메뉴 건너뛰기




Volumn 232, Issue 2, 2011, Pages 343-349

Quenching of excited states of red-pigment zinc protoporphyrin IX by hemin and natural reductors in dry-cured hams

Author keywords

Dry cured ham; Hemin; Laser flash photolysis; Photooxidation; Zinc protoporphyrin

Indexed keywords

ASCORBIC ACIDS; DEHYDROASCORBIC ACID; DIFFUSION CONTROLLED REACTIONS; DRY-CURED HAM; EXCITED SINGLET STATE; GLUTATHIONES; HEMIN; INTERSYSTEM CROSSING; LASER FLASH PHOTOLYSIS; METALLOPORPHYRINS; PHOTOSENSITIZED OXIDATION; POLYPHENOLS; QUENCHING RATE CONSTANT; RED PIGMENTS; SECOND ORDER KINETICS; TRANSIENT ABSORPTION SPECTROSCOPIES; VISIBLE LIGHT; ZINC PROTOPORPHYRIN;

EID: 78751649067     PISSN: 14382377     EISSN: 14382385     Source Type: Journal    
DOI: 10.1007/s00217-010-1392-6     Document Type: Article
Times cited : (11)

References (37)
  • 1
    • 0942267927 scopus 로고    scopus 로고
    • A Zn-porphyrin complex contributes to bright red color in Parma ham
    • Wakamatsu J, Nishimura T, Hattori A (2004) A Zn-porphyrin complex contributes to bright red color in Parma ham. Meat Sci 67: 95-100.
    • (2004) Meat Sci , vol.67 , pp. 95-100
    • Wakamatsu, J.1    Nishimura, T.2    Hattori, A.3
  • 2
    • 33847154036 scopus 로고    scopus 로고
    • Direct demonstration of the presence of zinc in the acetone-extractable red pigment from Parma ham
    • Wakamatsu J, Ito T, Nishimura T, Hattori A (2007) Direct demonstration of the presence of zinc in the acetone-extractable red pigment from Parma ham. Meat Sci 76: 385-387.
    • (2007) Meat Sci , vol.76 , pp. 385-387
    • Wakamatsu, J.1    Ito, T.2    Nishimura, T.3    Hattori, A.4
  • 3
    • 60249095550 scopus 로고    scopus 로고
    • Quantitative determination of Zn protoporphyrin IX, heme and protoporphyrin IX in Parma ham by HPLC
    • Wakamatsu J, Odagiri H, Nishimura T, Hattori A (2009) Quantitative determination of Zn protoporphyrin IX, heme and protoporphyrin IX in Parma ham by HPLC. Meat Sci 82: 139-142.
    • (2009) Meat Sci , vol.82 , pp. 139-142
    • Wakamatsu, J.1    Odagiri, H.2    Nishimura, T.3    Hattori, A.4
  • 5
    • 21044437069 scopus 로고    scopus 로고
    • Thermal and photochemical degradation of myoglobin pigments in relation to colour stability of sliced dry-cured Parma ham and sliced dry-cured ham produced with nitrite salt
    • Adamsen CE, Moller JKS, Hismani R, Skibsted LH (2004) Thermal and photochemical degradation of myoglobin pigments in relation to colour stability of sliced dry-cured Parma ham and sliced dry-cured ham produced with nitrite salt. Eur Food Res Technol 218: 403-409.
    • (2004) Eur Food Res Technol , vol.218 , pp. 403-409
    • Adamsen, C.E.1    Moller, J.K.S.2    Hismani, R.3    Skibsted, L.H.4
  • 7
    • 35748932428 scopus 로고
    • Metal phthalocyanines and porphyrins as photosensitizers for reduction of water to hydrogen
    • Darwent JR, Douglas P, Harriman A, Porter G, Richoux MC (1982) Metal phthalocyanines and porphyrins as photosensitizers for reduction of water to hydrogen. Coord Chem Rev 44: 83-126.
    • (1982) Coord Chem Rev , vol.44 , pp. 83-126
    • Darwent, J.R.1    Douglas, P.2    Harriman, A.3    Porter, G.4    Richoux, M.C.5
