Self-association of caseinomacropeptide in presence of CaCl2 at neutral pH: Calcium binding determination
The caseinomacropeptide (CMP) is a bioactive peptide produced during cheese making. It is found in abundance in whey. CMP aqueous solutions allow the incorporation of large amounts of CaCl2 but the mechanism of calcium-CMP interactions are unknown. In order to evaluate its calcium binding capacity,...
Ausführliche Beschreibung
Autor*in: |
Loria, Karina G. [verfasserIn] |
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E-Artikel |
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Sprache: |
Englisch |
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2022transfer abstract |
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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:161 ; year:2022 ; day:1 ; month:05 ; pages:0 |
Links: |
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DOI / URN: |
10.1016/j.lwt.2022.113419 |
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Katalog-ID: |
ELV057457646 |
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520 | |a The caseinomacropeptide (CMP) is a bioactive peptide produced during cheese making. It is found in abundance in whey. CMP aqueous solutions allow the incorporation of large amounts of CaCl2 but the mechanism of calcium-CMP interactions are unknown. In order to evaluate its calcium binding capacity, the following techniques were performed: Dynamic Light Scattering (DLS), Fourier Transform Infrared spectroscopy (FTIR), dialysis, conductivity, precipitation of CaCl2/CMP complex by ethanol, electrochemical Ca2+ binding isotherms, and inhibition of calcium phosphate precipitation. One mole of CMP can bind 9 mol of calcium, and the CMP self-assembles as a hexameric form. A model is proposed to explain the CMP self-association in presence of CaCl2. | ||
520 | |a The caseinomacropeptide (CMP) is a bioactive peptide produced during cheese making. It is found in abundance in whey. CMP aqueous solutions allow the incorporation of large amounts of CaCl2 but the mechanism of calcium-CMP interactions are unknown. In order to evaluate its calcium binding capacity, the following techniques were performed: Dynamic Light Scattering (DLS), Fourier Transform Infrared spectroscopy (FTIR), dialysis, conductivity, precipitation of CaCl2/CMP complex by ethanol, electrochemical Ca2+ binding isotherms, and inhibition of calcium phosphate precipitation. One mole of CMP can bind 9 mol of calcium, and the CMP self-assembles as a hexameric form. A model is proposed to explain the CMP self-association in presence of CaCl2. | ||
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10.1016/j.lwt.2022.113419 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001744.pica (DE-627)ELV057457646 (ELSEVIER)S0023-6438(22)00354-1 DE-627 ger DE-627 rakwb eng 690 VZ 74.12 bkl 74.72 bkl Loria, Karina G. verfasserin aut Self-association of caseinomacropeptide in presence of CaCl2 at neutral pH: Calcium binding determination 2022transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The caseinomacropeptide (CMP) is a bioactive peptide produced during cheese making. It is found in abundance in whey. CMP aqueous solutions allow the incorporation of large amounts of CaCl2 but the mechanism of calcium-CMP interactions are unknown. In order to evaluate its calcium binding capacity, the following techniques were performed: Dynamic Light Scattering (DLS), Fourier Transform Infrared spectroscopy (FTIR), dialysis, conductivity, precipitation of CaCl2/CMP complex by ethanol, electrochemical Ca2+ binding isotherms, and inhibition of calcium phosphate precipitation. One mole of CMP can bind 9 mol of calcium, and the CMP self-assembles as a hexameric form. A model is proposed to explain the CMP self-association in presence of CaCl2. The caseinomacropeptide (CMP) is a bioactive peptide produced during cheese making. It is found in abundance in whey. CMP aqueous solutions allow the incorporation of large amounts of CaCl2 but the mechanism of calcium-CMP interactions are unknown. In order to evaluate its calcium binding capacity, the following techniques were performed: Dynamic Light Scattering (DLS), Fourier Transform Infrared spectroscopy (FTIR), dialysis, conductivity, precipitation of CaCl2/CMP complex by ethanol, electrochemical Ca2+ binding isotherms, and inhibition of calcium phosphate precipitation. One mole of CMP can bind 9 mol of calcium, and the CMP self-assembles as a hexameric form. A model is proposed to explain the CMP self-association in presence of CaCl2. Calcium binding isotherms Elsevier Self-assembly Elsevier Calcium binding peptides Elsevier Pilosof, Ana M.R. oth Farías, María E. 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:161 year:2022 day:1 month:05 pages:0 https://doi.org/10.1016/j.lwt.2022.113419 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OPC-GGO 74.12 Stadtgeographie Siedlungsgeographie VZ 74.72 Stadtplanung kommunale Planung VZ AR 161 2022 1 0501 0 |
