메뉴 건너뛰기




Volumn 58, Issue 7, 2010, Pages 4448-4455

Effect of phenolic compounds on the formation of α-Aminoadipic and γ-Glutamic semialdehydes from myofibrillar proteins oxidized by copper, iron, and myoglobin

Author keywords

DNPH method; LC ESI MS; Myofibrillar proteins; Oxidation; Phenolic compounds; Semialdehydes

Indexed keywords

COPPER; IRON; MUSCLE PROTEIN; MYOGLOBIN; PHENOL DERIVATIVE;

EID: 77950664857     PISSN: 00218561     EISSN: 15205118     Source Type: Journal    
DOI: 10.1021/jf903757h     Document Type: Article
Times cited : (125)

References (33)
  • 1
    • 25844517160 scopus 로고    scopus 로고
    • Protein oxidation in frankfurters with increasing levels of added rosemary essential oil: Effect on color and texture deterioration
    • Estévez, M.; Ventanas, S.; Cava, R. Protein oxidation in frankfurters with increasing levels of added rosemary essential oil: effect on colour and texture deterioration J. Food Sci. 2005, 70, 427 - 432 (Pubitemid 41393204)
    • (2005) Journal of Food Science , vol.70 , Issue.7
    • Estevez, M.1    Ventanas, S.2    Cava, R.3
  • 2
    • 30844459050 scopus 로고    scopus 로고
    • Protein and lipid oxidation in Longissimus dorsi and dry cured loin from Iberian pigs as affected by crossbreeding and diet
    • DOI 10.1016/j.meatsci.2005.09.011, PII S0309174005003517
    • Ventanas, S.; Estévez, M.; Tejeda, J. F.; Ruiz, J. Protein and lipid oxidation in longissimus dorsi and dry cured loin from Iberian pigs as affected by crossbreeding and diet Meat Sci. 2006, 72, 647 - 655 (Pubitemid 43106753)
    • (2006) Meat Science , vol.72 , Issue.4 , pp. 647-655
    • Ventanas, S.1    Estevez, M.2    Tejeda, J.F.3    Ruiz, J.4
  • 3
    • 34347378854 scopus 로고    scopus 로고
    • Extensive feeding versus oleic acid and tocopherol enriched mixed diets for the production of Iberian dry-cured hams: Effect on chemical composition, oxidative status and sensory traits
    • DOI 10.1016/j.meatsci.2007.03.010, PII S0309174007000927
    • Ventanas, S.; Ventanas, J.; Tovar, J.; García, C.; Estévez, M. Extensive feeding versus oleic acid and tocopherol enriched mixed diets for the production of Iberian dry-cured hams: effect on chemical composition, oxidative status and sensory traits Meat Sci. 2007, 77, 246 - 256 (Pubitemid 47021343)
    • (2007) Meat Science , vol.77 , Issue.2 , pp. 246-256
    • Ventanas, S.1    Ventanas, J.2    Tovar, J.3    Garcia, C.4    Estevez, M.5
  • 4
    • 34547471557 scopus 로고    scopus 로고
    • High-oxygen packaging atmosphere influences protein oxidation and tenderness of porcine longissimus dorsi during chill storage
    • DOI 10.1016/j.meatsci.2007.03.016, PII S0309174007000988
    • Lund, M. N.; Lametsch, R.; Hviid, M. S.; Jensen, O. N.; Skibsted, L. H. High-oxygen packaging atmosphere influences protein oxidation and tenderness of porcine longissimus dorsi during chill storage Meat Sci. 2007, 77, 295 - 303 (Pubitemid 47176218)
    • (2007) Meat Science , vol.77 , Issue.3 , pp. 295-303
    • Lund, M.N.1    Lametsch, R.2    Hviid, M.S.3    Jensen, O.N.4    Skibsted, L.H.5
  • 5
    • 67349086867 scopus 로고    scopus 로고
    • Analysis of protein carbonyls in meat products by using the DNPH method, fluorescence spectroscopy and liquid chromatography-electrospray ionization-mass spectrometry (LC-ESI-MS)
