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Volumn 108, Issue SUPPL. 2, 2012, Pages

Impact of antinutritional factors in food proteins on the digestibility of protein and the bioavailability of amino acids and on protein quality

Author keywords

Antinutritional factors; protein digestibility quality

Indexed keywords

AMINO ACID; LYSINOALANINE; NUCLEIC ACID BASE; PHYTIC ACID; PROTEIN; TANNIN DERIVATIVE; TRYPSIN INHIBITOR;

EID: 84868154663     PISSN: 00071145     EISSN: 14752662     Source Type: Journal    
DOI: 10.1017/S0007114512002371     Document Type: Article
Times cited : (457)

References (92)
  • 1
    • 0004999149 scopus 로고    scopus 로고
    • World essential amino acid supply with special attention to South-East Asia
    • Pellett PL (1996) World essential amino acid supply with special reference to South-East Asia. Food Nutr Bull 17, 3, 204-234. (Pubitemid 126631903)
    • (1996) Food and Nutrition Bulletin , vol.17 , Issue.3 , pp. 204-234
    • Pellett, P.L.1
  • 2
    • 0023464218 scopus 로고
    • Digestibility of protein and bioavailability of amino acids in foods
    • Sarwar G (1987) Digestibility of protein and bioavailability of amino acids in foods. World Rev Nutr Diet 54, 26-70.
    • (1987) World Rev Nutr Diet , vol.54 , pp. 26-70
    • Sarwar, G.1
  • 4
    • 0001220936 scopus 로고
    • Effects of variation in protein digestibility
    • [CE Bodwell, JS Adkins and DT Hopkins, editors]. Westport, Connecticut: AVI Publishing
    • Hopkins DT (1981) Effects of variation in protein digestibility. In Protein Quality in Humans: Assessment and In Vitro Estimation, pp. 169-193 [CE Bodwell, JS Adkins and DT Hopkins, editors]. Westport, Connecticut: AVI Publishing.
    • (1981) Protein Quality in Humans: Assessment and in Vitro Estimation , pp. 169-193
    • Hopkins, D.T.1
  • 5
    • 23044513596 scopus 로고    scopus 로고
    • Effects of antinutritional factors on protein digestibility and amino acid availability in foods
    • Gilani GS, Cockell KA & Sepehr E (2005) Effects of antinutritional factors on protein digestibility and amino acid availability in foods. J AOAC Int 88, 967-987. (Pubitemid 41066498)
    • (2005) Journal of AOAC International , vol.88 , Issue.3 , pp. 967-987
    • Gilani, G.S.1    Cockell, K.A.2    Sepehr, E.3
  • 6
    • 0026293846 scopus 로고
    • Assessment of the uricogenic potential of processed foods based on the nature and quantity of dietary purines
    • Sarwar G & Brulé D (1991) Assessment of the uricogenic potential of processed foods based on the nature and quantity of dietary purines. Prog Food Nutr Sci 15, 159-181.
    • (1991) Prog Food Nutr Sci , vol.15 , pp. 159-181
    • Sarwar, G.1    Brulé, D.2
  • 8
    • 0028309335 scopus 로고
    • Implications of antinutritional components in soybean foods
    • Liener IE (1994) Implications of antinutritional components in soybean foods. Crit Rev Food Sci Nutr 34, 31-67.
    • (1994) Crit Rev Food Sci Nutr , vol.34 , pp. 31-67
    • Liener, I.E.1
  • 9
    • 0028816895 scopus 로고
    • Compositional changes in trypsin inhibitors, phytic acid, saponins and isoflavones related to soybean processing
    • Anderson RL & Wolf WJ (1995) Compositional changes in trypsin inhibitors, phytic acid, saponins and isoflavones related to soybean processing. J Nutr 125, 581S-585S.
    • (1995) J Nutr , vol.125
    • Anderson, R.L.1    Wolf, W.J.2
  • 11
    • 0036830421 scopus 로고    scopus 로고
    • Chemical composition and nutritional attributes of selected newly developed lines of soybean (Glycine max (L) Merr)
    • DOI 10.1002/jsfa.1239
    • Giami SY (2002) Chemical composition and nutritional attributes of selected newly developed lines of soybean (Glycine max (L) Merr). J Sci Food Agri 82, 1735-1739. (Pubitemid 35249836)
    • (2002) Journal of the Science of Food and Agriculture , vol.82 , Issue.14 , pp. 1735-1739
    • Giami, S.Y.1
  • 12
    • 38349166183 scopus 로고    scopus 로고
    • Enzymatic modification as a tool to improve the functional properties of heat-processed soy flour
    • Radha C, Kumar PR & Prakash V (2008) Enzymatic modification as a tool to improve the functional properties of heat-processed soy flour. J Sci Food Agric 88, 336-343.
