Gelation of shark myofibrillar proteins by weak organic acids
Washed, collagen-free shark muscle protein dispersions in water formed gels associated with an increase in viscosity when the pH was lowered to 4.5 by either acetic acid or lactic acid, while citric, tartaric and hydrochloric acids were ineffective in causing the gelation and viscosity rises. The in...
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| Autor*in: |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1994 |
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| Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
|---|---|
| Übergeordnetes Werk: |
in: Food Chemistry - Amsterdam : Elsevier, 50(1994), 2, Seite 185-190 |
| Übergeordnetes Werk: |
volume:50 ; year:1994 ; number:2 ; pages:185-190 |
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NLEJ188684611 |
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| 520 | |a Washed, collagen-free shark muscle protein dispersions in water formed gels associated with an increase in viscosity when the pH was lowered to 4.5 by either acetic acid or lactic acid, while citric, tartaric and hydrochloric acids were ineffective in causing the gelation and viscosity rises. The increase in viscosity, as measured by the Brabender viscograph, was dependent upon the protein concentration and was a slow process at ambient temperature. Heating of the acidified proteins up to 50^oC enhanced the viscosity, while at higher temperatures the gel broke as indicated by a rapid fall in viscosity as well as separation of water. The presence of NaCl, KCl and CaCl"2 inhibited the low-pH-induced gelation of the proteins. | ||
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(DE-627)NLEJ188684611 (DE-599)GBVNLZ188684611 DE-627 ger DE-627 rakwb eng Gelation of shark myofibrillar proteins by weak organic acids 1994 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Washed, collagen-free shark muscle protein dispersions in water formed gels associated with an increase in viscosity when the pH was lowered to 4.5 by either acetic acid or lactic acid, while citric, tartaric and hydrochloric acids were ineffective in causing the gelation and viscosity rises. The increase in viscosity, as measured by the Brabender viscograph, was dependent upon the protein concentration and was a slow process at ambient temperature. Heating of the acidified proteins up to 50^oC enhanced the viscosity, while at higher temperatures the gel broke as indicated by a rapid fall in viscosity as well as separation of water. The presence of NaCl, KCl and CaCl"2 inhibited the low-pH-induced gelation of the proteins. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Venugopal, V. oth Doke, S.N. oth Nair, P.M. oth in Food Chemistry Amsterdam : Elsevier 50(1994), 2, Seite 185-190 (DE-627)NLEJ18868154X (DE-600)1483647-6 0308-8146 nnns volume:50 year:1994 number:2 pages:185-190 http://dx.doi.org/10.1016/0308-8146(94)90118-X GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 50 1994 2 185-190 |
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(DE-627)NLEJ188684611 (DE-599)GBVNLZ188684611 DE-627 ger DE-627 rakwb eng Gelation of shark myofibrillar proteins by weak organic acids 1994 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Washed, collagen-free shark muscle protein dispersions in water formed gels associated with an increase in viscosity when the pH was lowered to 4.5 by either acetic acid or lactic acid, while citric, tartaric and hydrochloric acids were ineffective in causing the gelation and viscosity rises. The increase in viscosity, as measured by the Brabender viscograph, was dependent upon the protein concentration and was a slow process at ambient temperature. Heating of the acidified proteins up to 50^oC enhanced the viscosity, while at higher temperatures the gel broke as indicated by a rapid fall in viscosity as well as separation of water. The presence of NaCl, KCl and CaCl"2 inhibited the low-pH-induced gelation of the proteins. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Venugopal, V. oth Doke, S.N. oth Nair, P.M. oth in Food Chemistry Amsterdam : Elsevier 50(1994), 2, Seite 185-190 (DE-627)NLEJ18868154X (DE-600)1483647-6 0308-8146 nnns volume:50 year:1994 number:2 pages:185-190 http://dx.doi.org/10.1016/0308-8146(94)90118-X GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 50 1994 2 185-190 |
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(DE-627)NLEJ188684611 (DE-599)GBVNLZ188684611 DE-627 ger DE-627 rakwb eng Gelation of shark myofibrillar proteins by weak organic acids 1994 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Washed, collagen-free shark muscle protein dispersions in water formed gels associated with an increase in viscosity when the pH was lowered to 4.5 by either acetic acid or lactic acid, while citric, tartaric and hydrochloric acids were ineffective in causing the gelation and viscosity rises. The increase in viscosity, as measured by the Brabender viscograph, was dependent upon the protein concentration and was a slow process at ambient temperature. Heating of the acidified proteins up to 50^oC enhanced the viscosity, while at higher temperatures the gel broke as indicated by a rapid fall in viscosity as well as separation of water. The presence of NaCl, KCl and CaCl"2 inhibited the low-pH-induced gelation of the proteins. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Venugopal, V. oth Doke, S.N. oth Nair, P.M. oth in Food Chemistry Amsterdam : Elsevier 50(1994), 2, Seite 185-190 (DE-627)NLEJ18868154X (DE-600)1483647-6 0308-8146 nnns volume:50 year:1994 number:2 pages:185-190 http://dx.doi.org/10.1016/0308-8146(94)90118-X GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 50 1994 2 185-190 |
