Comparison of microcalorimetry and haze formation to quantify the association of B-type procyanidins to poly-l-proline and bovine serum albumin
Though many different methods have been applied to protein-tannin interactions, divergent results are often reported. To better understand the origin of these differences, we compare here haze/aggregates formation and thermodynamic parameters occurring for protein-procyanidin interactions. Proteins...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Watrelot, Aude A. [verfasserIn] |
|---|
| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2015transfer abstract |
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| Schlagwörter: |
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| Umfang: |
7 |
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| Übergeordnetes Werk: |
Enthalten in: Assessment of urban identity through a matrix of cultural landscapes - Ziyaee, Maryam ELSEVIER, 2017, an official journal of the Swiss Society of Food Science and Technology (SGLWT/SOSSTA) and the International Union of Food Science and Technology (IUFoST), Amsterdam [u.a.] |
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| Übergeordnetes Werk: |
volume:63 ; year:2015 ; number:1 ; pages:376-382 ; extent:7 |
| Links: |
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| DOI / URN: |
10.1016/j.lwt.2015.03.064 |
|---|
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ELV024036404 |
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| 245 | 1 | 0 | |a Comparison of microcalorimetry and haze formation to quantify the association of B-type procyanidins to poly-l-proline and bovine serum albumin |
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| 520 | |a Though many different methods have been applied to protein-tannin interactions, divergent results are often reported. To better understand the origin of these differences, we compare here haze/aggregates formation and thermodynamic parameters occurring for protein-procyanidin interactions. Proteins well referenced for interaction with polyphenols, namely a polypeptide of extended structure that resembles salivary proteins (poly-l-proline (PLP) and a standard globular protein (bovine serum albumin (BSA)) were used. Flavan-3-ols of three degrees of polymerization were tested, (-)-epicatechin (EPI), a dimer (DP2) and a procyanidin (DP8). The interactions were tested in identical conditions for both methods. The association constants determined by isothermal titration calorimetry (expressed as constitutive unit) varied with the following scale: PLP-DP8 >> BSA-DP8 ≈ BSA-DP2 ≈ PLP-DP2 > BSA-EPI (no affinity detected for PLP-EPI). However aggregates formed more readily for highly polymerized procyanidins DP8 with BSA than with PLP, and the scale (with 10 mmol/L of constitutive unit of polyphenol and 0.07 mmol/L of proteins) was: BSA-DP8 > BSA-DP2 >> PLP-DP8 > PLP-DP2 ≈ PLP-EPI, with no haze formation for BSA-EPI. However the impact of polyphenol concentration on haze formation and precipitation was different for the two proteins. | ||
| 520 | |a Though many different methods have been applied to protein-tannin interactions, divergent results are often reported. To better understand the origin of these differences, we compare here haze/aggregates formation and thermodynamic parameters occurring for protein-procyanidin interactions. Proteins well referenced for interaction with polyphenols, namely a polypeptide of extended structure that resembles salivary proteins (poly-l-proline (PLP) and a standard globular protein (bovine serum albumin (BSA)) were used. Flavan-3-ols of three degrees of polymerization were tested, (-)-epicatechin (EPI), a dimer (DP2) and a procyanidin (DP8). The interactions were tested in identical conditions for both methods. The association constants determined by isothermal titration calorimetry (expressed as constitutive unit) varied with the following scale: PLP-DP8 >> BSA-DP8 ≈ BSA-DP2 ≈ PLP-DP2 > BSA-EPI (no affinity detected for PLP-EPI). However aggregates formed more readily for highly polymerized procyanidins DP8 with BSA than with PLP, and the scale (with 10 mmol/L of constitutive unit of polyphenol and 0.07 mmol/L of proteins) was: BSA-DP8 > BSA-DP2 >> PLP-DP8 > PLP-DP2 ≈ PLP-EPI, with no haze formation for BSA-EPI. However the impact of polyphenol concentration on haze formation and precipitation was different for the two proteins. | ||