    • Armenteros, M.; Heinonen, M.; Ollilainen, V.; Toldrá, F.; Estévez, M. Analysis of protein carbonyls in meat products by using the DNPH method, fluorescence spectroscopy and liquid chromatography-electrospray ionization-mass spectrometry (LC-ESI-MS) Meat Sci. 2009, 83, 104 - 112
    • (2009) Meat Sci. , vol.83 , pp. 104-112
    • Armenteros, M.1    Heinonen, M.2    Ollilainen, V.3    Toldrá, F.4    Estévez, M.5
  • 6
    • 66149126095 scopus 로고    scopus 로고
    • Analysis of protein oxidation markers - α-aminoadipic and γ-glutamic semialdehydes - In food proteins by using LC-ESI-multi-stage tandem MS
    • Estévez, M.; Ollilainen, V.; Heinonen, M. Analysis of protein oxidation markers-α-aminoadipic and γ-glutamic semialdehydes-in food proteins by using LC-ESI-multi-stage tandem MS J. Agric. Food Chem. 2009, 57, 3901 - 3910
    • (2009) J. Agric. Food Chem. , vol.57 , pp. 3901-3910
    • Estévez, M.1    Ollilainen, V.2    Heinonen, M.3
  • 7
    • 0035793088 scopus 로고    scopus 로고
    • Glutamic and aminoadipic semialdehydes are the main carbonyl products of metal-catalyzed oxidation of proteins
    • Requena, J. R.; Chao, C.-C.; Levine, R. L.; Stadtman, E. R. Glutamic and aminoadipic semialdehydes are the main carbonyl products of metal-catalyzed oxidation of proteins Proc. Nat. Acad. Sci. U.S.A. 2001, 98, 69 - 74
    • (2001) Proc. Nat. Acad. Sci. U.S.A. , vol.98 , pp. 69-74
    • Requena, J.R.1    Chao, C.-C.2    Levine, R.L.3    Stadtman, E.R.4
  • 8
    • 23744453195 scopus 로고    scopus 로고
    • Formation of α-aminoadipic and γ-glutamic semialdehydes in proteins by the Maillard reaction
    • DOI 10.1196/annals.1333.016
    • Akagawa, K.; Sasaki, D.; Kurota, Y.; Suyama, K. Formation of α-aminoadipic and γ-glutamic semialdehydes in proteins by the Maillard reaction Ann. N.Y. Acad. Sci. 2005, 1043, 129 - 134 (Pubitemid 41123898)
    • (2005) Annals of the New York Academy of Sciences , vol.1043 , pp. 129-134
    • Akagawa, M.1    Sasaki, D.2    Kurota, Y.3    Suyama, K.4
  • 9
    • 0016126189 scopus 로고
    • Metmyoglobin and nonheme iron as prooxidants in cooked meat
    • Love, J. D.; Pearson, A. M. Metmyoglobin and nonheme iron as prooxidants in cooked meat J. Agric. Food Chem. 1974, 22, 1032 - 1034
    • (1974) J. Agric. Food Chem. , vol.22 , pp. 1032-1034
    • Love, J.D.1    Pearson, A.M.2
  • 10
    • 0031721802 scopus 로고    scopus 로고
    • Polyphenols: Chemistry, dietary sources, metabolism, and nutritional significance
    • Bravo, L. Polyphenols: chemistry, dietary sources, metabolism, and nutritional significance Nutr. Rev. 1998, 56, 317 - 333
    • (1998) Nutr. Rev. , vol.56 , pp. 317-333
    • Bravo, L.1
  • 11
    • 57849084888 scopus 로고    scopus 로고
    • Oxidation of skeletal muscle myofibrillar proteins in oil-in-water emulsions: Interaction with lipids and effect of selected phenolic compounds
    • Estévez, M.; Kylli, P.; Puolanne, E.; Kivikari, R.; Heinonen, M. Oxidation of skeletal muscle myofibrillar proteins in oil-in-water emulsions: interaction with lipids and effect of selected phenolic compounds J. Agric. Food Chem. 2008, 56, 10933 - 10940
    • (2008) J. Agric. Food Chem. , vol.56 , pp. 10933-10940
    • Estévez, M.1    Kylli, P.2    Puolanne, E.3    Kivikari, R.4    Heinonen, M.5
  • 12