  • 9
    • 76649116513 scopus 로고    scopus 로고
    • Modified atmosphere packaging and vacuum packaging for long period chilled storage of dry-cured Iberian ham
    • Parra V, Viguera J, Sanchez J, Peinado J, Esparrago F, Gutierrez JI, Andres AI (2010) Modified atmosphere packaging and vacuum packaging for long period chilled storage of dry-cured Iberian ham. Meat Sci 84: 760-768.
    • (2010) Meat Sci , vol.84 , pp. 760-768
    • Parra, V.1    Viguera, J.2    Sanchez, J.3    Peinado, J.4    Esparrago, F.5    Gutierrez, J.I.6    Andres, A.I.7
  • 10
    • 57749115867 scopus 로고    scopus 로고
    • Effect of pressure and holding time on colour, protein and lipid oxidation of sliced dry-cured Iberian ham and loin during refrigerated storage
    • Cava R, Ladero L, Gonzalez S, Carrasco A, Ramirez MR (2009) Effect of pressure and holding time on colour, protein and lipid oxidation of sliced dry-cured Iberian ham and loin during refrigerated storage. Innov Food Sci Emerg Technol 10: 76-81.
    • (2009) Innov Food Sci Emerg Technol , vol.10 , pp. 76-81
    • Cava, R.1    Ladero, L.2    Gonzalez, S.3    Carrasco, A.4    Ramirez, M.R.5
  • 11
    • 52249121362 scopus 로고    scopus 로고
    • Effect of high pressure treatment on colour, microbial and chemical characteristics of dry cured loin
    • Campus M, Flores M, Martinez A, Toldra F (2008) Effect of high pressure treatment on colour, microbial and chemical characteristics of dry cured loin. Meat Sci 80: 1174-1181.
    • (2008) Meat Sci , vol.80 , pp. 1174-1181
    • Campus, M.1    Flores, M.2    Martinez, A.3    Toldra, F.4
  • 12
    • 33646785073 scopus 로고    scopus 로고
    • Dry-cured ham quality and acceptability as affected by the preservation system used for retail sale
    • Cilla I, Martinez L, Beltran JA, Roncales P (2006) Dry-cured ham quality and acceptability as affected by the preservation system used for retail sale. Meat Sci 73: 581-589.
    • (2006) Meat Sci , vol.73 , pp. 581-589
    • Cilla, I.1    Martinez, L.2    Beltran, J.A.3    Roncales, P.4
  • 13
    • 21144442825 scopus 로고    scopus 로고
    • High pressure treatment of dry-cured Iberian ham. Effect on radical formation, lipid oxidation and colour
    • Andres AI, Moller JKS, Adamsen CE, Skibsted LH (2004) High pressure treatment of dry-cured Iberian ham. Effect on radical formation, lipid oxidation and colour. Eur Food Res Technol 219: 205-210.
    • (2004) Eur Food Res Technol , vol.219 , pp. 205-210
    • Andres, A.I.1    Moller, J.K.S.2    Adamsen, C.E.3    Skibsted, L.H.4
  • 14
    • 36248980366 scopus 로고    scopus 로고
    • The use and control of nitrate and nitrite for the processing of meat products
    • Honikel KO (2008) The use and control of nitrate and nitrite for the processing of meat products. Meat Sci 78: 68-76.
    • (2008) Meat Sci , vol.78 , pp. 68-76
    • Honikel, K.O.1
  • 16
    • 0027251053 scopus 로고
    • The pecking order of free-radicals and antioxidants-Lipid-peroxidation, alpha-tocopherol, and ascorbate
    • Buettner GR (1993) The pecking order of free-radicals and antioxidants-Lipid-peroxidation, alpha-tocopherol, and ascorbate. Arch Biochem Biophys 300: 535-543.
