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Volumn 62, Issue 3, 2014, Pages 699-707

Effect of oxidation of dietary proteins with performic acid on true ileal amino acid digestibility as determined in the growing rat

Author keywords

digestibility; ileal; oxidation; performic acid; protein

Indexed keywords

AMINO ACID DIGESTIBILITY; DIETARY PROTEINS; DIGESTIBILITY; ILEAL; PEPTIDE FORMATION; PERFORMIC ACIDS; PROTEIN DENATURATION; SOY PROTEIN ISOLATES;

EID: 84892978149     PISSN: 00218561     EISSN: 15205118     Source Type: Journal    
DOI: 10.1021/jf403146u     Document Type: Article
Times cited : (22)

References (34)
  • 1
    • 0031010333 scopus 로고    scopus 로고
    • Reactive oxygen-mediated protein oxidation in aging and disease
    • Stadtman, E. R.; Berlett, B. S. Reactive oxygen-mediated protein oxidation in aging and disease Chem. Res. Toxicol. 1997, 10, 485-494
    • (1997) Chem. Res. Toxicol. , vol.10 , pp. 485-494
    • Stadtman, E.R.1    Berlett, B.S.2
  • 4
    • 50649112771 scopus 로고
    • Methionine sulphoxide determination after alkaline hydrolysis of amino acid mixtures, model protein systems, soy products and infant formulas
    • Todd, J. M.; Marable, N. L.; Kehrberg, N. L. Methionine sulphoxide determination after alkaline hydrolysis of amino acid mixtures, model protein systems, soy products and infant formulas J. Food Sci. 1984, 49, 1547-1551
    • (1984) J. Food Sci. , vol.49 , pp. 1547-1551
    • Todd, J.M.1    Marable, N.L.2    Kehrberg, N.L.3
  • 5
    • 0022339538 scopus 로고
    • Determination of methionine sulphoxide in protein and food by hydrolysis with p -toluenesulfonic acid
    • Hayashi, R.; Suzuki, F. Determination of methionine sulphoxide in protein and food by hydrolysis with p -toluenesulfonic acid Anal. Biochem. 1985, 149, 521-528
    • (1985) Anal. Biochem. , vol.149 , pp. 521-528
    • Hayashi, R.1    Suzuki, F.2
  • 7
    • 41149156956 scopus 로고    scopus 로고
    • Oxidation of myosin by heme proteins generates myosin radicals and protein cross-links
    • Lund, M. N.; Luxford, C.; Skibsted, L. H.; Davies, M. J. Oxidation of myosin by heme proteins generates myosin radicals and protein cross-links Biochem. J. 2008, 410, 565-574
    • (2008) Biochem. J. , vol.410 , pp. 565-574
    • Lund, M.N.1    Luxford, C.2    Skibsted, L.H.3    Davies, M.J.4
  • 8
    • 0000959875 scopus 로고
    • Modification of food proteins by covalent crosslinking
    • Singh, H. Modification of food proteins by covalent crosslinking Trends Food Sci. Technol. 1991, 2, 196-200
    • (1991) Trends Food Sci. Technol. , vol.2 , pp. 196-200
    • Singh, H.1
  • 9
    • 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, 1582-1586
    • (1997) J. Agric. Food Chem. , vol.45 , pp. 1582-1586
    • Rutherfurd, S.M.1    Moughan, P.J.2
  • 10
    • 77955272041 scopus 로고    scopus 로고
    • Effect of composition and oxidation of proteins on their solubility, aggregation and proteolytic susceptibility during processing of Cantonese sausage
    • Sun, W.; Cui, C.; Zhao, M.; Zhao, Q.; Yang, B. Effect of composition and oxidation of proteins on their solubility, aggregation and proteolytic susceptibility during processing of Cantonese sausage Food Chem. 2011, 124, 336-341
