A note on the nature of the haematin pigments present in freeze dried and cooked beef
Analysis of the reflectance spectra of beef samples treated to contain all the haemoproteins in one pigment form indicated that little or no change in the haematin environment occurs on freeze drying fresh, oxymyoglobin-rich meat or cooked meat. Dehydration of metmyoglobin in meat results in the wat...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1987 |
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| Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
|---|---|
| Übergeordnetes Werk: |
in: Meat Science - Amsterdam : Elsevier, 21(1987), 3, Seite 231-237 |
| Übergeordnetes Werk: |
volume:21 ; year:1987 ; number:3 ; pages:231-237 |
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| 520 | |a Analysis of the reflectance spectra of beef samples treated to contain all the haemoproteins in one pigment form indicated that little or no change in the haematin environment occurs on freeze drying fresh, oxymyoglobin-rich meat or cooked meat. Dehydration of metmyoglobin in meat results in the water molecule at the sixth coordination site being replaced by a protein-bound ligand. On rehydration, this ligand may be replaced by water to reform metmyoglobin, but the degree of conversion depends on the rate of rehydration.The spectral similarity between cooked and freeze dried, oxidised meat indicates that the haematin environments are similar. It is suggested that in these meats the predominant pigments are di-imidazole complexes. | ||
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(DE-627)NLEJ188727043 (DE-599)GBVNLZ188727043 DE-627 ger DE-627 rakwb eng A note on the nature of the haematin pigments present in freeze dried and cooked beef 1987 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Analysis of the reflectance spectra of beef samples treated to contain all the haemoproteins in one pigment form indicated that little or no change in the haematin environment occurs on freeze drying fresh, oxymyoglobin-rich meat or cooked meat. Dehydration of metmyoglobin in meat results in the water molecule at the sixth coordination site being replaced by a protein-bound ligand. On rehydration, this ligand may be replaced by water to reform metmyoglobin, but the degree of conversion depends on the rate of rehydration.The spectral similarity between cooked and freeze dried, oxidised meat indicates that the haematin environments are similar. It is suggested that in these meats the predominant pigments are di-imidazole complexes. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Ledward, D.A. oth in Meat Science Amsterdam : Elsevier 21(1987), 3, Seite 231-237 (DE-627)NLEJ176928758 (DE-600)1491973-4 0309-1740 nnns volume:21 year:1987 number:3 pages:231-237 http://dx.doi.org/10.1016/0309-1740(87)90092-1 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 21 1987 3 231-237 |
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(DE-627)NLEJ188727043 (DE-599)GBVNLZ188727043 DE-627 ger DE-627 rakwb eng A note on the nature of the haematin pigments present in freeze dried and cooked beef 1987 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Analysis of the reflectance spectra of beef samples treated to contain all the haemoproteins in one pigment form indicated that little or no change in the haematin environment occurs on freeze drying fresh, oxymyoglobin-rich meat or cooked meat. Dehydration of metmyoglobin in meat results in the water molecule at the sixth coordination site being replaced by a protein-bound ligand. On rehydration, this ligand may be replaced by water to reform metmyoglobin, but the degree of conversion depends on the rate of rehydration.The spectral similarity between cooked and freeze dried, oxidised meat indicates that the haematin environments are similar. It is suggested that in these meats the predominant pigments are di-imidazole complexes. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Ledward, D.A. oth in Meat Science Amsterdam : Elsevier 21(1987), 3, Seite 231-237 (DE-627)NLEJ176928758 (DE-600)1491973-4 0309-1740 nnns volume:21 year:1987 number:3 pages:231-237 http://dx.doi.org/10.1016/0309-1740(87)90092-1 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 21 1987 3 231-237 |