    • (2008) J Sci Food Agric , vol.88 , pp. 336-343
    • Radha, C.1    Kumar, P.R.2    Prakash, V.3
  • 13
    • 0000954885 scopus 로고
    • Trypsin inhibitor levels in soy-based infant formulas and commercial soy protein isolates and concentrates
    • Peace RW, Sarwar G & Touchburn SP (1992) Trypsin inhibitor levels in soy-based infant formulas and commercial soy protein isolates and concentrates. Food Res Int 25, 137-141.
    • (1992) Food Res Int , vol.25 , pp. 137-141
    • Peace, R.W.1    Sarwar, G.2    Touchburn, S.P.3
  • 14
    • 0000944822 scopus 로고
    • Protein quality of legume seeds for non-ruminant animals: A literature review
    • Gatel F (1994) Protein quality of legume seeds for non-ruminant animals: a literature review. Anim Feed Sci Tech 45, 317-348.
    • (1994) Anim Feed Sci Tech , vol.45 , pp. 317-348
    • Gatel, F.1
  • 15
    • 0036007618 scopus 로고    scopus 로고
    • Nutritional composition and antinutritional factors of chick peas (Cicer arietinum L.) undergoing different cooking methods and germination
    • El-Adaway TA (2002) Nutritional composition and antinutritional factors of chick peas (Cicer arietinum L.) undergoing different cooking methods and germination. Plant Foods Hum Nutr 57, 83-97.
    • (2002) Plant Foods Hum Nutr , vol.57 , pp. 83-97
    • El-Adaway, T.A.1
  • 16
    • 22144480678 scopus 로고    scopus 로고
    • Nutritional and antinutritional characteristics of seven South Indian wild legumes
    • DOI 10.1007/s11130-005-5102-y
    • Vadivel V & Janardhanan (2005) Nutritional and antinutritional characteristics of seven South Indian wild legumes. Plant Food Hum Nutr 60, 69-75. (Pubitemid 40968363)
    • (2005) Plant Foods for Human Nutrition , vol.60 , Issue.2 , pp. 69-75
    • Vadivel, V.1    Janardhanan, K.2
  • 17
    • 33847024273 scopus 로고    scopus 로고
    • Effect of processing on antinutrients and in vitro protein digestibility of kidney bean (Phaseolus vulgaris L.) varieties grown in East Africa
    • DOI 10.1016/j.foodchem.2006.08.005, PII S030881460600625X
    • Shimelis EA & Rakshit SK (2007) Effect of processing on antinutrients and in vitro protein digestibility of kidney bean (Phaseolus vulgaris L.) varieties grown in East Africa. Food Chem 103, 161-172. (Pubitemid 46274081)
    • (2007) Food Chemistry , vol.103 , Issue.1 , pp. 161-172
    • Shimelis, E.A.1    Rakshit, S.K.2
  • 19
    • 0015998033 scopus 로고
    • Biological and physiological factors in soybeans
    • Rackis JJ (1974) Biological and physiological factors in soybeans. J Am Oil Chem Soc 51, 161A.
    • (1974) J Am Oil Chem Soc , vol.51
    • Rackis, J.J.1
  • 20
    • 22144470846 scopus 로고    scopus 로고
    • Soy protein isolate increases hepatic thyroid hormone receptor content and inhibits its binding to target genes in rats
    • Huang W, Wood C, L'Abbe MR, et al. (2005) Soy protein isolate increases hepatic thyroid hormone receptor content and inhibits its binding to target genes in rats. J Nutr 135, 1631-1635. (Pubitemid 40980710)
    • (2005) Journal of Nutrition , vol.135 , Issue.7 , pp. 1631-1635
    • Huang, W.1    Wood, C.2    L'Abbe, M.R.3    Gilani, G.S.4    Cockell, K.A.5    Xiao, C.W.6
  • 21
    • 0031884162 scopus 로고    scopus 로고
    • Response of pancreatic secretions to feeding diets with low and high levels of soybean trypsin inhibitors in growing pigs
    • DOI 10.1002/(SICI)1097-0010(199803)76:3 <347::AID-JSFA954>3.0.CO;2- 8
    • Li S, Sauer WC, Huang S, et al. (1998) Response of pancreatic secretions to feeding diets with low and high levels of soybean trypsin inhibitors in growing pigs. J Sci Food Agric 76, 347-356. (Pubitemid 28129636)
    • (1998) Journal of the Science of Food and Agriculture , vol.76 , Issue.3 , pp. 347-356
    • Li, S.1    Sauer, W.C.2    Huang, S.3    Hardin, R.T.4
  • 23
    • 0022444068 scopus 로고
    • Comparisons between true digestibility of total nitrogen and limiting amino acids in vegetable proteins fed to rats
    • Sarwar G & Peace RW (1986) Comparisons between true digestibility of total nitrogen and limiting amino acids in vegetable proteins fed to rats. J Nutr 116, 1172-1184. (Pubitemid 16053856)
    • (1986) Journal of Nutrition , vol.116 , Issue.7 , pp. 1172-1184
    • Sarwar, G.1    Peace, R.W.2
  • 24
    • 33444474134 scopus 로고
    • Comparative utilization of raw and autoclaved soybean protein by the human
    • Lewis JH & Taylor FHL (1947) Comparative utilization of raw and autoclaved soybean protein by the human. Proc Soc Exp Biol Med 85.