    • (1993) Arch Biochem Biophys , vol.300 , pp. 535-543
    • Buettner, G.R.1
  • 17
    • 78751646964 scopus 로고    scopus 로고
    • Danish Food Composition Databank-ed. 7. 01, technical University of Denmark, Accessed 23 June 2010
    • Danish Food Composition Databank-ed. 7. 01 (2010) National food institute, technical University of Denmark. http://www. foodcomp. dk/v7/fvdb_details. asp?FoodId=0923. Accessed 23 June 2010.
    • (2010) National food institute
  • 18
    • 0021773320 scopus 로고
    • Nicotinamide adenine-dinucleotide (Nad +)-Formal potential of the Nad + Nad. Couple and Nad. Dimerization rate
    • Jensen MA, Elving PJ (1984) Nicotinamide adenine-dinucleotide (Nad +)-Formal potential of the Nad + Nad. Couple and Nad. Dimerization rate. Biochim Biophys Acta 764: 310-315.
    • (1984) Biochim Biophys Acta , vol.764 , pp. 310-315
    • Jensen, M.A.1    Elving, P.J.2
  • 19
    • 1542376929 scopus 로고    scopus 로고
    • Glutathione metabolism and its implications for health
    • Wu GY, Fang YZ, Yang S, Lupton JR, Turner ND (2004) Glutathione metabolism and its implications for health. J Nutr 134: 489-492.
    • (2004) J Nutr , vol.134 , pp. 489-492
    • Wu, G.Y.1    Fang, Y.Z.2    Yang, S.3    Lupton, J.R.4    Turner, N.D.5
  • 21
    • 0027390330 scopus 로고
    • A thermodynamic appraisal of the radical sink hypothesis
    • Koppenol WH (1993) A thermodynamic appraisal of the radical sink hypothesis. Free Radic Biol Med 14: 91-94.
    • (1993) Free Radic Biol Med , vol.14 , pp. 91-94
    • Koppenol, W.H.1
  • 22
    • 0037154534 scopus 로고    scopus 로고
    • Direct electrochemical reduction of hemin in imidazolium-based ionic liquids
    • Compton DL, Laszlo JA (2002) Direct electrochemical reduction of hemin in imidazolium-based ionic liquids. J Electroanal Chem 520: 71-78.
    • (2002) J Electroanal Chem , vol.520 , pp. 71-78
    • Compton, D.L.1    Laszlo, J.A.2
  • 24
    • 77950865952 scopus 로고    scopus 로고
    • Fluorescence quenching to study protein-ligand binding: Common errors
    • van de Weert M (2010) Fluorescence quenching to study protein-ligand binding: common errors. J Fluoresc 20: 625-629.
    • (2010) J Fluoresc , vol.20 , pp. 625-629
    • van de Weert, M.1
  • 26
    • 0037124390 scopus 로고    scopus 로고
    • Molten-globule and other conformational forms of zinc cytochrome c. Effect of partial and complete unfolding of the protein on its electron-transfer reactivity
    • Tremain SM, Kostic NM (2002) Molten-globule and other conformational forms of zinc cytochrome c. Effect of partial and complete unfolding of the protein on its electron-transfer reactivity. Inorg Chem 41: 3291-3301.
    • (2002) Inorg Chem , vol.41 , pp. 3291-3301
    • Tremain, S.M.1    Kostic, N.M.2
  • 27
    • 0000723751 scopus 로고
    • Long-range triplet-triplet energy-transfer within metal-substituted hemoglobins
    • Zemel H, Hoffman BM (1981) Long-range triplet-triplet energy-transfer within metal-substituted hemoglobins. J Am Chem Soc 103: 1192-1201.
    • (1981) J Am Chem Soc , vol.103 , pp. 1192-1201
    • Zemel, H.1    Hoffman, B.M.2
  • 28
    • 0011284481 scopus 로고