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(DE-627)NLEJ188727043 (DE-599)GBVNLZ188727043 DE-627 ger DE-627 rakwb eng A note on the nature of the haematin pigments present in freeze dried and cooked beef 1987 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Analysis of the reflectance spectra of beef samples treated to contain all the haemoproteins in one pigment form indicated that little or no change in the haematin environment occurs on freeze drying fresh, oxymyoglobin-rich meat or cooked meat. Dehydration of metmyoglobin in meat results in the water molecule at the sixth coordination site being replaced by a protein-bound ligand. On rehydration, this ligand may be replaced by water to reform metmyoglobin, but the degree of conversion depends on the rate of rehydration.The spectral similarity between cooked and freeze dried, oxidised meat indicates that the haematin environments are similar. It is suggested that in these meats the predominant pigments are di-imidazole complexes. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Ledward, D.A. oth in Meat Science Amsterdam : Elsevier 21(1987), 3, Seite 231-237 (DE-627)NLEJ176928758 (DE-600)1491973-4 0309-1740 nnns volume:21 year:1987 number:3 pages:231-237 http://dx.doi.org/10.1016/0309-1740(87)90092-1 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 21 1987 3 231-237 |
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(DE-627)NLEJ188727043 (DE-599)GBVNLZ188727043 DE-627 ger DE-627 rakwb eng A note on the nature of the haematin pigments present in freeze dried and cooked beef 1987 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Analysis of the reflectance spectra of beef samples treated to contain all the haemoproteins in one pigment form indicated that little or no change in the haematin environment occurs on freeze drying fresh, oxymyoglobin-rich meat or cooked meat. Dehydration of metmyoglobin in meat results in the water molecule at the sixth coordination site being replaced by a protein-bound ligand. On rehydration, this ligand may be replaced by water to reform metmyoglobin, but the degree of conversion depends on the rate of rehydration.The spectral similarity between cooked and freeze dried, oxidised meat indicates that the haematin environments are similar. It is suggested that in these meats the predominant pigments are di-imidazole complexes. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Ledward, D.A. oth in Meat Science Amsterdam : Elsevier 21(1987), 3, Seite 231-237 (DE-627)NLEJ176928758 (DE-600)1491973-4 0309-1740 nnns volume:21 year:1987 number:3 pages:231-237 http://dx.doi.org/10.1016/0309-1740(87)90092-1 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 21 1987 3 231-237 |
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note on the nature of the haematin pigments present in freeze dried and cooked beef |
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A note on the nature of the haematin pigments present in freeze dried and cooked beef |
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Analysis of the reflectance spectra of beef samples treated to contain all the haemoproteins in one pigment form indicated that little or no change in the haematin environment occurs on freeze drying fresh, oxymyoglobin-rich meat or cooked meat. Dehydration of metmyoglobin in meat results in the water molecule at the sixth coordination site being replaced by a protein-bound ligand. On rehydration, this ligand may be replaced by water to reform metmyoglobin, but the degree of conversion depends on the rate of rehydration.The spectral similarity between cooked and freeze dried, oxidised meat indicates that the haematin environments are similar. It is suggested that in these meats the predominant pigments are di-imidazole complexes. |
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Analysis of the reflectance spectra of beef samples treated to contain all the haemoproteins in one pigment form indicated that little or no change in the haematin environment occurs on freeze drying fresh, oxymyoglobin-rich meat or cooked meat. Dehydration of metmyoglobin in meat results in the water molecule at the sixth coordination site being replaced by a protein-bound ligand. On rehydration, this ligand may be replaced by water to reform metmyoglobin, but the degree of conversion depends on the rate of rehydration.The spectral similarity between cooked and freeze dried, oxidised meat indicates that the haematin environments are similar. It is suggested that in these meats the predominant pigments are di-imidazole complexes. |
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Analysis of the reflectance spectra of beef samples treated to contain all the haemoproteins in one pigment form indicated that little or no change in the haematin environment occurs on freeze drying fresh, oxymyoglobin-rich meat or cooked meat. Dehydration of metmyoglobin in meat results in the water molecule at the sixth coordination site being replaced by a protein-bound ligand. On rehydration, this ligand may be replaced by water to reform metmyoglobin, but the degree of conversion depends on the rate of rehydration.The spectral similarity between cooked and freeze dried, oxidised meat indicates that the haematin environments are similar. It is suggested that in these meats the predominant pigments are di-imidazole complexes. |
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