    • (1947) Proc Soc Exp Biol Med , vol.85
    • Lewis, J.H.1    Fhl, T.2
  • 25
    • 0028269137 scopus 로고
    • Production of proline-rich proteins by the parotid glands of rats is enhanced by feeding diets containing tannins from faba beans (Vicia faba L.)
    • Jansman AFJ, Frohlich AA & Marquardt RR (1994) Production of proline-rich proteins by the parotid glands of rats is enhanced by feeding diets containing tannins from faba beans (Vicia faba L.). J Nutr 124, 249-258. (Pubitemid 24093964)
    • (1994) Journal of Nutrition , vol.124 , Issue.2 , pp. 249-258
    • Jansman, A.J.M.1    Frohlich, A.A.2    Marquardt, R.R.3
  • 26
    • 0006685216 scopus 로고
    • Occurrence, nature and composition
    • [DK Salunkhe, JK Chavan and SS Kadam, editors]. Boca Raton, FL: CRC Press
    • Salunkhe DK, Chavan JK & Kadam SS (1990) Occurrence, nature and composition. In Dietary Tannins: Consequences and Remedies, pp. 29-68 [DK Salunkhe, JK Chavan and SS Kadam, editors]. Boca Raton, FL: CRC Press.
    • (1990) Dietary Tannins: Consequences and Remedies , pp. 29-68
    • Salunkhe, D.K.1    Chavan, J.K.2    Kadam, S.S.3
  • 28
    • 73749087412 scopus 로고    scopus 로고
    • Nutritional value of faba bean (Vicia faba L.) seeds for feed and food
    • Krépon K, Marget P, Peyronnet C, et al. (2010) Nutritional value of faba bean (Vicia faba L.) seeds for feed and food. Field Crop Res 115, 329-339.
    • (2010) Field Crop Res , vol.115 , pp. 329-339
    • Krépon, K.1    Marget, P.2    Peyronnet, C.3
  • 29
    • 0025911603 scopus 로고
    • Activities of enzymes of the pancreas, and the lumen and mucosa of the small intestine in growing broiler cockerels fed on tannin-containing diets
    • Ahmed AE, Smithard R & Ellis M (1991) Activities of enzymes of the pancreas, and the lumen and mucosa of the small intestine in growing broiler cockerels fed on tannin-containing diets. Br J Nutr 65, 189-197.
    • (1991) Br J Nutr , vol.65 , pp. 189-197
    • Ahmed, A.E.1    Smithard, R.2    Ellis, M.3
  • 31
    • 0029187215 scopus 로고
    • Effects of hulls of faba beans (Vicia faba L.) with a low or high contents of condensed tannins on the apparent ileal and fecal digestibility of nutrients and the excretion of endogenous protein in ileal digesta and feces of pigs
    • Jansman AJM, Verstegen MWA, Huisman J, et al. (1995) Effects of hulls of faba beans (Vicia faba L.) With a low or high contents of condensed tannins on the apparent ileal and fecal digestibility of nutrients and the excretion of endogenous protein in ileal digesta and feces of pigs. J Anim Sci 73, 118-127.
    • (1995) J Anim Sci , vol.73 , pp. 118-127
    • Jansman, A.J.M.1    Verstegen, M.W.A.2    Huisman, J.3
  • 33
    • 0002431773 scopus 로고
    • Tanninmediated induction of proline-rich protein synthesis
    • Mehansho H, Asquith TN, Butler LG, et al. (1992) Tanninmediated induction of proline-rich protein synthesis. J Agri Food Chem 40, 93-97.
    • (1992) J Agri Food Chem , vol.40 , pp. 93-97
    • Mehansho, H.1    Asquith, T.N.2    Butler, L.G.3
  • 35
    • 0011810564 scopus 로고    scopus 로고
    • Phytic acid and phosphorus in crop grain seeds and fruits
    • [NR Reddy and SK Sethe, editors]. Boca Raton, FL: CRC Press
    • Lott JNA, Ockenden I, Raboy Raboy, et al. (2002) Phytic acid and phosphorus in crop grain seeds and fruits. In Food Phytates, pp. 7-24 [NR Reddy and SK Sethe, editors]. Boca Raton, FL: CRC Press.
