Effect of amidation on the foaming and physico-chemical properties of bovine serum albumin
Amidation of bovine serum albumin (BSA) was achieved by a water-soluble carbo-diimide, ethyl-3-(3-dimethylaminopropyl) carbodiimide (EDC)-mediated reaction using ammonium chloride as the nucleophile. Partial and substantial amidation of 0.5% (w/v) BSA in 5.5 m ammonium chloride solution with 1 times...
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| Autor*in: |
HOWELL, NAZLIN K. [verfasserIn] TAYLOR, CLAIRE [verfasserIn] |
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| Format: |
E-Artikel |
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| Erschienen: |
Oxford, UK: Blackwell Publishing Ltd ; 1991 |
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| Umfang: |
Online-Ressource |
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| Reproduktion: |
2007 ; Blackwell Publishing Journal Backfiles 1879-2005 |
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| Übergeordnetes Werk: |
In: International journal of food science & technology - Oxford [u.a.] : Wiley-Blackwell, 1987, 26(1991), 4, Seite 0 |
| Übergeordnetes Werk: |
volume:26 ; year:1991 ; number:4 ; pages:0 |
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| DOI / URN: |
10.1111/j.1365-2621.1991.tb01981.x |
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| 520 | |a Amidation of bovine serum albumin (BSA) was achieved by a water-soluble carbo-diimide, ethyl-3-(3-dimethylaminopropyl) carbodiimide (EDC)-mediated reaction using ammonium chloride as the nucleophile. Partial and substantial amidation of 0.5% (w/v) BSA in 5.5 m ammonium chloride solution with 1 times 10-2mmol EDC over 120 min and 1 times 10-1mmol EDC over 10 min respectively was achieved on a large scale using diafiltration for rapid termination of the reaction and purification. Residual ammonium chloride otherwise enhanced foaming properties. The amidated proteins were characterized by isoelectric focusing, electrophoresis and hydrophobicity and disulphide- and sulphydryl-group measurements. Compared with native BSA, partially amidated BSA (PA-BSA) produced enhanced foam expansion and foam stability values. This was attributed to minimal denaturation and to the presence of both acidic and basic components (pI range 5.25–7.50) within the single protein. In contrast, substantially amidated BSA (SA-BSA) (pI range 7–9.1) had similar foaming properties to those of the ultrafiltered BSA control which were slightly lower than those of native BSA. However SA-BSA interacted synergistically with native BSA producing enhanced foaming properties particularly at the 1:1 ratio through electrostatic interactions, conformational changes and increased hydrophobicity. | ||
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10.1111/j.1365-2621.1991.tb01981.x doi (DE-627)NLEJ239420136 DE-627 ger DE-627 rakwb HOWELL, NAZLIN K. verfasserin aut Effect of amidation on the foaming and physico-chemical properties of bovine serum albumin Oxford, UK Blackwell Publishing Ltd 1991 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Amidation of bovine serum albumin (BSA) was achieved by a water-soluble carbo-diimide, ethyl-3-(3-dimethylaminopropyl) carbodiimide (EDC)-mediated reaction using ammonium chloride as the nucleophile. Partial and substantial amidation of 0.5% (w/v) BSA in 5.5 m ammonium chloride solution with 1 times 10-2mmol EDC over 120 min and 1 times 10-1mmol EDC over 10 min respectively was achieved on a large scale using diafiltration for rapid termination of the reaction and purification. Residual ammonium chloride otherwise enhanced foaming properties. The amidated proteins were characterized by isoelectric focusing, electrophoresis and hydrophobicity and disulphide- and sulphydryl-group measurements. Compared with native BSA, partially amidated BSA (PA-BSA) produced enhanced foam expansion and foam stability values. This was attributed to minimal denaturation and to the presence of both acidic and basic components (pI range 5.25–7.50) within the single protein. In contrast, substantially amidated BSA (SA-BSA) (pI range 7–9.1) had similar foaming properties to those of the ultrafiltered BSA control which were slightly lower than those of native BSA. However SA-BSA interacted synergistically with native BSA producing enhanced foaming properties particularly at the 1:1 ratio through electrostatic interactions, conformational changes and increased hydrophobicity. 2007 Blackwell Publishing Journal Backfiles 1879-2005 |2007|||||||||| Chemical modification of protein TAYLOR, CLAIRE verfasserin aut In International journal of food science & technology Oxford [u.a.] : Wiley-Blackwell, 1987 26(1991), 4, Seite 0 Online-Ressource (DE-627)NLEJ243926502 (DE-600)2016518-3 1365-2621 nnns volume:26 year:1991 number:4 pages:0 http://dx.doi.org/10.1111/j.1365-2621.1991.tb01981.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 26 1991 4 0 |
