. Nutr. , vol.127 , Issue.6 , pp. 1160-1165
    • Gausseres, N.1    Mahe, S.2    Benamouzig, R.3    Luengo, C.4    Ferriere, F.5    Rautureau, J.6    Tome, D.7
  • 29
    • 0000724306 scopus 로고
    • Estimation of lysine damage in heated whey proteins by furosine determinations in conjonction with the digestion cell technique
    • Desrosiers, T.; Savoie, L.; Bergeron, G.; Parent, G. Estimation of lysine damage in heated whey proteins by furosine determinations in conjonction with the digestion cell technique. J. Agric. Food Chem. 1989, 37 (5), 1385-1391.
    • (1989) J. Agric. Food Chem. , vol.37 , Issue.5 , pp. 1385-1391
    • Desrosiers, T.1    Savoie, L.2    Bergeron, G.3    Parent, G.4
  • 30
    • 84982339095 scopus 로고
    • Effect of heat treatment on the nutritive value of proteins: Chemical and balance studies
    • Donoso, G.; Lewis, O. A. M.; Miller, D. S.; Payne, P. R. Effect of heat treatment on the nutritive value of proteins: Chemical and balance studies. J. Sci. Food Agric. 1962, 13, 192-197.
    • (1962) J. Sci. Food Agric. , vol.13 , pp. 192-197
    • Donoso, G.1    Lewis, O.A.M.2    Miller, D.S.3    Payne, P.R.4
  • 31
    • 0020998272 scopus 로고
    • Food processing and storage as a determinant of protein and amino acid availability
    • Hurrell, R. F.; Finot, P. A. Food processing and storage as a determinant of protein and amino acid availability. Exp. Suppl. 1983, 44, 135-156.
    • (1983) Exp. Suppl. , vol.44 , pp. 135-156
    • Hurrell, R.F.1    Finot, P.A.2
  • 32
    • 0036943526 scopus 로고    scopus 로고
    • Nutritional and metabolic consequences of the early Maillard reaction of heat treated milk in the pig. Significance for man
    • Rerat, A.; Calmes, R.; Vaissade, P.; Finot, P. A. Nutritional and metabolic consequences of the early Maillard reaction of heat treated milk in the pig. Significance for man. Eur. J. Nutr. 2002, 41 (1), 1-11.
    • (2002) Eur. J. Nutr. , vol.41 , Issue.1 , pp. 1-11
    • Rerat, A.1    Calmes, R.2    Vaissade, P.3    Finot, P.A.4
  • 33
    • 0032941281 scopus 로고    scopus 로고
    • Formation of stable covalent dimer explains the high solubility at pH 4.6 of lactose-β-lactoglobulin conjugates heated near neutral pH
    • Bouhallab, S.; Morgan, F.; Henry, G.; Molle, D.; Leonil, J. Formation of stable covalent dimer explains the high solubility at pH 4.6 of lactose-β-lactoglobulin conjugates heated near neutral pH. J. Agric. Food Chem. 1999, 47 (4), 1489-1494.
    • (1999) J. Agric. Food Chem. , vol.47 , Issue.4 , pp. 1489-1494
    • Bouhallab, S.1    Morgan, F.2    Henry, G.3    Molle, D.4    Leonil, J.5
  • 34
    • 0033931268 scopus 로고    scopus 로고
    • Protein-bound D-amino acids, and to a lesser extent lysinoalanine, decrease true ileal protein digestibility in minipigs as determined with (15)N-labeling
    • de Vrese, M.; Frik, R.; Roos, N.; Hagemeister, H. Protein-bound D-amino acids, and to a lesser extent lysinoalanine, decrease true ileal protein digestibility in minipigs as determined with (15)N-labeling. J. Nutr. 2000, 130 (8), 2026-2031.
    • (2000) J. Nutr. , vol.130 , Issue.8 , pp. 2026-2031
    • De Vrese, M.1    Frik, R.2    Roos, N.3    Hagemeister, H.4
  • 35
    • 0345434987 scopus 로고    scopus 로고
    • Type of milk consumed can influence plasma concentrations of fatty acids and minerals and body composition in infant and weanling pigs
    • Murry, A. C., Jr.; Gelaye, S.; Casey, J. M.; Foutz, T. L.; Kouakou, B.; Arora, D. Type of milk consumed can influence plasma concentrations of fatty acids and minerals and body composition in infant and weanling pigs. J. Nutr. 1999, 129 (1), 132-138.
    • (1999) J. Nutr. , vol.129 , Issue.1 , pp. 132-138
    • Murry Jr., A.C.1    Gelaye, S.2    Casey, J.M.3    Foutz, T.L.4    Kouakou, B.5    Arora, D.6
  • 36
    • 0026778293 scopus 로고
    • Solubility and digestibility of milk proteins in infant formulas exposed to different heat treatments
    • Rudloff, S.; Lonnerdal, B. Solubility and digestibility of milk proteins in infant formulas exposed to different heat treatments. J. Pediatr. Gastroenterol. Nutr. 1992, 15 (1), 25-33.