    • (2002) Food Phytates , pp. 7-24
    • Jna, L.1    Ockenden, I.2    Raboy, R.3
  • 36
    • 0033124344 scopus 로고    scopus 로고
    • Influence of microbial phytase on apparent ileal amino acid digestibility of feedstuffs for broilers
    • Ravindran V, Cabahug S, Ravindran G, et al. (1999) Influence of microbial phytase on apparent ileal amino acid digestibility of food stuffs for broilers. Poultry Sci 78, 699-706. (Pubitemid 129555212)
    • (1999) Poultry Science , vol.78 , Issue.5 , pp. 699-706
    • Ravindran, V.1    Cabahug, S.2    Ravindran, G.3    Bryden, W.L.4
  • 38
    • 84906907181 scopus 로고    scopus 로고
    • Occurrence, distribution, content and dietary intake of phytate
    • [NR Reddy and SK Sethe, editors]. Boca Raton, FL: CRC Press
    • Reddy NR (2002) Occurrence, distribution, content and dietary intake of phytate. In Food Phytates, pp. 25-52 [NR Reddy and SK Sethe, editors]. Boca Raton, FL: CRC Press.
    • (2002) Food Phytates , pp. 25-52
    • Reddy, N.R.1
  • 40
    • 0039419798 scopus 로고
    • Vitro alpha-amylase inhibitor activity-phytate relationships in proteins from Phaseolus beans
    • Li Z, Alli I & Kermasha S (1993) In vitro alpha-amylase inhibitor activity-phytate relationships in proteins from Phaseolus beans. Food Res 26, 195-201.
    • (1993) Food Res , vol.26 , pp. 195-201
    • Li, Z.1    Alli, I.2    Kermasha, S.3
  • 41
    • 0029243435 scopus 로고
    • Variability in phytic acid content and protein digestibility of grain legumes
    • Chitra U, Vimala V, Singh U, et al. (1995) Variability in phytic acid content and protein digestibility of grain legumes. Plant Foods Hum Nutr 47, 163-172.
    • (1995) Plant Foods Hum Nutr , vol.47 , pp. 163-172
    • Chitra, U.1    Vimala, V.2    Singh, U.3
  • 42
    • 77953890008 scopus 로고    scopus 로고
    • Changes in functional properties and antinutritional factors of extruded hard-to-cook common beans (Phaseolus vulgaris L.)
    • Batista KA, Prudêncio SH & Fernandes KE (2010) Changes in functional properties and antinutritional factors of extruded hard-to-cook common beans (Phaseolus vulgaris L.). J Food Sci 75, C286-C290.
    • (2010) J Food Sci , vol.75
    • Batista, K.A.1    Prudêncio, S.H.2    Fernandes, K.E.3
  • 45
    • 0001342861 scopus 로고
    • Effect of phytate on the in vitro activity of digestive proteinases
    • Vaintraub IA & Bulmaga VP (1991) Effect of phytate on the in vitro activity of digestive proteinases. J Agri Food Chem 39, 859-861.
    • (1991) J Agri Food Chem , vol.39 , pp. 859-861
    • Vaintraub, I.A.1    Bulmaga, V.P.2
  • 46
    • 0023585403 scopus 로고
    • Influence of phytate on in vitro digestibility of casein under physiological conditions
    • Lothia D, Hoch H & Kievernagel Y (1987) Influence of phytate on in vitro digestibility of casein under physiological conditions. Plant Foods Hum Nutr 37, 229-235.
    • (1987) Plant Foods Hum Nutr , vol.37 , pp. 229-235
    • Lothia, D.1    Hoch, H.2    Kievernagel, Y.3
  • 47
    • 0032821910 scopus 로고    scopus 로고
    • Enzymatic treatment and use of starters for the nutrient enhancement in fermented flour of red and white varieties of finger millet (Eleusine coracana)
    • DOI 10.1021/jf980564a
    • Antony U & Chnadra TS (1999) Enzymatic treatment and use of starters for the nutrient enhancement in fermented flour of red and white varieties of finger millet (Eleusine coracana). J Agri Food Chem 47, 2016-2019. (Pubitemid 29438753)
    • (1999) Journal of Agricultural and Food Chemistry , vol.47 , Issue.5 , pp. 2016-2019
    • Antony, U.1    Chandra, T.S.2
  • 48
    • 0035292802 scopus 로고    scopus 로고
    • Microbial phytase improves performance, apparent metabolizable energy, and ileal amino acid digestibility of broilers fed a lysine-deficient diet
    • Ravindran V, Selle PH, Ravindran G, et al. (2001) Microbial phytase improves performance, apparent metabolizable energy, and ileal amino acid digestibility of broilers fed a lysine-deficient diet. Poultry Sci 80, 338-344. (Pubitemid 33659903)
    • (2001) Poultry Science , vol.80 , Issue.3 , pp. 338-344
    • Ravindran, V.1    Selle, P.H.2    Ravindran, G.3    Morel, P.C.H.4    Kies, A.K.5    Bryden, W.L.6
  • 49
    • 0023908986 scopus 로고
    • Differences in uricogenic effects of dietary purine bases, nucleosides and nucleotides in rats
    • Brulé D, Sarwar G, Savoie L, et al. (1988) Differences in uricogenic effects of dietary purine bases, nucleosides and nucleotides in rats. J Nutr 118, 780-786.