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10.1016/j.lwt.2015.03.064 doi GBVA2015022000026.pica (DE-627)ELV024036404 (ELSEVIER)S0023-6438(15)00217-0 DE-627 ger DE-627 rakwb eng 660 660 DE-600 690 VZ 74.12 bkl 74.72 bkl Watrelot, Aude A. verfasserin aut Comparison of microcalorimetry and haze formation to quantify the association of B-type procyanidins to poly-l-proline and bovine serum albumin 2015transfer abstract 7 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Though many different methods have been applied to protein-tannin interactions, divergent results are often reported. To better understand the origin of these differences, we compare here haze/aggregates formation and thermodynamic parameters occurring for protein-procyanidin interactions. Proteins well referenced for interaction with polyphenols, namely a polypeptide of extended structure that resembles salivary proteins (poly-l-proline (PLP) and a standard globular protein (bovine serum albumin (BSA)) were used. Flavan-3-ols of three degrees of polymerization were tested, (-)-epicatechin (EPI), a dimer (DP2) and a procyanidin (DP8). The interactions were tested in identical conditions for both methods. The association constants determined by isothermal titration calorimetry (expressed as constitutive unit) varied with the following scale: PLP-DP8 >> BSA-DP8 ≈ BSA-DP2 ≈ PLP-DP2 > BSA-EPI (no affinity detected for PLP-EPI). However aggregates formed more readily for highly polymerized procyanidins DP8 with BSA than with PLP, and the scale (with 10 mmol/L of constitutive unit of polyphenol and 0.07 mmol/L of proteins) was: BSA-DP8 > BSA-DP2 >> PLP-DP8 > PLP-DP2 ≈ PLP-EPI, with no haze formation for BSA-EPI. However the impact of polyphenol concentration on haze formation and precipitation was different for the two proteins. Though many different methods have been applied to protein-tannin interactions, divergent results are often reported. To better understand the origin of these differences, we compare here haze/aggregates formation and thermodynamic parameters occurring for protein-procyanidin interactions. Proteins well referenced for interaction with polyphenols, namely a polypeptide of extended structure that resembles salivary proteins (poly-l-proline (PLP) and a standard globular protein (bovine serum albumin (BSA)) were used. Flavan-3-ols of three degrees of polymerization were tested, (-)-epicatechin (EPI), a dimer (DP2) and a procyanidin (DP8). The interactions were tested in identical conditions for both methods. The association constants determined by isothermal titration calorimetry (expressed as constitutive unit) varied with the following scale: PLP-DP8 >> BSA-DP8 ≈ BSA-DP2 ≈ PLP-DP2 > BSA-EPI (no affinity detected for PLP-EPI). However aggregates formed more readily for highly polymerized procyanidins DP8 with BSA than with PLP, and the scale (with 10 mmol/L of constitutive unit of polyphenol and 0.07 mmol/L of proteins) was: BSA-DP8 > BSA-DP2 >> PLP-DP8 > PLP-DP2 ≈ PLP-EPI, with no haze formation for BSA-EPI. However the impact of polyphenol concentration on haze formation and precipitation was different for the two proteins. Polyphenol Elsevier Affinity Elsevier ITC Elsevier Precipitate Elsevier Protein Elsevier Renard, Catherine M.G.C. oth Le Bourvellec, Carine oth Enthalten in Elsevier Ziyaee, Maryam ELSEVIER Assessment of urban identity through a matrix of cultural landscapes 2017 an official journal of the Swiss Society of Food Science and Technology (SGLWT/SOSSTA) and the International Union of Food Science and Technology (IUFoST) Amsterdam [u.a.] (DE-627)ELV004078675 volume:63 year:2015 number:1 pages:376-382 extent:7 https://doi.org/10.1016/j.lwt.2015.03.064 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OPC-GGO 74.12 Stadtgeographie Siedlungsgeographie VZ 74.72 Stadtplanung kommunale Planung VZ AR 63 2015 1 376-382 7 045F 660 |