    • 52049119358 scopus 로고    scopus 로고
    • Fluorescence spectroscopy as a novel approach for the assessment of myofibrillar protein oxidation in oil-in-water emulsions
    • Estévez, M.; Kylli, P.; Puolanne, E.; Kivikari, R.; Heinonen, M. Fluorescence spectroscopy as a novel approach for the assessment of myofibrillar protein oxidation in oil-in-water emulsions Meat Sci. 2008, 80, 1290 - 1296
    • (2008) Meat Sci. , vol.80 , pp. 1290-1296
    • Estévez, M.1    Kylli, P.2    Puolanne, E.3    Kivikari, R.4    Heinonen, M.5
  • 14
    • 33748670503 scopus 로고    scopus 로고
    • New method for the quantitative determination of major protein carbonyls, α-aminoadipic and γ-glutamic semialdehydes: Investigation of the formation mechanism and chemical nature in vitro and in vivo
    • DOI 10.1021/tx060026p
    • Akagawa, M.; Sasaki, D.; Ishii, Y.; Kurota, Y.; Yotsu-Yamashita, M.; Uchida, K.; Suyuma, K. New methods for the quantitative determination of mayor protein carbonyls, α-aminoadipic and γ-glutamic semialdehydes: Investigation of the formation mechanism and chemical nature in vitro and in vivo Chem. Res. Toxicol. 2006, 19, 1059 - 1065 (Pubitemid 44384836)
    • (2006) Chemical Research in Toxicology , vol.19 , Issue.8 , pp. 1059-1065
    • Akagawa, M.1    Sasaki, D.2    Ishii, Y.3    Kurota, Y.4    Yotsu-Yamashita, M.5    Uchida, K.6    Suyama, K.7
  • 15
    • 0036441178 scopus 로고    scopus 로고
    • Oxidative deamination of lysine residue in plasma protein of diabetic rats
    • Akagawa, M.; Sasaki, T.; Suyama, K. Oxidative deamination of lysine residue in plasma protein of diabetic rats Eur. J. Biochem. 2002, 269, 5451 - 5458
    • (2002) Eur. J. Biochem. , vol.269 , pp. 5451-5458
    • Akagawa, M.1    Sasaki, T.2    Suyama, K.3
  • 17
    • 0029028452 scopus 로고
    • Early destruction of tryptophan residues of apolipoprotein B is a vitamin e independent process during copper-mediated oxidation of LDL
    • Giessauf, A.; Steiner, E.; Esterbauer, H. Early destruction of tryptophan residues of apolipoprotein B is a vitamin E independent process during copper-mediated oxidation of LDL Biochim. Biophys. Acta 1995, 1256, 221 - 232
    • (1995) Biochim. Biophys. Acta , vol.1256 , pp. 221-232
    • Giessauf, A.1    Steiner, E.2    Esterbauer, H.3
  • 18
    • 1542377346 scopus 로고    scopus 로고
    • Protein-lipid interactions during liposome oxidation with added anthocyanin and other phenolic compounds
    • Viljanen, K.; Kivikari, R.; Heinonen, M. Protein-lipid interactions during liposome oxidation with added anthocyanin and other phenolic compounds J. Agric. Food Chem. 2004, 52, 1104 - 1111
    • (2004) J. Agric. Food Chem. , vol.52 , pp. 1104-1111
    • Viljanen, K.1    Kivikari, R.2    Heinonen, M.3
  • 19
    • 0025674536 scopus 로고
    • Metal ion-catalyzed oxidation of proteins: Biochemical mechanism and biological consequences
    • Stadtman, E. R. Metal ion-catalyzed oxidation of proteins: biochemical mechanism and biological consequences Free Radical Biol. Med. 1990, 9, 315 - 325
    • (1990) Free Radical Biol. Med. , vol.9 , pp. 315-325
    • Stadtman, E.R.1
  • 20
    • 0031045361 scopus 로고    scopus 로고
    • Oxidative damage to collagen and related substrates by metal ion/hydrogen peroxide systems: Random attack or site-specific damage?
