Functionality of β-Casein Peptides: Importance of Amphipathicity for Emulsion-Stabilizing Properties
To investigate structure−function relationships with regard to emulsion-stabilizing properties, peptides from bovine β-casein (βCN), obtained by plasmin hydrolysis and fractionation of the hydrolysate, were isolated and identified on the basis of their masses determined by electrospray ionization ma...
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Published in | Journal of agricultural and food chemistry Vol. 47; no. 5; pp. 1856 - 1862 |
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Main Authors | , , , , |
Format | Journal Article |
Language | English |
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Washington, DC
American Chemical Society
01.05.1999
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Abstract | To investigate structure−function relationships with regard to emulsion-stabilizing properties, peptides from bovine β-casein (βCN), obtained by plasmin hydrolysis and fractionation of the hydrolysate, were isolated and identified on the basis of their masses determined by electrospray ionization mass spectrometry, the primary structure of the intact protein, and the known specificity of the enzyme. An amphipathic peptide fraction was fractionated further by ion-exchange chromatography and subsequent hydrophobic interaction chromatography resulting in the components βCN[f 1−105/107] and βCN[f 29−105/107]. The latter peptides had poor emulsion-stabilizing properties compared to the former ones, and the stability of an emulsion formed with βCN[f 29−105/107] was also more sensitive to hydrophobic impurities than that of an emulsion formed with βCN[f 1−105/107]. The highly charged N-terminal part appeared to be important for the emulsion-stabilizing properties of these peptides. A hypothesis for the structure−function relationship is given. Keywords: β-Casein peptides; plasmin; emulsion; mass spectrometry; structure−function relationship |
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AbstractList | To investigate structure-function relationships with regard to emulsion-stabilizing properties, peptides from bovine beta-casein (betaCN), obtained by plasmin hydrolysis and fractionation of the hydrolysate, were isolated and identified on the basis of their masses determined by electrospray ionization mass spectrometry, the primary structure of the intact protein, and the known specificity of the enzyme. An amphipathic peptide fraction was fractionated further by ion-exchange chromatography and subsequent hydrophobic interaction chromatography resulting in the components betaCN[f 1-105/107] and betaCN[f 29-105/107]. The latter peptides had poor emulsion-stabilizing properties compared to the former ones, and the stability of an emulsion formed with betaCN[f 29-105/107] was also more sensitive to hydrophobic impurities than that of an emulsion formed with betaCN[f 1-105/107]. The highly charged N-terminal part appeared to be important for the emulsion-stabilizing properties of these peptides. A hypothesis for the structure-function relationship is given. To investigate structure−function relationships with regard to emulsion-stabilizing properties, peptides from bovine β-casein (βCN), obtained by plasmin hydrolysis and fractionation of the hydrolysate, were isolated and identified on the basis of their masses determined by electrospray ionization mass spectrometry, the primary structure of the intact protein, and the known specificity of the enzyme. An amphipathic peptide fraction was fractionated further by ion-exchange chromatography and subsequent hydrophobic interaction chromatography resulting in the components βCN[f 1−105/107] and βCN[f 29−105/107]. The latter peptides had poor emulsion-stabilizing properties compared to the former ones, and the stability of an emulsion formed with βCN[f 29−105/107] was also more sensitive to hydrophobic impurities than that of an emulsion formed with βCN[f 1−105/107]. The highly charged N-terminal part appeared to be important for the emulsion-stabilizing properties of these peptides. A hypothesis for the structure−function relationship is given. Keywords: β-Casein peptides; plasmin; emulsion; mass spectrometry; structure−function relationship |
Author | Voragen, Alphons G. J Visser, Servaas Caessens, Petra W. J. R Slangen, Charles J Gruppen, Harry |
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Keywords | Amphipathic compound Fractionation Biochemical analysis Serine endopeptidases Enzyme Emulsifying power Primary structure Food additive Experimental study N terminal peptide Synergism Protein Molecular weight Plasmin Hydrolysis Peptidases Milk protein Emulsion Casein Stabilizer agent Hydrolases Property structure relationship Physicochemical properties Comparative study |
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Snippet | To investigate structure−function relationships with regard to emulsion-stabilizing properties, peptides from bovine β-casein (βCN), obtained by plasmin... To investigate structure-function relationships with regard to emulsion-stabilizing properties, peptides from bovine beta-casein (betaCN), obtained by plasmin... |
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SubjectTerms | amphipathic peptides Animal, plant, fungal and microbial proteins, edible seaweeds and food yeasts Animals beta-casein Biological and medical sciences Caseins - chemistry Cattle Chromatography, High Pressure Liquid - methods Chromatography, Ion Exchange Emulsions Excipients fat emulsions Fibrinolysin - metabolism Food additives Food industries Fundamental and applied biological sciences. Psychology General aspects lipids Peptide Fragments - chemistry Peptide Fragments - isolation & purification peptides protein hydrolysates Spectrometry, Mass, Secondary Ion stabilizing structure-activity relationships tricaprylin |
Title | Functionality of β-Casein Peptides: Importance of Amphipathicity for Emulsion-Stabilizing Properties |
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