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10.1016/j.lwt.2015.03.064 doi GBVA2015022000026.pica (DE-627)ELV024036404 (ELSEVIER)S0023-6438(15)00217-0 DE-627 ger DE-627 rakwb eng 660 660 DE-600 690 VZ 74.12 bkl 74.72 bkl Watrelot, Aude A. verfasserin aut Comparison of microcalorimetry and haze formation to quantify the association of B-type procyanidins to poly-l-proline and bovine serum albumin 2015transfer abstract 7 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Though many different methods have been applied to protein-tannin interactions, divergent results are often reported. To better understand the origin of these differences, we compare here haze/aggregates formation and thermodynamic parameters occurring for protein-procyanidin interactions. Proteins well referenced for interaction with polyphenols, namely a polypeptide of extended structure that resembles salivary proteins (poly-l-proline (PLP) and a standard globular protein (bovine serum albumin (BSA)) were used. Flavan-3-ols of three degrees of polymerization were tested, (-)-epicatechin (EPI), a dimer (DP2) and a procyanidin (DP8). The interactions were tested in identical conditions for both methods. The association constants determined by isothermal titration calorimetry (expressed as constitutive unit) varied with the following scale: PLP-DP8 >> BSA-DP8 ≈ BSA-DP2 ≈ PLP-DP2 > BSA-EPI (no affinity detected for PLP-EPI). However aggregates formed more readily for highly polymerized procyanidins DP8 with BSA than with PLP, and the scale (with 10 mmol/L of constitutive unit of polyphenol and 0.07 mmol/L of proteins) was: BSA-DP8 > BSA-DP2 >> PLP-DP8 > PLP-DP2 ≈ PLP-EPI, with no haze formation for BSA-EPI. However the impact of polyphenol concentration on haze formation and precipitation was different for the two proteins. Though many different methods have been applied to protein-tannin interactions, divergent results are often reported. To better understand the origin of these differences, we compare here haze/aggregates formation and thermodynamic parameters occurring for protein-procyanidin interactions. Proteins well referenced for interaction with polyphenols, namely a polypeptide of extended structure that resembles salivary proteins (poly-l-proline (PLP) and a standard globular protein (bovine serum albumin (BSA)) were used. Flavan-3-ols of three degrees of polymerization were tested, (-)-epicatechin (EPI), a dimer (DP2) and a procyanidin (DP8). The interactions were tested in identical conditions for both methods. The association constants determined by isothermal titration calorimetry (expressed as constitutive unit) varied with the following scale: PLP-DP8 >> BSA-DP8 ≈ BSA-DP2 ≈ PLP-DP2 > BSA-EPI (no affinity detected for PLP-EPI). However aggregates formed more readily for highly polymerized procyanidins DP8 with BSA than with PLP, and the scale (with 10 mmol/L of constitutive unit of polyphenol and 0.07 mmol/L of proteins) was: BSA-DP8 > BSA-DP2 >> PLP-DP8 > PLP-DP2 ≈ PLP-EPI, with no haze formation for BSA-EPI. However the impact of polyphenol concentration on haze formation and precipitation was different for the two proteins. Polyphenol Elsevier Affinity Elsevier ITC Elsevier Precipitate Elsevier Protein Elsevier Renard, Catherine M.G.C. oth Le Bourvellec, Carine oth Enthalten in Elsevier Ziyaee, Maryam ELSEVIER Assessment of urban identity through a matrix of cultural landscapes 2017 an official journal of the Swiss Society of Food Science and Technology (SGLWT/SOSSTA) and the International Union of Food Science and Technology (IUFoST) Amsterdam [u.a.] (DE-627)ELV004078675 volume:63 year:2015 number:1 pages:376-382 extent:7 https://doi.org/10.1016/j.lwt.2015.03.064 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OPC-GGO 74.12 Stadtgeographie Siedlungsgeographie VZ 74.72 Stadtplanung kommunale Planung VZ AR 63 2015 1 376-382 7 045F 660 |