    • Hawkins, C. L.; Davies, M. J. Oxidative damage to collagen and related substrates by metal ion/hydrogen peroxide systems: random attack or site-specific damage? Biochim. Biophys. Acta 1997, 1360, 84 - 96
    • (1997) Biochim. Biophys. Acta , vol.1360 , pp. 84-96
    • Hawkins, C.L.1    Davies, M.J.2
  • 21
    • 0037092057 scopus 로고    scopus 로고
    • Comparative time-courses of copper-ion-mediated protein and lipid oxidation in low-density lipoprotein
    • DOI 10.1016/S0003-9861(02)00018-8, PII S0003986102000188
    • Knott, H. M.; Baoutina, A.; Davies, M. J.; Dean, R. T. Comparative time-courses of copper-ion-mediated protein and lipid oxidation in low density lipoprotein ABB 2002, 400, 223 - 232 (Pubitemid 34852403)
    • (2002) Archives of Biochemistry and Biophysics , vol.400 , Issue.2 , pp. 223-232
    • Knott, H.M.1    Baoutina, A.2    Davies, M.J.3    Dean, R.T.4
  • 22
    • 21144466779 scopus 로고
    • Catalysis of lipid oxidation in muscle model systems by haem and inorganic iron
    • Monahan, F. J.; Crackel, R. L.; Gray, J. I.; Buckley, D. J.; Morrissey, P. A. Catalysis of lipid oxidation in muscle model systems by haem and inorganic iron Meat Sci. 1993, 34, 95 - 106
    • (1993) Meat Sci. , vol.34 , pp. 95-106
    • Monahan, F.J.1    Crackel, R.L.2    Gray, J.I.3    Buckley, D.J.4    Morrissey, P.A.5
  • 23
    • 0037014283 scopus 로고    scopus 로고
    • Myoglobin-induced lipid oxidation. A review
    • Baron, C. P.; Andersen, H. J. Myoglobin-induced lipid oxidation. A review J. Agric. Food Chem. 2002, 50, 3887 - 3897
    • (2002) J. Agric. Food Chem. , vol.50 , pp. 3887-3897
    • Baron, C.P.1    Andersen, H.J.2
  • 24
    • 44349188157 scopus 로고    scopus 로고
    • Oxidation of porcine myosin by hypervalent myoglobin: The role of thiol groups
    • Frederiksen, A. M.; Lund, M. N.; Andersen, M. L.; Skibsted, L. H. Oxidation of porcine myosin by hypervalent myoglobin: the role of thiol groups J. Agric. Food Chem. 2008, 56, 3297 - 3304
    • (2008) J. Agric. Food Chem. , vol.56 , pp. 3297-3304
    • Frederiksen, A.M.1    Lund, M.N.2    Andersen, M.L.3    Skibsted, L.H.4
  • 25
    • 0037098877 scopus 로고    scopus 로고
    • Reaction between protein radicals and other biomolecules
    • DOI 10.1016/S0891-5849(02)00785-2, PII S0891584902007852
    • Ostdal, H.; Davies, M. J.; Andersen, H. J. Reaction between protein radicals and other biomolecules Free Radical Biol. Med. 2002, 33, 201 - 209 (Pubitemid 34775192)
    • (2002) Free Radical Biology and Medicine , vol.33 , Issue.2 , pp. 201-209
    • Ostdal, H.1    Davies, M.J.2    Andersen, H.J.3
  • 26
    • 0000522990 scopus 로고
    • Catalysts of lipid oxidation in meat-products
    • Johns, A. M.; Birkinshaw, L. H.; Ledward, D. A. Catalysts of lipid oxidation in meat-products Meat Sci. 1989, 25, 209 - 220