    • (1992) J. Pediatr. Gastroenterol. Nutr. , vol.15 , Issue.1 , pp. 25-33
    • Rudloff, S.1    Lonnerdal, B.2
  • 37
    • 0024411645 scopus 로고
    • Differences in protein digestibility and quality of liquid concentrate and powder forms of milk-based infant formulas fed to rats
    • Sarwar, G.; Peace, R. W.; Botting, H. G. Differences in protein digestibility and quality of liquid concentrate and powder forms of milk-based infant formulas fed to rats. Am. J. Clin. Nutr. 1989, 49 (5), 806-813.
    • (1989) Am. J. Clin. Nutr. , vol.49 , Issue.5 , pp. 806-813
    • Sarwar, G.1    Peace, R.W.2    Botting, H.G.3
  • 38
    • 0043071267 scopus 로고    scopus 로고
    • The rat as a model animal for the growing pig in determining ileal amino acid digestibility in soya and milk proteins
    • Rutherfurd, S. M.; Moughan, P. J. The rat as a model animal for the growing pig in determining ileal amino acid digestibility in soya and milk proteins. J. Anim. Physiol. Anim. Nutr. (Berlin) 2003, 87 (7-8), 292-300.
    • (2003) J. Anim. Physiol. Anim. Nutr. (Berlin) , vol.87 , Issue.7-8 , pp. 292-300
    • Rutherfurd, S.M.1    Moughan, P.J.2
  • 40
    • 0025319781 scopus 로고
    • Effect of casein and β-casomorphins on gastrointestinal motility in rats
    • Daniel, H.; Vohwinkel, M.; Rehner, G. Effect of casein and β-casomorphins on gastrointestinal motility in rats. J. Nutr. 1990, 120 (3), 252-257.
    • (1990) J. Nutr. , vol.120 , Issue.3 , pp. 252-257
    • Daniel, H.1    Vohwinkel, M.2    Rehner, G.3
  • 42
    • 0033135733 scopus 로고    scopus 로고
    • Deterioration of protein fraction by Maillard reaction in dietetic milks
    • Evangelisti, F.; Calcagno, C.; Nardi, S.; Zunin, P. Deterioration of protein fraction by Maillard reaction in dietetic milks. J. Dairy Res. 1999, 66 (2), 237-243.
    • (1999) J. Dairy Res. , vol.66 , Issue.2 , pp. 237-243
    • Evangelisti, F.1    Calcagno, C.2    Nardi, S.3    Zunin, P.4
  • 43
  • 44
    • 0041417609 scopus 로고    scopus 로고
    • Increasing habitual protein intake accentuates differences in postprandial dietary nitrogen utilization between protein sources in humans
    • Morens, C.; Bos, C.; Pueyo, M. E.; Benamouzig, R.; Gausseres, N.; Luengo, C.; Tome, D.; Gaudichon, C. Increasing habitual protein intake accentuates differences in postprandial dietary nitrogen utilization between protein sources in humans. J. Nutr. 2003, 133 (9), 2733-2740.
    • (2003) J. Nutr. , vol.133 , Issue.9 , pp. 2733-2740
    • Morens, C.1    Bos, C.2    Pueyo, M.E.3    Benamouzig, R.4    Gausseres, N.5    Luengo, C.6    Tome, D.7    Gaudichon, C.8
  • 45
    • 0033946159 scopus 로고    scopus 로고
    • Human adult amino acid requirements: [1-13C]Leucine balance evaluation of the efficiency of utilization and apparent requirements for wheat protein and lysine compared with those for milk protein in healthy adults
    • Millward, D. J.; Fereday, A.; Gibson, N. R.; Pacy, P. J. Human adult amino acid requirements: [1-13C]Leucine balance evaluation of the efficiency of utilization and apparent requirements for wheat protein and lysine compared with those for milk protein in healthy adults. Am. J. Clin. Nutr. 2000, 72 (1), 112-121.
    • (2000) Am. J. Clin. Nutr. , vol.72 , Issue.1 , pp. 112-121
    • Millward, D.J.1    Fereday, A.2    Gibson, N.R.3    Pacy, P.J.4
  • 46
    • 0041802887 scopus 로고    scopus 로고
    • Formation of soluble and micelle-bound protein aggregates in heated milk
    • Guyomarc'h, F.; Law, A. J.; Dalgleish, D. G. Formation of soluble and micelle-bound protein aggregates in heated milk. J. Agric. Food Chem. 2003, 51 (16), 4652-4660.
    • (2003) J. Agric. Food Chem. , vol.51 , Issue.16 , pp. 4652-4660
    • Guyomarc'h, F.1    Law, A.J.2    Dalgleish, D.G.3
  • 47
    • 0019072753 scopus 로고
    • Heat-induced association of β-lactoglobulin and casein micelles
    • Smits, P.; Van Brouwershaven, J. H. Heat-induced association of β-lactoglobulin and casein micelles. J. Dairy Res. 1980, 47 (3), 313-325.
    • (1980) J. Dairy Res. , vol.47 , Issue.3 , pp. 313-325
    • Smits, P.1    Van Brouwershaven, J.H.2
  • 49
    • 0033939409 scopus 로고    scopus 로고
    • The protein digestibility-corrected amino acid score
    • Schaafsma, G. The protein digestibility-corrected amino acid score. J. Nutr. 2000, 130 (7), 1865S-1867S.
    • (2000) J. Nutr. , vol.130 , Issue.7
    • Schaafsma, G.1


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