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10.1016/j.lwt.2015.03.064 doi GBVA2015022000026.pica (DE-627)ELV024036404 (ELSEVIER)S0023-6438(15)00217-0 DE-627 ger DE-627 rakwb eng 660 660 DE-600 690 VZ 74.12 bkl 74.72 bkl Watrelot, Aude A. verfasserin aut Comparison of microcalorimetry and haze formation to quantify the association of B-type procyanidins to poly-l-proline and bovine serum albumin 2015transfer abstract 7 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Though many different methods have been applied to protein-tannin interactions, divergent results are often reported. To better understand the origin of these differences, we compare here haze/aggregates formation and thermodynamic parameters occurring for protein-procyanidin interactions. Proteins well referenced for interaction with polyphenols, namely a polypeptide of extended structure that resembles salivary proteins (poly-l-proline (PLP) and a standard globular protein (bovine serum albumin (BSA)) were used. Flavan-3-ols of three degrees of polymerization were tested, (-)-epicatechin (EPI), a dimer (DP2) and a procyanidin (DP8). The interactions were tested in identical conditions for both methods. The association constants determined by isothermal titration calorimetry (expressed as constitutive unit) varied with the following scale: PLP-DP8 >> BSA-DP8 ≈ BSA-DP2 ≈ PLP-DP2 > BSA-EPI (no affinity detected for PLP-EPI). However aggregates formed more readily for highly polymerized procyanidins DP8 with BSA than with PLP, and the scale (with 10 mmol/L of constitutive unit of polyphenol and 0.07 mmol/L of proteins) was: BSA-DP8 > BSA-DP2 >> PLP-DP8 > PLP-DP2 ≈ PLP-EPI, with no haze formation for BSA-EPI. However the impact of polyphenol concentration on haze formation and precipitation was different for the two proteins. Though many different methods have been applied to protein-tannin interactions, divergent results are often reported. To better understand the origin of these differences, we compare here haze/aggregates formation and thermodynamic parameters occurring for protein-procyanidin interactions. Proteins well referenced for interaction with polyphenols, namely a polypeptide of extended structure that resembles salivary proteins (poly-l-proline (PLP) and a standard globular protein (bovine serum albumin (BSA)) were used. Flavan-3-ols of three degrees of polymerization were tested, (-)-epicatechin (EPI), a dimer (DP2) and a procyanidin (DP8). The interactions were tested in identical conditions for both methods. The association constants determined by isothermal titration calorimetry (expressed as constitutive unit) varied with the following scale: PLP-DP8 >> BSA-DP8 ≈ BSA-DP2 ≈ PLP-DP2 > BSA-EPI (no affinity detected for PLP-EPI). However aggregates formed more readily for highly polymerized procyanidins DP8 with BSA than with PLP, and the scale (with 10 mmol/L of constitutive unit of polyphenol and 0.07 mmol/L of proteins) was: BSA-DP8 > BSA-DP2 >> PLP-DP8 > PLP-DP2 ≈ PLP-EPI, with no haze formation for BSA-EPI. However the impact of polyphenol concentration on haze formation and precipitation was different for the two proteins. Polyphenol Elsevier Affinity Elsevier ITC Elsevier Precipitate Elsevier Protein Elsevier Renard, Catherine M.G.C. oth Le Bourvellec, Carine oth Enthalten in Elsevier Ziyaee, Maryam ELSEVIER Assessment of urban identity through a matrix of cultural landscapes 2017 an official journal of the Swiss Society of Food Science and Technology (SGLWT/SOSSTA) and the International Union of Food Science and Technology (IUFoST) Amsterdam [u.a.] (DE-627)ELV004078675 volume:63 year:2015 number:1 pages:376-382 extent:7 https://doi.org/10.1016/j.lwt.2015.03.064 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OPC-GGO 74.12 Stadtgeographie Siedlungsgeographie VZ 74.72 Stadtplanung kommunale Planung VZ AR 63 2015 1 376-382 7 045F 660 |