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10.1111/j.1365-2621.1991.tb01981.x doi (DE-627)NLEJ239420136 DE-627 ger DE-627 rakwb HOWELL, NAZLIN K. verfasserin aut Effect of amidation on the foaming and physico-chemical properties of bovine serum albumin Oxford, UK Blackwell Publishing Ltd 1991 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Amidation of bovine serum albumin (BSA) was achieved by a water-soluble carbo-diimide, ethyl-3-(3-dimethylaminopropyl) carbodiimide (EDC)-mediated reaction using ammonium chloride as the nucleophile. Partial and substantial amidation of 0.5% (w/v) BSA in 5.5 m ammonium chloride solution with 1 times 10-2mmol EDC over 120 min and 1 times 10-1mmol EDC over 10 min respectively was achieved on a large scale using diafiltration for rapid termination of the reaction and purification. Residual ammonium chloride otherwise enhanced foaming properties. The amidated proteins were characterized by isoelectric focusing, electrophoresis and hydrophobicity and disulphide- and sulphydryl-group measurements. Compared with native BSA, partially amidated BSA (PA-BSA) produced enhanced foam expansion and foam stability values. This was attributed to minimal denaturation and to the presence of both acidic and basic components (pI range 5.25–7.50) within the single protein. In contrast, substantially amidated BSA (SA-BSA) (pI range 7–9.1) had similar foaming properties to those of the ultrafiltered BSA control which were slightly lower than those of native BSA. However SA-BSA interacted synergistically with native BSA producing enhanced foaming properties particularly at the 1:1 ratio through electrostatic interactions, conformational changes and increased hydrophobicity. 2007 Blackwell Publishing Journal Backfiles 1879-2005 |2007|||||||||| Chemical modification of protein TAYLOR, CLAIRE verfasserin aut In International journal of food science & technology Oxford [u.a.] : Wiley-Blackwell, 1987 26(1991), 4, Seite 0 Online-Ressource (DE-627)NLEJ243926502 (DE-600)2016518-3 1365-2621 nnns volume:26 year:1991 number:4 pages:0 http://dx.doi.org/10.1111/j.1365-2621.1991.tb01981.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 26 1991 4 0 |
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10.1111/j.1365-2621.1991.tb01981.x doi (DE-627)NLEJ239420136 DE-627 ger DE-627 rakwb HOWELL, NAZLIN K. verfasserin aut Effect of amidation on the foaming and physico-chemical properties of bovine serum albumin Oxford, UK Blackwell Publishing Ltd 1991 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Amidation of bovine serum albumin (BSA) was achieved by a water-soluble carbo-diimide, ethyl-3-(3-dimethylaminopropyl) carbodiimide (EDC)-mediated reaction using ammonium chloride as the nucleophile. Partial and substantial amidation of 0.5% (w/v) BSA in 5.5 m ammonium chloride solution with 1 times 10-2mmol EDC over 120 min and 1 times 10-1mmol EDC over 10 min respectively was achieved on a large scale using diafiltration for rapid termination of the reaction and purification. Residual ammonium chloride otherwise enhanced foaming properties. The amidated proteins were characterized by isoelectric focusing, electrophoresis and hydrophobicity and disulphide- and sulphydryl-group measurements. Compared with native BSA, partially amidated BSA (PA-BSA) produced enhanced foam expansion and foam stability values. This was attributed to minimal denaturation and to the presence of both acidic and basic components (pI range 5.25–7.50) within the single protein. In contrast, substantially amidated BSA (SA-BSA) (pI range 7–9.1) had similar foaming properties to those of the ultrafiltered BSA control which were slightly lower than those of native BSA. However SA-BSA interacted synergistically with native BSA producing enhanced foaming properties particularly at the 1:1 ratio through electrostatic interactions, conformational changes and increased hydrophobicity. 2007 Blackwell Publishing Journal Backfiles 1879-2005 |2007|||||||||| Chemical modification of protein TAYLOR, CLAIRE verfasserin aut In International journal of food science & technology Oxford [u.a.] : Wiley-Blackwell, 1987 26(1991), 4, Seite 0 Online-Ressource (DE-627)NLEJ243926502 (DE-600)2016518-3 1365-2621 nnns volume:26 year:1991 number:4 pages:0 http://dx.doi.org/10.1111/j.1365-2621.1991.tb01981.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 26 1991 4 0 |