    • (1988) J Nutr , vol.118 , pp. 780-786
    • Brulé, D.1    Sarwar, G.2    Savoie, L.3
  • 50
    • 38249032215 scopus 로고
    • Purine contents of selected Canadian food products
    • Brulé D, Sarwar G & Savoie L (1988) Purine contents of selected Canadian food products. J Food Comp Anal 1, 130-138.
    • (1988) J Food Comp Anal , vol.1 , pp. 130-138
    • Brulé, D.1    Sarwar, G.2    Savoie, L.3
  • 51
    • 0009988766 scopus 로고
    • PAG ad hoc working group on clinical evaluation and acceptance of nucleic acids of SCP for human consumption
    • FAO/WHO
    • FAO/WHO (1975) PAG ad hoc working group on clinical evaluation and acceptance of nucleic acids of SCP for human consumption. In Protein-Calorie Advisory Group (PAG) of the United Nations System Bulletin 5, pp. 17-26.
    • (1975) Protein-Calorie Advisory Group (PAG) of the United Nations System Bulletin , vol.5 , pp. 17-26
  • 52
    • 0017143834 scopus 로고
    • Adenine metabolism during and after exchange transfusion in newborn infants with CPD-adenine blood
    • Kreuger A (1976) Adenine metabolism during and after exchange transfusion in newborn infants with CPD-adenine blood. Translation 16, 249-252.
    • (1976) Translation , vol.16 , pp. 249-252
    • Kreuger, A.1
  • 53
    • 0036943526 scopus 로고    scopus 로고
    • Nutritional and metabolic consequences of the early Maillard reaction of heat treated milk in the pig. Significance for man
    • DOI 10.1007/s003940200000
    • Rérat A, Calmes R, Vaissade P, et al. (2002) Nutritional and metabolic consequences of the early Maillard reaction of heat treated milk in the pig. Significance for man. Eur J Nutr 41, 1-11. (Pubitemid 36055988)
    • (2002) European Journal of Nutrition , vol.41 , Issue.1 , pp. 1-11
    • Rerat, A.1    Calmes, R.2    Vaissade, P.3    Finot, P.-A.4
  • 54
    • 0024487515 scopus 로고
    • Protein reactions during food processing and storage and their relevance to human nutrition
    • Erbersdobler HF (1989) Protein reactions during food processing and storage and their relevance to human nutrition. Bibl Nutr Dieta 43, 140-155.
    • (1989) Bibl Nutr Dieta , vol.43 , pp. 140-155
    • Erbersdobler, H.F.1
  • 56
    • 0002423936 scopus 로고
    • Metabolic and physiological consequences of Maillard reaction products
    • [PA Finot, HU Aeschbacher, RF Hurrell and R Liardon, editors]. Basel: Birkhauser
    • Finot PA (1990) Metabolic and physiological consequences of Maillard reaction products. In The Maillard Reaction in Food Processing, Human Nutrition and Physiology, pp. 259-272 [PA Finot, HU Aeschbacher, RF Hurrell and R Liardon, editors]. Basel: Birkhauser.
    • (1990) The Maillard Reaction in Food Processing, Human Nutrition and Physiology , pp. 259-272
    • Finot, P.A.1
  • 58
    • 0026778293 scopus 로고
    • Solubility and digestibility of milk proteins in infant formulas exposed to different heat treatments
    • Rudolff S & Lönnerdal B (1992) Solubility and digestibility of milk proteins in infant formulas exposed to different heat treatments. J Pediatr Gastr Nutr 15, 25-33.
    • (1992) J Pediatr Gastr Nutr , vol.15 , pp. 25-33
    • Rudolff, S.1    Lönnerdal, B.2
  • 59
    • 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 RW & Botting HG (1989) Differences in protein digestibility and quality of liquid concentrates and powder forms of milk-based formulas fed to rats. Am J Clin Nutr 49, 806-813. (Pubitemid 19139781)
    • (1989) American Journal of Clinical Nutrition , vol.49 , Issue.5 , pp. 806-813
    • Sarwar, G.1    Peace, R.W.2    Botting, H.G.3
  • 60
    • 0032839957 scopus 로고    scopus 로고
    • Chemistry, nutrition, and microbiology of D-amino acids
    • DOI 10.1021/jf990080u
    • Friedman M (1999) Chemistry, nutrition, and microbiology of D-amino acids. J Agr Food Chem 47, 3457-3479. (Pubitemid 29449456)
    • (1999) Journal of Agricultural and Food Chemistry , vol.47 , Issue.9 , pp. 3457-3479
    • Friedman, M.1
  • 61
    • 0025733478 scopus 로고
    • Formation, nutritional value and safety of D-amino acids
    • [M Friedman, editor]. New York, N.Y: Plenum Press
    • Friedman M (1991) Formation, nutritional value and safety of D-amino acids. In Nutritional and Toxicological Consequences of Food Processing, pp. 447-481 [M Friedman, editor]. New York, N.Y: Plenum Press.