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10.1016/j.lwt.2015.03.064 doi GBVA2015022000026.pica (DE-627)ELV024036404 (ELSEVIER)S0023-6438(15)00217-0 DE-627 ger DE-627 rakwb eng 660 660 DE-600 690 VZ 74.12 bkl 74.72 bkl Watrelot, Aude A. verfasserin aut Comparison of microcalorimetry and haze formation to quantify the association of B-type procyanidins to poly-l-proline and bovine serum albumin 2015transfer abstract 7 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Though many different methods have been applied to protein-tannin interactions, divergent results are often reported. To better understand the origin of these differences, we compare here haze/aggregates formation and thermodynamic parameters occurring for protein-procyanidin interactions. Proteins well referenced for interaction with polyphenols, namely a polypeptide of extended structure that resembles salivary proteins (poly-l-proline (PLP) and a standard globular protein (bovine serum albumin (BSA)) were used. Flavan-3-ols of three degrees of polymerization were tested, (-)-epicatechin (EPI), a dimer (DP2) and a procyanidin (DP8). The interactions were tested in identical conditions for both methods. The association constants determined by isothermal titration calorimetry (expressed as constitutive unit) varied with the following scale: PLP-DP8 >> BSA-DP8 ≈ BSA-DP2 ≈ PLP-DP2 > BSA-EPI (no affinity detected for PLP-EPI). However aggregates formed more readily for highly polymerized procyanidins DP8 with BSA than with PLP, and the scale (with 10 mmol/L of constitutive unit of polyphenol and 0.07 mmol/L of proteins) was: BSA-DP8 > BSA-DP2 >> PLP-DP8 > PLP-DP2 ≈ PLP-EPI, with no haze formation for BSA-EPI. However the impact of polyphenol concentration on haze formation and precipitation was different for the two proteins. Though many different methods have been applied to protein-tannin interactions, divergent results are often reported. To better understand the origin of these differences, we compare here haze/aggregates formation and thermodynamic parameters occurring for protein-procyanidin interactions. Proteins well referenced for interaction with polyphenols, namely a polypeptide of extended structure that resembles salivary proteins (poly-l-proline (PLP) and a standard globular protein (bovine serum albumin (BSA)) were used. Flavan-3-ols of three degrees of polymerization were tested, (-)-epicatechin (EPI), a dimer (DP2) and a procyanidin (DP8). The interactions were tested in identical conditions for both methods. The association constants determined by isothermal titration calorimetry (expressed as constitutive unit) varied with the following scale: PLP-DP8 >> BSA-DP8 ≈ BSA-DP2 ≈ PLP-DP2 > BSA-EPI (no affinity detected for PLP-EPI). However aggregates formed more readily for highly polymerized procyanidins DP8 with BSA than with PLP, and the scale (with 10 mmol/L of constitutive unit of polyphenol and 0.07 mmol/L of proteins) was: BSA-DP8 > BSA-DP2 >> PLP-DP8 > PLP-DP2 ≈ PLP-EPI, with no haze formation for BSA-EPI. However the impact of polyphenol concentration on haze formation and precipitation was different for the two proteins. Polyphenol Elsevier Affinity Elsevier ITC Elsevier Precipitate Elsevier Protein Elsevier Renard, Catherine M.G.C. oth Le Bourvellec, Carine oth Enthalten in Elsevier Ziyaee, Maryam ELSEVIER Assessment of urban identity through a matrix of cultural landscapes 2017 an official journal of the Swiss Society of Food Science and Technology (SGLWT/SOSSTA) and the International Union of Food Science and Technology (IUFoST) Amsterdam [u.a.] (DE-627)ELV004078675 volume:63 year:2015 number:1 pages:376-382 extent:7 https://doi.org/10.1016/j.lwt.2015.03.064 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OPC-GGO 74.12 Stadtgeographie Siedlungsgeographie VZ 74.72 Stadtplanung kommunale Planung VZ AR 63 2015 1 376-382 7 045F 660 |