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10.1111/j.1365-2621.1991.tb01981.x doi (DE-627)NLEJ239420136 DE-627 ger DE-627 rakwb HOWELL, NAZLIN K. verfasserin aut Effect of amidation on the foaming and physico-chemical properties of bovine serum albumin Oxford, UK Blackwell Publishing Ltd 1991 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Amidation of bovine serum albumin (BSA) was achieved by a water-soluble carbo-diimide, ethyl-3-(3-dimethylaminopropyl) carbodiimide (EDC)-mediated reaction using ammonium chloride as the nucleophile. Partial and substantial amidation of 0.5% (w/v) BSA in 5.5 m ammonium chloride solution with 1 times 10-2mmol EDC over 120 min and 1 times 10-1mmol EDC over 10 min respectively was achieved on a large scale using diafiltration for rapid termination of the reaction and purification. Residual ammonium chloride otherwise enhanced foaming properties. The amidated proteins were characterized by isoelectric focusing, electrophoresis and hydrophobicity and disulphide- and sulphydryl-group measurements. Compared with native BSA, partially amidated BSA (PA-BSA) produced enhanced foam expansion and foam stability values. This was attributed to minimal denaturation and to the presence of both acidic and basic components (pI range 5.25–7.50) within the single protein. In contrast, substantially amidated BSA (SA-BSA) (pI range 7–9.1) had similar foaming properties to those of the ultrafiltered BSA control which were slightly lower than those of native BSA. However SA-BSA interacted synergistically with native BSA producing enhanced foaming properties particularly at the 1:1 ratio through electrostatic interactions, conformational changes and increased hydrophobicity. 2007 Blackwell Publishing Journal Backfiles 1879-2005 |2007|||||||||| Chemical modification of protein TAYLOR, CLAIRE verfasserin aut In International journal of food science & technology Oxford [u.a.] : Wiley-Blackwell, 1987 26(1991), 4, Seite 0 Online-Ressource (DE-627)NLEJ243926502 (DE-600)2016518-3 1365-2621 nnns volume:26 year:1991 number:4 pages:0 http://dx.doi.org/10.1111/j.1365-2621.1991.tb01981.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 26 1991 4 0 |
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10.1111/j.1365-2621.1991.tb01981.x doi (DE-627)NLEJ239420136 DE-627 ger DE-627 rakwb HOWELL, NAZLIN K. verfasserin aut Effect of amidation on the foaming and physico-chemical properties of bovine serum albumin Oxford, UK Blackwell Publishing Ltd 1991 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Amidation of bovine serum albumin (BSA) was achieved by a water-soluble carbo-diimide, ethyl-3-(3-dimethylaminopropyl) carbodiimide (EDC)-mediated reaction using ammonium chloride as the nucleophile. Partial and substantial amidation of 0.5% (w/v) BSA in 5.5 m ammonium chloride solution with 1 times 10-2mmol EDC over 120 min and 1 times 10-1mmol EDC over 10 min respectively was achieved on a large scale using diafiltration for rapid termination of the reaction and purification. Residual ammonium chloride otherwise enhanced foaming properties. The amidated proteins were characterized by isoelectric focusing, electrophoresis and hydrophobicity and disulphide- and sulphydryl-group measurements. Compared with native BSA, partially amidated BSA (PA-BSA) produced enhanced foam expansion and foam stability values. This was attributed to minimal denaturation and to the presence of both acidic and basic components (pI range 5.25–7.50) within the single protein. In contrast, substantially amidated BSA (SA-BSA) (pI range 7–9.1) had similar foaming properties to those of the ultrafiltered BSA control which were slightly lower than those of native BSA. However SA-BSA interacted synergistically with native BSA producing enhanced foaming properties particularly at the 1:1 ratio through electrostatic interactions, conformational changes and increased hydrophobicity. 2007 Blackwell Publishing Journal Backfiles 1879-2005 |2007|||||||||| Chemical modification of protein TAYLOR, CLAIRE verfasserin aut In International journal of food science & technology Oxford [u.a.] : Wiley-Blackwell, 1987 26(1991), 4, Seite 0 Online-Ressource (DE-627)NLEJ243926502 (DE-600)2016518-3 1365-2621 nnns volume:26 year:1991 number:4 pages:0 http://dx.doi.org/10.1111/j.1365-2621.1991.tb01981.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 26 1991 4 0 |