    • (1989) Meat Sci. , vol.25 , pp. 209-220
    • Johns, A.M.1    Birkinshaw, L.H.2    Ledward, D.A.3
  • 27
    • 77949824878 scopus 로고    scopus 로고
    • Tryptophan depletion and formation of α-aminoadipic and γ-glutamic semialdehydes in porcine burger patties with added phenolic-rich fruit extracts
    • [Online early access]. DOI: 10.1021/jf903356m. Published Online: Feb 19
    • Ganhão, R.; Morcuende, D.; Estévez, M. Tryptophan depletion and formation of α-aminoadipic and γ-glutamic semialdehydes in porcine burger patties with added phenolic-rich fruit extracts. J. Agric. Food Chem. [Online early access]. DOI: 10.1021/jf903356m. Published Online: Feb 19, 2010.
    • (2010) J. Agric. Food Chem.
    • Ganhão, R.1    Morcuende, D.2    Estévez, M.3
  • 28
    • 0033805608 scopus 로고    scopus 로고
    • The problems of using one-dimensional methods to evaluate multifunctional food and biological antioxidants: Review
    • Frankel, E. N.; Meyer, A. S. The problems of using one-dimensional methods to evaluate multifunctional food and biological antioxidants: review J. Sci. Food Agric. 2000, 80, 1925 - 1941
    • (2000) J. Sci. Food Agric. , vol.80 , pp. 1925-1941
    • Frankel, E.N.1    Meyer, A.S.2
  • 29
    • 0034856552 scopus 로고    scopus 로고
    • Amine oxidase-like activity of polyphenols: Mechanism and properties
    • DOI 10.1046/j.1432-1327.2001.02068.x
    • Akagawa, M.; Suyama, K. Aminooxidase-like activity of polyphenols. Mechanism and properties Eur. J. Biochem. 2001, 268, 1953 - 1963 (Pubitemid 32852936)
    • (2001) European Journal of Biochemistry , vol.268 , Issue.7 , pp. 1953-1963
    • Akagawa, M.1    Suyama, K.2
  • 30
    • 27144523499 scopus 로고    scopus 로고
    • Oxidative deamination of benzylamine and lysine residue in bovine serum albumin by green tea, black tea, and coffee
    • DOI 10.1021/jf050843f
    • Akagawa, M.; Shigemitsu, T.; Suyama, K. Oxidative deamination of benzylamine and lysine residue in bovine serum albumin by green tea, black tea, and coffee J. Agric. Food Chem. 2005, 53, 8019 - 8024 (Pubitemid 41499653)
    • (2005) Journal of Agricultural and Food Chemistry , vol.53 , Issue.20 , pp. 8019-8024
    • Akagawa, M.1    Shigemitsu, T.2    Suyama, K.3
  • 32
    • 0031812255 scopus 로고    scopus 로고
    • Flavonoid deactivation of ferrylmyoglobin in relation to ease of oxidation as determined by cyclic voltammetry
    • Jorgensen, L. V.; Skibsted, L. H. Flavonoid deactivation of ferrylmyoglobin in relation to ease of oxidation as determined by cyclic voltammetry Free Radical Res. 1998, 28, 335 - 351
    • (1998) Free Radical Res. , vol.28 , pp. 335-351
    • Jorgensen, L.V.1    Skibsted, L.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.