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10.1016/j.lwt.2015.03.064 doi GBVA2015022000026.pica (DE-627)ELV024036404 (ELSEVIER)S0023-6438(15)00217-0 DE-627 ger DE-627 rakwb eng 660 660 DE-600 690 VZ 74.12 bkl 74.72 bkl Watrelot, Aude A. verfasserin aut Comparison of microcalorimetry and haze formation to quantify the association of B-type procyanidins to poly-l-proline and bovine serum albumin 2015transfer abstract 7 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Though many different methods have been applied to protein-tannin interactions, divergent results are often reported. To better understand the origin of these differences, we compare here haze/aggregates formation and thermodynamic parameters occurring for protein-procyanidin interactions. Proteins well referenced for interaction with polyphenols, namely a polypeptide of extended structure that resembles salivary proteins (poly-l-proline (PLP) and a standard globular protein (bovine serum albumin (BSA)) were used. Flavan-3-ols of three degrees of polymerization were tested, (-)-epicatechin (EPI), a dimer (DP2) and a procyanidin (DP8). The interactions were tested in identical conditions for both methods. The association constants determined by isothermal titration calorimetry (expressed as constitutive unit) varied with the following scale: PLP-DP8 >> BSA-DP8 ≈ BSA-DP2 ≈ PLP-DP2 > BSA-EPI (no affinity detected for PLP-EPI). However aggregates formed more readily for highly polymerized procyanidins DP8 with BSA than with PLP, and the scale (with 10 mmol/L of constitutive unit of polyphenol and 0.07 mmol/L of proteins) was: BSA-DP8 > BSA-DP2 >> PLP-DP8 > PLP-DP2 ≈ PLP-EPI, with no haze formation for BSA-EPI. However the impact of polyphenol concentration on haze formation and precipitation was different for the two proteins. Though many different methods have been applied to protein-tannin interactions, divergent results are often reported. To better understand the origin of these differences, we compare here haze/aggregates formation and thermodynamic parameters occurring for protein-procyanidin interactions. Proteins well referenced for interaction with polyphenols, namely a polypeptide of extended structure that resembles salivary proteins (poly-l-proline (PLP) and a standard globular protein (bovine serum albumin (BSA)) were used. Flavan-3-ols of three degrees of polymerization were tested, (-)-epicatechin (EPI), a dimer (DP2) and a procyanidin (DP8). The interactions were tested in identical conditions for both methods. The association constants determined by isothermal titration calorimetry (expressed as constitutive unit) varied with the following scale: PLP-DP8 >> BSA-DP8 ≈ BSA-DP2 ≈ PLP-DP2 > BSA-EPI (no affinity detected for PLP-EPI). However aggregates formed more readily for highly polymerized procyanidins DP8 with BSA than with PLP, and the scale (with 10 mmol/L of constitutive unit of polyphenol and 0.07 mmol/L of proteins) was: BSA-DP8 > BSA-DP2 >> PLP-DP8 > PLP-DP2 ≈ PLP-EPI, with no haze formation for BSA-EPI. However the impact of polyphenol concentration on haze formation and precipitation was different for the two proteins. Polyphenol Elsevier Affinity Elsevier ITC Elsevier Precipitate Elsevier Protein Elsevier Renard, Catherine M.G.C. oth Le Bourvellec, Carine oth Enthalten in Elsevier Ziyaee, Maryam ELSEVIER Assessment of urban identity through a matrix of cultural landscapes 2017 an official journal of the Swiss Society of Food Science and Technology (SGLWT/SOSSTA) and the International Union of Food Science and Technology (IUFoST) Amsterdam [u.a.] (DE-627)ELV004078675 volume:63 year:2015 number:1 pages:376-382 extent:7 https://doi.org/10.1016/j.lwt.2015.03.064 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OPC-GGO 74.12 Stadtgeographie Siedlungsgeographie VZ 74.72 Stadtplanung kommunale Planung VZ AR 63 2015 1 376-382 7 045F 660 |
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comparison of microcalorimetry and haze formation to quantify the association of b-type procyanidins to poly-l-proline and bovine serum albumin |
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Comparison of microcalorimetry and haze formation to quantify the association of B-type procyanidins to poly-l-proline and bovine serum albumin |
| abstract |