    • (1991) Nutritional and Toxicological Consequences of Food Processing , pp. 447-481
    • Friedman, M.1
  • 62
    • 84872614785 scopus 로고    scopus 로고
    • The D-amino acid content of foodstuffs (A Review)
    • Csapó J, Albert Cs & Csapóo-Kiss Zs (2009) The D-amino acid content of foodstuffs (A Review). Acta Univ Sapientiae Alimentaria 2, 5-30.
    • (2009) Acta Univ Sapientiae Alimentaria , vol.2 , pp. 5-30
    • Csapó, J.1    Cs, A.2    Zs, C.3
  • 63
    • 0022397331 scopus 로고
    • Analysis of problems encountered in the determination of amino acid enantiomeric ratios by gas chromatography
    • DOI 10.1016/0003-2697(85)90603-7
    • Payan IL, Cadilla-Perezrios R, Fisher GH, et al. (1985) Analysis of problems encountered in the determination of amino acid enantiomeric ratios by gas chromatography. Anal Biochem 149, 484-491. (Pubitemid 16238631)
    • (1985) Analytical Biochemistry , vol.149 , Issue.2 , pp. 484-491
    • Payan, I.L.1    Cadilla-Perezrios, R.2    Fisher, G.H.3    Man, E.H.4
  • 64
    • 0011339194 scopus 로고
    • Amino acid racemisation in alkali-treated food proteins-chemistry, toxicology, and nutritional consequences
    • [JH Whitaker and M Fujimaki, editors]. Washington, DC: American Chemical Society
    • Masters PM & Friedman M (1980) Amino acid racemisation in alkali-treated food proteins-chemistry, toxicology, and nutritional consequences. In Chemical Deterioration of Proteins, pp. 165-194 [JH Whitaker and M Fujimaki, editors]. Washington, DC: American Chemical Society.
    • (1980) Chemical Deterioration of Proteins , pp. 165-194
    • Masters, P.M.1    Friedman, M.2
  • 65
    • 0006877541 scopus 로고
    • Environmental effects of protein quality
    • Inst. Food Technologies Basic Symp Ser Westport, Connecticut: AVI Publishing
    • Finley JW (1985) Environmental effects of protein quality. In Chemical Changes in Food Processing, pp. 443-482. Inst. Food Technologies Basic Symp Ser Westport, Connecticut: AVI Publishing.
    • (1985) Chemical Changes in Food Processing , pp. 443-482
    • Finley, J.W.1
  • 66
    • 0024412670 scopus 로고
    • Occurence of D-amino acids in food. Detection by capillary gas chromatography and by reversed-phase high-performance liquid chromatography with L-phenylalaninamides as chiral selectors
    • DOI 10.1016/S0021-9673(00)91414-6
    • Palla G, Marchelli R, Dossena G, et al. (1989) Occurrence of D-amino acids in food. Detection by capillary gas chromatography and by reversed-phase high-performance liquid chromatography with L-phenylalanine amides as chiral selectors. J Chromatogr 475, 45-53. (Pubitemid 19193591)
    • (1989) Journal of Chromatography , vol.475 , pp. 45-53
    • Palla, G.1    Marchelli, R.2    Dossena, A.3    Casnati, G.4
  • 67
    • 0012371565 scopus 로고
    • Lysinolanine: Biological effects and significance
    • [HL Wilcke, DT Hopkins and DH Waggle, editors]. New York, NY: Academic Press
    • Struthers BJ, Dahlgren RR, Hopkins DT, et al. (1979) Lysinolanine: biological effects and significance. In Soy Protein and Human Nutrition, pp. 235-260 [HL Wilcke, DT Hopkins and DH Waggle, editors]. New York, NY: Academic Press.
    • (1979) Soy Protein and Human Nutrition , pp. 235-260
    • Struthers, B.J.1    Dahlgren, R.R.2    Hopkins, D.T.3
  • 68
    • 0002118863 scopus 로고
    • Lysinoalanine in food proteins
    • Finot PA (1983) Lysinoalanine in food proteins. Rev Clin Nutr 53, 67-80.
    • (1983) Rev Clin Nutr , vol.53 , pp. 67-80
    • Finot, P.A.1
  • 69
    • 0032965144 scopus 로고    scopus 로고
    • Chemistry, biochemistry, nutrition, and microbiology of lysinoalanine, lanthionine, and histidinoalanine in food and other proteins
    • DOI 10.1021/jf981000+
    • Friedman M (1999) Chemistry, biochemistry, nutrition and microbiology of lysinoalanine, lanthionine, and histidinoalanine in food and other proteins. J Agr Food Chem 47, 1295-1319. (Pubitemid 29217113)
    • (1999) Journal of Agricultural and Food Chemistry , vol.47 , Issue.4 , pp. 1295-1319
    • Friedman, M.1
  • 71
    • 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 15N-labeling
    • de Vrese M, Frik R, Roos N, et al. (2000) Protein-bound D-amino acids, and to a lesser extent lysinoalanine, decrease true ileal protein digestibility in minipigs as determined with 15N-labeling. J Nutr 130, 2026-2203.