    • (2011) Food Chem. , vol.124 , pp. 336-341
    • Sun, W.1    Cui, C.2    Zhao, M.3    Zhao, Q.4    Yang, B.5
  • 11
    • 79952816145 scopus 로고    scopus 로고
    • Oxidation of sarcoplasmic proteins during processing of Cantonese sausage in relation to their aggregation behaviour and in vitro digestibility
    • Sun, W.; Zhao, M.; Yang, B.; Zhao, H.; Cui, C. Oxidation of sarcoplasmic proteins during processing of Cantonese sausage in relation to their aggregation behaviour and in vitro digestibility Meat Sci. 2011, 88, 462-467
    • (2011) Meat Sci. , vol.88 , pp. 462-467
    • Sun, W.1    Zhao, M.2    Yang, B.3    Zhao, H.4    Cui, C.5
  • 12
    • 0035543057 scopus 로고    scopus 로고
    • Inhibition of proteolysis in oxidized lipid-damaged proteins
    • Zamora, R.; Hidalgo, F. J. Inhibition of proteolysis in oxidized lipid-damaged proteins J. Agric. Food Chem. 2001, 49, 6006-6011
    • (2001) J. Agric. Food Chem. , vol.49 , pp. 6006-6011
    • Zamora, R.1    Hidalgo, F.J.2
  • 13
    • 0034127455 scopus 로고    scopus 로고
    • Electrophoretic pattern, thermal denaturation, and in vitro digestibility of oxidized myosin
    • Liu, G.; Xiong, Y. L. Electrophoretic pattern, thermal denaturation, and in vitro digestibility of oxidized myosin J. Agric. Food Chem. 2000, 48, 624-630
    • (2000) J. Agric. Food Chem. , vol.48 , pp. 624-630
    • Liu, G.1    Xiong, Y.L.2
  • 15
    • 0003335338 scopus 로고
    • Nutrient requirement of the laboratory rat
    • National Research Council. In, 4 th ed. National Academy of Sciences: Washington, DC
    • National Research Council. Nutrient requirement of the laboratory rat. In Nutrient Requirements of Laboratory Animals, 4 th ed.; National Academy of Sciences: Washington, DC, 1995.
    • (1995) Nutrient Requirements of Laboratory Animals
  • 16
    • 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. 2003, 87, 292-300
    • (2003) J. Anim. Physiol. Anim. Nutr. , vol.87 , pp. 292-300
    • Rutherfurd, S.M.1    Moughan, P.J.2
  • 17
    • 84859704606 scopus 로고    scopus 로고
    • Proteinaceous foods of India and the supply of available lysine
    • Rutherfurd, S. M.; Bains, K.; Moughan, P. J. Proteinaceous foods of India and the supply of available lysine Br. J. Nutr. 2012, 108, S59-S68
    • (2012) Br. J. Nutr. , vol.108
    • Rutherfurd, S.M.1    Bains, K.2    Moughan, P.J.3
  • 18
    • 0001055862 scopus 로고    scopus 로고
    • Determination of titanium dioxide added as an inert marker in chicken digestibility studies
    • Short, F. J.; Gorton, P.; Wiseman, J.; Boorman, K. N. Determination of titanium dioxide added as an inert marker in chicken digestibility studies Anim. Feed Sci. Technol. 1996, 59, 215-221
    • (1996) Anim. Feed Sci. Technol. , vol.59 , pp. 215-221
    • Short, F.J.1    Gorton, P.2    Wiseman, J.3    Boorman, K.N.4
  • 19
    • 0032039144 scopus 로고    scopus 로고
    • The digestible amino acid composition of several milk proteins - Application of a new bioassay
    • Rutherfurd, S. M.; Moughan, P. J. The digestible amino acid composition of several milk proteins-application of a new bioassay J. Dairy Sci. 1998, 81, 909-917
    • (1998) J. Dairy Sci. , vol.81 , pp. 909-917
    • Rutherfurd, S.M.1    Moughan, P.J.2
  • 20