Though many different methods have been applied to protein-tannin interactions, divergent results are often reported. To better understand the origin of these differences, we compare here haze/aggregates formation and thermodynamic parameters occurring for protein-procyanidin interactions. Proteins well referenced for interaction with polyphenols, namely a polypeptide of extended structure that resembles salivary proteins (poly-l-proline (PLP) and a standard globular protein (bovine serum albumin (BSA)) were used. Flavan-3-ols of three degrees of polymerization were tested, (-)-epicatechin (EPI), a dimer (DP2) and a procyanidin (DP8). The interactions were tested in identical conditions for both methods. The association constants determined by isothermal titration calorimetry (expressed as constitutive unit) varied with the following scale: PLP-DP8 >> BSA-DP8 ≈ BSA-DP2 ≈ PLP-DP2 > BSA-EPI (no affinity detected for PLP-EPI). However aggregates formed more readily for highly polymerized procyanidins DP8 with BSA than with PLP, and the scale (with 10 mmol/L of constitutive unit of polyphenol and 0.07 mmol/L of proteins) was: BSA-DP8 > BSA-DP2 >> PLP-DP8 > PLP-DP2 ≈ PLP-EPI, with no haze formation for BSA-EPI. However the impact of polyphenol concentration on haze formation and precipitation was different for the two proteins. |
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Though many different methods have been applied to protein-tannin interactions, divergent results are often reported. To better understand the origin of these differences, we compare here haze/aggregates formation and thermodynamic parameters occurring for protein-procyanidin interactions. Proteins well referenced for interaction with polyphenols, namely a polypeptide of extended structure that resembles salivary proteins (poly-l-proline (PLP) and a standard globular protein (bovine serum albumin (BSA)) were used. Flavan-3-ols of three degrees of polymerization were tested, (-)-epicatechin (EPI), a dimer (DP2) and a procyanidin (DP8). The interactions were tested in identical conditions for both methods. The association constants determined by isothermal titration calorimetry (expressed as constitutive unit) varied with the following scale: PLP-DP8 >> BSA-DP8 ≈ BSA-DP2 ≈ PLP-DP2 > BSA-EPI (no affinity detected for PLP-EPI). However aggregates formed more readily for highly polymerized procyanidins DP8 with BSA than with PLP, and the scale (with 10 mmol/L of constitutive unit of polyphenol and 0.07 mmol/L of proteins) was: BSA-DP8 > BSA-DP2 >> PLP-DP8 > PLP-DP2 ≈ PLP-EPI, with no haze formation for BSA-EPI. However the impact of polyphenol concentration on haze formation and precipitation was different for the two proteins. |
| abstract_unstemmed |
Though many different methods have been applied to protein-tannin interactions, divergent results are often reported. To better understand the origin of these differences, we compare here haze/aggregates formation and thermodynamic parameters occurring for protein-procyanidin interactions. Proteins well referenced for interaction with polyphenols, namely a polypeptide of extended structure that resembles salivary proteins (poly-l-proline (PLP) and a standard globular protein (bovine serum albumin (BSA)) were used. Flavan-3-ols of three degrees of polymerization were tested, (-)-epicatechin (EPI), a dimer (DP2) and a procyanidin (DP8). The interactions were tested in identical conditions for both methods. The association constants determined by isothermal titration calorimetry (expressed as constitutive unit) varied with the following scale: PLP-DP8 >> BSA-DP8 ≈ BSA-DP2 ≈ PLP-DP2 > BSA-EPI (no affinity detected for PLP-EPI). However aggregates formed more readily for highly polymerized procyanidins DP8 with BSA than with PLP, and the scale (with 10 mmol/L of constitutive unit of polyphenol and 0.07 mmol/L of proteins) was: BSA-DP8 > BSA-DP2 >> PLP-DP8 > PLP-DP2 ≈ PLP-EPI, with no haze formation for BSA-EPI. However the impact of polyphenol concentration on haze formation and precipitation was different for the two proteins. |
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