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10.1016/j.lwt.2022.113419 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001744.pica (DE-627)ELV057457646 (ELSEVIER)S0023-6438(22)00354-1 DE-627 ger DE-627 rakwb eng 690 VZ 74.12 bkl 74.72 bkl Loria, Karina G. verfasserin aut Self-association of caseinomacropeptide in presence of CaCl2 at neutral pH: Calcium binding determination 2022transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The caseinomacropeptide (CMP) is a bioactive peptide produced during cheese making. It is found in abundance in whey. CMP aqueous solutions allow the incorporation of large amounts of CaCl2 but the mechanism of calcium-CMP interactions are unknown. In order to evaluate its calcium binding capacity, the following techniques were performed: Dynamic Light Scattering (DLS), Fourier Transform Infrared spectroscopy (FTIR), dialysis, conductivity, precipitation of CaCl2/CMP complex by ethanol, electrochemical Ca2+ binding isotherms, and inhibition of calcium phosphate precipitation. One mole of CMP can bind 9 mol of calcium, and the CMP self-assembles as a hexameric form. A model is proposed to explain the CMP self-association in presence of CaCl2. The caseinomacropeptide (CMP) is a bioactive peptide produced during cheese making. It is found in abundance in whey. CMP aqueous solutions allow the incorporation of large amounts of CaCl2 but the mechanism of calcium-CMP interactions are unknown. In order to evaluate its calcium binding capacity, the following techniques were performed: Dynamic Light Scattering (DLS), Fourier Transform Infrared spectroscopy (FTIR), dialysis, conductivity, precipitation of CaCl2/CMP complex by ethanol, electrochemical Ca2+ binding isotherms, and inhibition of calcium phosphate precipitation. One mole of CMP can bind 9 mol of calcium, and the CMP self-assembles as a hexameric form. A model is proposed to explain the CMP self-association in presence of CaCl2. Calcium binding isotherms Elsevier Self-assembly Elsevier Calcium binding peptides Elsevier Pilosof, Ana M.R. oth Farías, María E. 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:161 year:2022 day:1 month:05 pages:0 https://doi.org/10.1016/j.lwt.2022.113419 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OPC-GGO 74.12 Stadtgeographie Siedlungsgeographie VZ 74.72 Stadtplanung kommunale Planung VZ AR 161 2022 1 0501 0 |
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10.1016/j.lwt.2022.113419 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001744.pica (DE-627)ELV057457646 (ELSEVIER)S0023-6438(22)00354-1 DE-627 ger DE-627 rakwb eng 690 VZ 74.12 bkl 74.72 bkl Loria, Karina G. verfasserin aut Self-association of caseinomacropeptide in presence of CaCl2 at neutral pH: Calcium binding determination 2022transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The caseinomacropeptide (CMP) is a bioactive peptide produced during cheese making. It is found in abundance in whey. CMP aqueous solutions allow the incorporation of large amounts of CaCl2 but the mechanism of calcium-CMP interactions are unknown. In order to evaluate its calcium binding capacity, the following techniques were performed: Dynamic Light Scattering (DLS), Fourier Transform Infrared spectroscopy (FTIR), dialysis, conductivity, precipitation of CaCl2/CMP complex by ethanol, electrochemical Ca2+ binding isotherms, and inhibition of calcium phosphate precipitation. One mole of CMP can bind 9 mol of calcium, and the CMP self-assembles as a hexameric form. A model is proposed to explain the CMP self-association in presence of CaCl2. The caseinomacropeptide (CMP) is a bioactive peptide produced during cheese making. It is found in abundance in whey. CMP aqueous solutions allow the incorporation of large amounts of CaCl2 but the mechanism of calcium-CMP interactions are unknown. In order to evaluate its calcium binding capacity, the following techniques were performed: Dynamic Light Scattering (DLS), Fourier Transform Infrared spectroscopy (FTIR), dialysis, conductivity, precipitation of CaCl2/CMP complex by ethanol, electrochemical Ca2+ binding isotherms, and inhibition of calcium phosphate precipitation. One mole of CMP can bind 9 mol of calcium, and the CMP self-assembles as a hexameric form. A model is proposed to explain the CMP self-association in presence of CaCl2. Calcium binding isotherms Elsevier Self-assembly Elsevier Calcium binding peptides Elsevier Pilosof, Ana M.R. oth Farías, María E. 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:161 year:2022 day:1 month:05 pages:0 https://doi.org/10.1016/j.lwt.2022.113419 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OPC-GGO 74.12 Stadtgeographie Siedlungsgeographie VZ 74.72 Stadtplanung kommunale Planung VZ AR 161 2022 1 0501 0 |