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(DE-627)NLEJ188684611 (DE-599)GBVNLZ188684611 DE-627 ger DE-627 rakwb eng Gelation of shark myofibrillar proteins by weak organic acids 1994 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Washed, collagen-free shark muscle protein dispersions in water formed gels associated with an increase in viscosity when the pH was lowered to 4.5 by either acetic acid or lactic acid, while citric, tartaric and hydrochloric acids were ineffective in causing the gelation and viscosity rises. The increase in viscosity, as measured by the Brabender viscograph, was dependent upon the protein concentration and was a slow process at ambient temperature. Heating of the acidified proteins up to 50^oC enhanced the viscosity, while at higher temperatures the gel broke as indicated by a rapid fall in viscosity as well as separation of water. The presence of NaCl, KCl and CaCl"2 inhibited the low-pH-induced gelation of the proteins. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Venugopal, V. oth Doke, S.N. oth Nair, P.M. oth in Food Chemistry Amsterdam : Elsevier 50(1994), 2, Seite 185-190 (DE-627)NLEJ18868154X (DE-600)1483647-6 0308-8146 nnns volume:50 year:1994 number:2 pages:185-190 http://dx.doi.org/10.1016/0308-8146(94)90118-X GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 50 1994 2 185-190 |
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(DE-627)NLEJ188684611 (DE-599)GBVNLZ188684611 DE-627 ger DE-627 rakwb eng Gelation of shark myofibrillar proteins by weak organic acids 1994 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Washed, collagen-free shark muscle protein dispersions in water formed gels associated with an increase in viscosity when the pH was lowered to 4.5 by either acetic acid or lactic acid, while citric, tartaric and hydrochloric acids were ineffective in causing the gelation and viscosity rises. The increase in viscosity, as measured by the Brabender viscograph, was dependent upon the protein concentration and was a slow process at ambient temperature. Heating of the acidified proteins up to 50^oC enhanced the viscosity, while at higher temperatures the gel broke as indicated by a rapid fall in viscosity as well as separation of water. The presence of NaCl, KCl and CaCl"2 inhibited the low-pH-induced gelation of the proteins. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Venugopal, V. oth Doke, S.N. oth Nair, P.M. oth in Food Chemistry Amsterdam : Elsevier 50(1994), 2, Seite 185-190 (DE-627)NLEJ18868154X (DE-600)1483647-6 0308-8146 nnns volume:50 year:1994 number:2 pages:185-190 http://dx.doi.org/10.1016/0308-8146(94)90118-X GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 50 1994 2 185-190 |
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Gelation of shark myofibrillar proteins by weak organic acids |
| abstract |
Washed, collagen-free shark muscle protein dispersions in water formed gels associated with an increase in viscosity when the pH was lowered to 4.5 by either acetic acid or lactic acid, while citric, tartaric and hydrochloric acids were ineffective in causing the gelation and viscosity rises. The increase in viscosity, as measured by the Brabender viscograph, was dependent upon the protein concentration and was a slow process at ambient temperature. Heating of the acidified proteins up to 50^oC enhanced the viscosity, while at higher temperatures the gel broke as indicated by a rapid fall in viscosity as well as separation of water. The presence of NaCl, KCl and CaCl"2 inhibited the low-pH-induced gelation of the proteins. |
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Washed, collagen-free shark muscle protein dispersions in water formed gels associated with an increase in viscosity when the pH was lowered to 4.5 by either acetic acid or lactic acid, while citric, tartaric and hydrochloric acids were ineffective in causing the gelation and viscosity rises. The increase in viscosity, as measured by the Brabender viscograph, was dependent upon the protein concentration and was a slow process at ambient temperature. Heating of the acidified proteins up to 50^oC enhanced the viscosity, while at higher temperatures the gel broke as indicated by a rapid fall in viscosity as well as separation of water. The presence of NaCl, KCl and CaCl"2 inhibited the low-pH-induced gelation of the proteins. |
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Washed, collagen-free shark muscle protein dispersions in water formed gels associated with an increase in viscosity when the pH was lowered to 4.5 by either acetic acid or lactic acid, while citric, tartaric and hydrochloric acids were ineffective in causing the gelation and viscosity rises. The increase in viscosity, as measured by the Brabender viscograph, was dependent upon the protein concentration and was a slow process at ambient temperature. Heating of the acidified proteins up to 50^oC enhanced the viscosity, while at higher temperatures the gel broke as indicated by a rapid fall in viscosity as well as separation of water. The presence of NaCl, KCl and CaCl"2 inhibited the low-pH-induced gelation of the proteins. |
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