    • (2000) J Nutr , vol.130 , pp. 2026-2203
    • De Vrese, M.1    Frik, R.2    Roos, N.3
  • 72
    • 0024760827 scopus 로고
    • Mechanism of toxicity of lysinoalanine
    • International Life Sciences Institute
    • International Life Sciences Institute (1989) Mechanism of toxicity of lysinoalanine. Nutr Rev 47, 362-364.
    • (1989) Nutr Rev , vol.47 , pp. 362-364
  • 73
    • 0016596222 scopus 로고
    • Lysinoalanine: Presence in foods and food ingredients
    • Sternberg M, Kim CY & Schwende FJ (1975) Lysinoalanine: presence in foods and food ingredients. Science 190, 992-994.
    • (1975) Science , vol.190 , pp. 992-994
    • Sternberg, M.1    Kim, C.Y.2    Schwende, F.J.3
  • 74
    • 0017325528 scopus 로고
    • Biological effects of alkalitreated protein and lysinoalanine: An overview
    • [M Friedman, editor]. New York, NY: Plenum Press
    • Gould DH & MacGregor JT (1977) Biological effects of alkalitreated protein and lysinoalanine: an overview. In Protein Crosslinking: Nutritional and Medical Consequences, pp. 29-48 [M Friedman, editor]. New York, NY: Plenum Press.
    • (1977) Protein Crosslinking: Nutritional and Medical Consequences , pp. 29-48
    • Gould, D.H.1    MacGregor, J.T.2
  • 75
    • 0018614005 scopus 로고
    • Biological effects of alkali-treated soya protein and lactalbumin in the rat and mouse
    • DOI 10.1016/0015-6264(79)90119-6
    • Karayiannis N, MacGregor JT & Bjeldanes LF (1979) Biological effects of alkali-treated soy protein and lactalbumin in the rat and mouse. Food Cosmet Toxicol 17, 591-604. (Pubitemid 10184993)
    • (1979) Food and Cosmetics Toxicology , vol.17 , Issue.6 , pp. 591-604
    • Karayiannis, N.I.1    MacGregor, J.T.2    Bjeldanes, L.F.3
  • 76
    • 0017146124 scopus 로고
    • Feeding of alkali-treated proteins: Feeding studies with free and protein- bound lysinoalanine in rats and other animals
    • DeGroot AP, Slump P, Feron WJ, et al. (1976) Feeding of alkali-treated proteins: feeding studies with free and protein- bound lysinoalanine in rats and other animals. J Nutr 106, 1527-1538.
    • (1976) J Nutr , vol.106 , pp. 1527-1538
    • Degroot, A.P.1    Slump, P.2    Feron, W.J.3
  • 77
    • 0016594598 scopus 로고
    • Renal toxicity of Ne-DL (2-amino-2- carboxyethyl)-L-lysine, lysinoalanine
    • Woodard JC (1975) Renal toxicity of Ne-DL (2-amino-2- carboxyethyl)-L-lysine, lysinoalanine. Vet Path 12, 65-66.
    • (1975) Vet Path , vol.12 , pp. 65-66
    • Woodard, J.C.1
  • 78
    • 0017869534 scopus 로고
    • Lysinoalanine in alkali treated proteins and factors influencing its biological activity
    • Slump P (1978) Lysinoalanine in alkali treated proteins and factors influencing its biological activity. Annales de la Nutr et de l'Alimentation 32, 271-279.
    • (1978) Annales de la Nutr et de L'Alimentation , vol.32 , pp. 271-279
    • Slump, P.1
  • 79
    • 0033281790 scopus 로고    scopus 로고
    • Influence of feeding alkaline/heat processed proteins on growth and protein and mineral status of rats
    • Sarwar G, L'Abbé MR, Trick K, et al. (1999) Influence of feeding alkaline/heat processed proteins on growth and protein and mineral status of rats. Adv Exp Med Biol 459, 161-177.
    • (1999) Adv Exp Med Biol , vol.459 , pp. 161-177
    • Sarwar, G.1    L'abbé, M.R.2    Trick, K.3
  • 80
    • 84985275155 scopus 로고
    • Relationship between in vitro digestibility of casein and its contents of lysinoalanine and D-amino acids
    • Friedman M, Zahnley JC & Masters PM (1981) Relationship between in vitro digestibility of casein and its contents of lysinoalanine and D-amino acids. J Food Sci 46, 127-131.