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10.1016/j.lwt.2022.113419 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001744.pica (DE-627)ELV057457646 (ELSEVIER)S0023-6438(22)00354-1 DE-627 ger DE-627 rakwb eng 690 VZ 74.12 bkl 74.72 bkl Loria, Karina G. verfasserin aut Self-association of caseinomacropeptide in presence of CaCl2 at neutral pH: Calcium binding determination 2022transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The caseinomacropeptide (CMP) is a bioactive peptide produced during cheese making. It is found in abundance in whey. CMP aqueous solutions allow the incorporation of large amounts of CaCl2 but the mechanism of calcium-CMP interactions are unknown. In order to evaluate its calcium binding capacity, the following techniques were performed: Dynamic Light Scattering (DLS), Fourier Transform Infrared spectroscopy (FTIR), dialysis, conductivity, precipitation of CaCl2/CMP complex by ethanol, electrochemical Ca2+ binding isotherms, and inhibition of calcium phosphate precipitation. One mole of CMP can bind 9 mol of calcium, and the CMP self-assembles as a hexameric form. A model is proposed to explain the CMP self-association in presence of CaCl2. The caseinomacropeptide (CMP) is a bioactive peptide produced during cheese making. It is found in abundance in whey. CMP aqueous solutions allow the incorporation of large amounts of CaCl2 but the mechanism of calcium-CMP interactions are unknown. In order to evaluate its calcium binding capacity, the following techniques were performed: Dynamic Light Scattering (DLS), Fourier Transform Infrared spectroscopy (FTIR), dialysis, conductivity, precipitation of CaCl2/CMP complex by ethanol, electrochemical Ca2+ binding isotherms, and inhibition of calcium phosphate precipitation. One mole of CMP can bind 9 mol of calcium, and the CMP self-assembles as a hexameric form. A model is proposed to explain the CMP self-association in presence of CaCl2. Calcium binding isotherms Elsevier Self-assembly Elsevier Calcium binding peptides Elsevier Pilosof, Ana M.R. oth Farías, María E. 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:161 year:2022 day:1 month:05 pages:0 https://doi.org/10.1016/j.lwt.2022.113419 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OPC-GGO 74.12 Stadtgeographie Siedlungsgeographie VZ 74.72 Stadtplanung kommunale Planung VZ AR 161 2022 1 0501 0 |
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10.1016/j.lwt.2022.113419 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001744.pica (DE-627)ELV057457646 (ELSEVIER)S0023-6438(22)00354-1 DE-627 ger DE-627 rakwb eng 690 VZ 74.12 bkl 74.72 bkl Loria, Karina G. verfasserin aut Self-association of caseinomacropeptide in presence of CaCl2 at neutral pH: Calcium binding determination 2022transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The caseinomacropeptide (CMP) is a bioactive peptide produced during cheese making. It is found in abundance in whey. CMP aqueous solutions allow the incorporation of large amounts of CaCl2 but the mechanism of calcium-CMP interactions are unknown. In order to evaluate its calcium binding capacity, the following techniques were performed: Dynamic Light Scattering (DLS), Fourier Transform Infrared spectroscopy (FTIR), dialysis, conductivity, precipitation of CaCl2/CMP complex by ethanol, electrochemical Ca2+ binding isotherms, and inhibition of calcium phosphate precipitation. One mole of CMP can bind 9 mol of calcium, and the CMP self-assembles as a hexameric form. A model is proposed to explain the CMP self-association in presence of CaCl2. The caseinomacropeptide (CMP) is a bioactive peptide produced during cheese making. It is found in abundance in whey. CMP aqueous solutions allow the incorporation of large amounts of CaCl2 but the mechanism of calcium-CMP interactions are unknown. In order to evaluate its calcium binding capacity, the following techniques were performed: Dynamic Light Scattering (DLS), Fourier Transform Infrared spectroscopy (FTIR), dialysis, conductivity, precipitation of CaCl2/CMP complex by ethanol, electrochemical Ca2+ binding isotherms, and inhibition of calcium phosphate precipitation. One mole of CMP can bind 9 mol of calcium, and the CMP self-assembles as a hexameric form. A model is proposed to explain the CMP self-association in presence of CaCl2. Calcium binding isotherms Elsevier Self-assembly Elsevier Calcium binding peptides Elsevier Pilosof, Ana M.R. oth Farías, María E. 