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effect of amidation on the foaming and physico-chemical properties of bovine serum albumin |
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Effect of amidation on the foaming and physico-chemical properties of bovine serum albumin |
| abstract |
Amidation of bovine serum albumin (BSA) was achieved by a water-soluble carbo-diimide, ethyl-3-(3-dimethylaminopropyl) carbodiimide (EDC)-mediated reaction using ammonium chloride as the nucleophile. Partial and substantial amidation of 0.5% (w/v) BSA in 5.5 m ammonium chloride solution with 1 times 10-2mmol EDC over 120 min and 1 times 10-1mmol EDC over 10 min respectively was achieved on a large scale using diafiltration for rapid termination of the reaction and purification. Residual ammonium chloride otherwise enhanced foaming properties. The amidated proteins were characterized by isoelectric focusing, electrophoresis and hydrophobicity and disulphide- and sulphydryl-group measurements. Compared with native BSA, partially amidated BSA (PA-BSA) produced enhanced foam expansion and foam stability values. This was attributed to minimal denaturation and to the presence of both acidic and basic components (pI range 5.25–7.50) within the single protein. In contrast, substantially amidated BSA (SA-BSA) (pI range 7–9.1) had similar foaming properties to those of the ultrafiltered BSA control which were slightly lower than those of native BSA. However SA-BSA interacted synergistically with native BSA producing enhanced foaming properties particularly at the 1:1 ratio through electrostatic interactions, conformational changes and increased hydrophobicity. |
| abstractGer |
Amidation of bovine serum albumin (BSA) was achieved by a water-soluble carbo-diimide, ethyl-3-(3-dimethylaminopropyl) carbodiimide (EDC)-mediated reaction using ammonium chloride as the nucleophile. Partial and substantial amidation of 0.5% (w/v) BSA in 5.5 m ammonium chloride solution with 1 times 10-2mmol EDC over 120 min and 1 times 10-1mmol EDC over 10 min respectively was achieved on a large scale using diafiltration for rapid termination of the reaction and purification. Residual ammonium chloride otherwise enhanced foaming properties. The amidated proteins were characterized by isoelectric focusing, electrophoresis and hydrophobicity and disulphide- and sulphydryl-group measurements. Compared with native BSA, partially amidated BSA (PA-BSA) produced enhanced foam expansion and foam stability values. This was attributed to minimal denaturation and to the presence of both acidic and basic components (pI range 5.25–7.50) within the single protein. In contrast, substantially amidated BSA (SA-BSA) (pI range 7–9.1) had similar foaming properties to those of the ultrafiltered BSA control which were slightly lower than those of native BSA. However SA-BSA interacted synergistically with native BSA producing enhanced foaming properties particularly at the 1:1 ratio through electrostatic interactions, conformational changes and increased hydrophobicity. |
| abstract_unstemmed |
Amidation of bovine serum albumin (BSA) was achieved by a water-soluble carbo-diimide, ethyl-3-(3-dimethylaminopropyl) carbodiimide (EDC)-mediated reaction using ammonium chloride as the nucleophile. Partial and substantial amidation of 0.5% (w/v) BSA in 5.5 m ammonium chloride solution with 1 times 10-2mmol EDC over 120 min and 1 times 10-1mmol EDC over 10 min respectively was achieved on a large scale using diafiltration for rapid termination of the reaction and purification. Residual ammonium chloride otherwise enhanced foaming properties. The amidated proteins were characterized by isoelectric focusing, electrophoresis and hydrophobicity and disulphide- and sulphydryl-group measurements. Compared with native BSA, partially amidated BSA (PA-BSA) produced enhanced foam expansion and foam stability values. This was attributed to minimal denaturation and to the presence of both acidic and basic components (pI range 5.25–7.50) within the single protein. In contrast, substantially amidated BSA (SA-BSA) (pI range 7–9.1) had similar foaming properties to those of the ultrafiltered BSA control which were slightly lower than those of native BSA. However SA-BSA interacted synergistically with native BSA producing enhanced foaming properties particularly at the 1:1 ratio through electrostatic interactions, conformational changes and increased hydrophobicity. |
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Effect of amidation on the foaming and physico-chemical properties of bovine serum albumin |
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