    • 84986764162 scopus 로고
    • Perchloric and trichloroacetic acids as precipitants of protein in endogenous ileal digesta from the rat
    • Moughan, P. J.; Darragh, A. J.; Smith, W. C.; Butts, C. A. Perchloric and trichloroacetic acids as precipitants of protein in endogenous ileal digesta from the rat J. Sci. Food Agric. 1990, 52, 13-21
    • (1990) J. Sci. Food Agric. , vol.52 , pp. 13-21
    • Moughan, P.J.1    Darragh, A.J.2    Smith, W.C.3    Butts, C.A.4
  • 21
    • 84986777829 scopus 로고
    • Endogenous amino acid flow at the terminal ileum of the rat determined under conditions of peptide alimentation
    • Butts, C. A.; Moughan, P. J.; Smith, W. C. Endogenous amino acid flow at the terminal ileum of the rat determined under conditions of peptide alimentation J. Sci. Food Agric. 1991, 55, 175-187
    • (1991) J. Sci. Food Agric. , vol.55 , pp. 175-187
    • Butts, C.A.1    Moughan, P.J.2    Smith, W.C.3
  • 22
    • 84870834134 scopus 로고    scopus 로고
    • version 9.3; SAS Institute Inc. Cary, NC
    • SAS User's Guide: Statistics, version 9.3; SAS Institute Inc.: Cary, NC, 2009.
    • (2009) SAS User's Guide: Statistics
  • 23
    • 84858708718 scopus 로고    scopus 로고
    • Effect of feed intake level on ileal digestibilities of crude protein and amino acids in diets for piglets
    • Goerke, M.; Eklund, M.; Sauer, N.; Rademacher, M.; Piepho, H. P.; Börner, C.; Mosenthin, R. Effect of feed intake level on ileal digestibilities of crude protein and amino acids in diets for piglets J. Sci. Food Agric. 2012, 92, 1261-1266
    • (2012) J. Sci. Food Agric. , vol.92 , pp. 1261-1266
    • Goerke, M.1    Eklund, M.2    Sauer, N.3    Rademacher, M.4    Piepho, H.P.5    Börner, C.6    Mosenthin, R.7
  • 24
    • 50449133154 scopus 로고
    • Modification of tyrosine during performic acid oxidation
    • Thompson, E. O. P. Modification of tyrosine during performic acid oxidation Biochim. Biophys. Acta 1954, 15, 440-441
    • (1954) Biochim. Biophys. Acta , vol.15 , pp. 440-441
    • Thompson, E.O.P.1
  • 25
    • 0028887099 scopus 로고
    • Quantification of cysteine residues following oxidation to cysteic acid in the presence of sodium azide
    • Manneberg, M.; Lahm, H.-W.; Fountoulakis, M. Quantification of cysteine residues following oxidation to cysteic acid in the presence of sodium azide Anal. Biochem. 1995, 231, 349-353
    • (1995) Anal. Biochem. , vol.231 , pp. 349-353
    • Manneberg, M.1    Lahm, H.-W.2    Fountoulakis, M.3
  • 26
    • 84893003967 scopus 로고    scopus 로고
    • Performic acid oxidation of proteins
    • Cold Spring Harbor Laboratory Press: Cold Spring Harbor, NY, USA
    • Simpson, R. J. Performic acid oxidation of proteins. Cold Spring Harbor Protocols; Cold Spring Harbor Laboratory Press: Cold Spring Harbor, NY, USA, 2007.
    • (2007) Cold Spring Harbor Protocols
    • Simpson, R.J.1
  • 27
    • 0029040377 scopus 로고
    • Mass spectrometry identification of amino acid transformations during oxidation of peptides and proteins: Modifications of methionine and tyrosine
    • Chowdhury, S. K.; Eshraghi, J.; Wolfe, H.; Forde, D.; Hlavac, A. G.; Johnston, D. Mass spectrometry identification of amino acid transformations during oxidation of peptides and proteins: modifications of methionine and tyrosine Anal. Chem. 1995, 67, 390-398