    • Triplet-state reactions of zinc protoporphyrins
    • Feitelson J, Barboy N (1986) Triplet-state reactions of zinc protoporphyrins. J Phys Chem 90: 271-274.
    • (1986) J Phys Chem , vol.90 , pp. 271-274
    • Feitelson, J.1    Barboy, N.2
  • 30
    • 34547479187 scopus 로고    scopus 로고
    • Fluorescence dynamics of zinc protoporphyrin in solution and inside anodized aluminum oxide (AAO) nano-channel arrays
    • Lin JS, Chen YC, Chen CC, Luo LY, Diau EWG, Liu TF (2006) Fluorescence dynamics of zinc protoporphyrin in solution and inside anodized aluminum oxide (AAO) nano-channel arrays. J Chin Chem Soc 53: 1405-1412.
    • (2006) J Chin Chem Soc , vol.53 , pp. 1405-1412
    • Lin, J.S.1    Chen, Y.C.2    Chen, C.C.3    Luo, L.Y.4    Diau, E.W.G.5    Liu, T.F.6
  • 31
    • 43049117869 scopus 로고    scopus 로고
    • Zinc-protoporphyrin IX promoting activity in pork muscle
    • Benedini R, Raja V, Parolari G (2008) Zinc-protoporphyrin IX promoting activity in pork muscle. Lwt-Food Sci Technol 41: 1160-1166.
    • (2008) Lwt-Food Sci Technol , vol.41 , pp. 1160-1166
    • Benedini, R.1    Raja, V.2    Parolari, G.3
  • 32
    • 84970583204 scopus 로고
    • Outer-sphere electron-transfer reactions of ascorbate anions
    • Williams NH, Yandell JK (1982) Outer-sphere electron-transfer reactions of ascorbate anions. Aust J Chem 35: 1133-1144.
    • (1982) Aust J Chem , vol.35 , pp. 1133-1144
    • Williams, N.H.1    Yandell, J.K.2
  • 33
    • 0042630956 scopus 로고    scopus 로고
    • Equilibrium (NAD(+)/NADH) potential on poly(Neutral Red) modified electrode
    • Karyakin AA, Ivanova YN, Karyakina EE (2003) Equilibrium (NAD(+)/NADH) potential on poly(Neutral Red) modified electrode. Electrochem Commun 5: 677-680.
    • (2003) Electrochem Commun , vol.5 , pp. 677-680
    • Karyakin, A.A.1    Ivanova, Y.N.2    Karyakina, E.E.3
  • 35
    • 0031812255 scopus 로고    scopus 로고
    • Flavonoid deactivation of ferrylmyoglobin in relation to ease of oxidation as determined by cyclic voltammetry
    • Jorgensen LV, Skibsted LH (1998) Flavonoid deactivation of ferrylmyoglobin in relation to ease of oxidation as determined by cyclic voltammetry. Free Radic Res 28: 335-351.
    • (1998) Free Radic Res , vol.28 , pp. 335-351
    • Jorgensen, L.V.1    Skibsted, L.H.2
  • 36
    • 78751643509 scopus 로고
    • The oxidation-reduction potentials of hemin and related substances. I. The potentials of various hemins and hematins in the absence and presence of pyridine
    • Conant JB, Tongberg CO (1930) The oxidation-reduction potentials of hemin and related substances. I. The potentials of various hemins and hematins in the absence and presence of pyridine. J Bioll Chem 86: 0733-0741.
    • (1930) J Bioll Chem , vol.86 , pp. 0733-0741
    • Conant, J.B.1    Tongberg, C.O.2
  • 37
    • 0035371184 scopus 로고    scopus 로고
    • Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple
    • Schafer FQ, Buettner GR (2001) Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple. Free Radic Biol Med 30: 1191-1212.
    • (2001) Free Radic Biol Med , vol.30 , pp. 1191-1212
    • Schafer, F.Q.1    Buettner, G.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.