    • (1981) J Food Sci , vol.46 , pp. 127-131
    • Friedman, M.1    Zahnley, J.C.2    Masters, P.M.3
  • 81
    • 0020442078 scopus 로고
    • The nutritional value of lysinoalanine as a source of lysing for mice
    • Friedman M, Gumbmann MR & Savoie L (1982) The nutritional value of lysinoalanine as a source of lysine. Nutr Rep Int 26, 937-943. (Pubitemid 13141007)
    • (1982) Nutrition Reports International , vol.26 , Issue.6 , pp. 937-943
    • Friedman, M.1    Gumbmann, M.R.2    Savoie, L.3
  • 82
    • 0019314462 scopus 로고
    • Studies on the utilization of lysinoalanine and lanthionine
    • Robbins KR, Baker DH & Finley JW (1980) Studies on the utilization of lysinoalanine and lanthionine. J Nutr 110, 907-915. (Pubitemid 10046112)
    • (1980) Journal of Nutrition , vol.110 , Issue.5 , pp. 907-915
    • Robbins, K.R.1    Baker, D.H.2    Finley, J.W.3
  • 83
    • 0028030297 scopus 로고
    • The protein quality of some enteral products is inferior to that of casein as assessed by rat growth methods and digestibility-corrected amino acid scores
    • Sarwar G & Peace RW (1994) The protein quality of some enteral products is inferior to that of casein as assessed by rat growth methods and digestibility-corrected amino acid scores. J Nutr 124, 2223-2232. (Pubitemid 24365249)
    • (1994) Journal of Nutrition , vol.124 , Issue.11 , pp. 2223-2232
    • Sarwar, G.1    Peace, R.W.2
  • 84
    • 84964423067 scopus 로고
    • Protein quality in commercial milk-based infant formulas
    • Pompei C, RossiM& Mare F (1987) Protein quality in commercial milk-based infant formulas. J Food Quality 10, 375-391.
    • (1987) J Food Quality , vol.10 , pp. 375-391
    • Pompei, C.1    Rossi, M.2    Mare, F.3
  • 85
    • 0028938119 scopus 로고
    • Dipeptide transport and hydrolysis in isolated loops of rat small intestine: Effects of stereospecificity
    • Lister N, Sykes AP, Baily PD, et al. (1995) Dipeptide transport and hydrolysis in isolated loops of rat small intestine: effects of stereospecificity. J Physiol London 484, 173-182.
    • (1995) J Physiol London , vol.484 , pp. 173-182
    • Lister, N.1    Sykes, A.P.2    Baily, P.D.3
  • 86
    • 0021984599 scopus 로고
    • Syntheses and digestibility determination of some epimeric tripeptides occurring in dietary proteins
    • DOI 10.1016/S0271-5317(85)80176-7
    • Paquet A, Thresher WC, Swaisgood HE, et al. (1985) Synthesis and digestibility determination of some epimeric tripeptides occurring in dietary proteins. Nutr Res 5, 891-901. (Pubitemid 15231360)
    • (1985) Nutrition Research , vol.5 , Issue.8 , pp. 891-901
    • Paquet, A.1    Thresher, W.C.2    Swaisgood, H.E.3    Catignani, G.L.4
  • 87
    • 0021931715 scopus 로고
    • Bioavailability of methionine in some tripeptides occurring in dietary proteins as determined by rat growth
    • DOI 10.1016/S0271-5317(85)80177-9
    • Sarwar G, Paquet A & Peace RW (1985) Bioavailability of methionine in some tripeptides occurring in dietary proteins as determined by rat growth. Nutr Res 5, 903-909. (Pubitemid 15231361)
    • (1985) Nutrition Research , vol.5 , Issue.8 , pp. 903-909
    • Sarwar, G.1    Paquet, A.2    Peace, R.W.3
  • 89
    • 0037228809 scopus 로고    scopus 로고
    • Protein digestibility and quality in products containing antinutritional factors are adversely affected by old age in rats
    • Gilani GS & Sepehr E (2003) Protein digestibility and quality in products containing antinutritional factors are adversely affected by old age in rats. J Nutr 133, 220-225. (Pubitemid 36070604)
    • (2003) Journal of Nutrition , vol.133 , Issue.1 , pp. 220-225
    • Gilani, G.S.1    Sepehr, E.2
  • 91
    • 21344483828 scopus 로고
    • Trypsin loss at the ileum of calves fed milk replacers containing legume protein
    • Lalles SP & Toullec R (1994) Trypsin loss at the ileum of calves fed milk replacers containing legume protein. Ann Zootech 43, 263.
    • (1994) Ann Zootech , vol.43 , pp. 263
    • Lalles, S.P.1    Toullec, R.2
  • 92
    • 0022523304 scopus 로고
    • Influence of aging upon pancreatic digestive enzymes
    • Greenberg RE & Holt PR (1986) Influence of aging upon pancreatic digestive enzymes. Dig Dis Sci 31, 970-977. (Pubitemid 16016522)
    • (1986) Digestive Diseases and Sciences , vol.31 , Issue.9 , pp. 970-977
    • Greenberg, R.E.1    Holt, P.R.2


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