    • (1995) Anal. Chem. , vol.67 , pp. 390-398
    • Chowdhury, S.K.1    Eshraghi, J.2    Wolfe, H.3    Forde, D.4    Hlavac, A.G.5    Johnston, D.6
  • 28
    • 0025249194 scopus 로고
    • Amino acid analysis
    • Ozols, J. Amino acid analysis Methods Enzymol. 1990, 182, 587-601
    • (1990) Methods Enzymol. , vol.182 , pp. 587-601
    • Ozols, J.1
  • 29
    • 0030841350 scopus 로고    scopus 로고
    • Protein oxidation in aging disease, and oxidative stress
    • Berlett, B. S.; Stadtman, E. R. Protein oxidation in aging disease, and oxidative stress J. Biol. Chem. 1997, 272, 20313-20316
    • (1997) J. Biol. Chem. , vol.272 , pp. 20313-20316
    • Berlett, B.S.1    Stadtman, E.R.2
  • 30
    • 0000695967 scopus 로고
    • Heat-induced conformational-changes in phaseolin and its relation to proteolysis
    • Deshpande, S. S.; Damodaran, S. Heat-induced conformational-changes in phaseolin and its relation to proteolysis Biochim. Biophys. Acta 1989, 998, 179-188
    • (1989) Biochim. Biophys. Acta , vol.998 , pp. 179-188
    • Deshpande, S.S.1    Damodaran, S.2
  • 31
    • 84872146329 scopus 로고    scopus 로고
    • Detect the sensitivity and response of protein molecular structure of whole canola seed (yellow and brown) to different heat processing methods and relation to protein utilization and availability using ATR-FT/IR molecular spectroscopy with chemometrics
    • Samadi; Theodoridou, K.; Yu, P. Detect the sensitivity and response of protein molecular structure of whole canola seed (yellow and brown) to different heat processing methods and relation to protein utilization and availability using ATR-FT/IR molecular spectroscopy with chemometrics Spectrochim. Acta A: Mol. Biomol. Spectrosc. 2013, 105, 304-313
    • (2013) Spectrochim. Acta A: Mol. Biomol. Spectrosc. , vol.105 , pp. 304-313
    • Samadi1    Theodoridou, K.2    Yu, P.3
  • 32
    • 84864765300 scopus 로고    scopus 로고
    • Relationship between digestibility and secondary structure of raw and thermally treated legume proteins: A Fourier transform infrared (FT-IR) spectroscopic study
    • Carbonara, M.; Maselli, P.; Nucara, A. Relationship between digestibility and secondary structure of raw and thermally treated legume proteins: a Fourier transform infrared (FT-IR) spectroscopic study Amino Acids. 2012, 43, 911-921
    • (2012) Amino Acids. , vol.43 , pp. 911-921
    • Carbonara, M.1    Maselli, P.2    Nucara, A.3
  • 33
    • 84892970256 scopus 로고    scopus 로고
    • BRENDA (Braunschweig Enzyme Database) enzyme portal; (accessed)
    • BRENDA (Braunschweig Enzyme Database) enzyme portal; http://www.brenda- enzymes.org (accessed 2013).
    • (2013)
  • 34
    • 0001419607 scopus 로고    scopus 로고
    • Absorption of lysine and deoxyketosyllysine in an early Maillard browned casein by the growing pig
    • Moughan, P. J.; Gall, M. P. J.; Rutherfurd, S. M. Absorption of lysine and deoxyketosyllysine in an early Maillard browned casein by the growing pig J. Agric. Food Chem. 1996, 44, 1520-1525
    • (1996) J. Agric. Food Chem. , vol.44 , pp. 1520-1525
    • Moughan, P.J.1    Gall, M.P.J.2    Rutherfurd, S.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.