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:161 year:2022 day:1 month:05 pages:0 https://doi.org/10.1016/j.lwt.2022.113419 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OPC-GGO 74.12 Stadtgeographie Siedlungsgeographie VZ 74.72 Stadtplanung kommunale Planung VZ AR 161 2022 1 0501 0 |
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Assessment of urban identity through a matrix of cultural landscapes |
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Self-association of caseinomacropeptide in presence of CaCl2 at neutral pH: Calcium binding determination |
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Self-association of caseinomacropeptide in presence of CaCl2 at neutral pH: Calcium binding determination |
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Loria, Karina G. |
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Assessment of urban identity through a matrix of cultural landscapes |
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self-association of caseinomacropeptide in presence of cacl2 at neutral ph: calcium binding determination |
title_auth |
Self-association of caseinomacropeptide in presence of CaCl2 at neutral pH: Calcium binding determination |
abstract |
The caseinomacropeptide (CMP) is a bioactive peptide produced during cheese making. It is found in abundance in whey. CMP aqueous solutions allow the incorporation of large amounts of CaCl2 but the mechanism of calcium-CMP interactions are unknown. In order to evaluate its calcium binding capacity, the following techniques were performed: Dynamic Light Scattering (DLS), Fourier Transform Infrared spectroscopy (FTIR), dialysis, conductivity, precipitation of CaCl2/CMP complex by ethanol, electrochemical Ca2+ binding isotherms, and inhibition of calcium phosphate precipitation. One mole of CMP can bind 9 mol of calcium, and the CMP self-assembles as a hexameric form. A model is proposed to explain the CMP self-association in presence of CaCl2. |
abstractGer |
The caseinomacropeptide (CMP) is a bioactive peptide produced during cheese making. It is found in abundance in whey. CMP aqueous solutions allow the incorporation of large amounts of CaCl2 but the mechanism of calcium-CMP interactions are unknown. In order to evaluate its calcium binding capacity, the following techniques were performed: Dynamic Light Scattering (DLS), Fourier Transform Infrared spectroscopy (FTIR), dialysis, conductivity, precipitation of CaCl2/CMP complex by ethanol, electrochemical Ca2+ binding isotherms, and inhibition of calcium phosphate precipitation. One mole of CMP can bind 9 mol of calcium, and the CMP self-assembles as a hexameric form. A model is proposed to explain the CMP self-association in presence of CaCl2. |
abstract_unstemmed |
The caseinomacropeptide (CMP) is a bioactive peptide produced during cheese making. It is found in abundance in whey. CMP aqueous solutions allow the incorporation of large amounts of CaCl2 but the mechanism of calcium-CMP interactions are unknown. In order to evaluate its calcium binding capacity, the following techniques were performed: Dynamic Light Scattering (DLS), Fourier Transform Infrared spectroscopy (FTIR), dialysis, conductivity, precipitation of CaCl2/CMP complex by ethanol, electrochemical Ca2+ binding isotherms, and inhibition of calcium phosphate precipitation. One mole of CMP can bind 9 mol of calcium, and the CMP self-assembles as a hexameric form. A model is proposed to explain the CMP self-association in presence of CaCl2. |
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title_short |
Self-association of caseinomacropeptide in presence of CaCl2 at neutral pH: Calcium binding determination |
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https://doi.org/10.1016/j.lwt.2022.113419 |
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Pilosof, Ana M.R. Farías, María E. |
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