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Interfacial properties of tryptic peptides of .beta.-lactoglobulin

beta-Lactoglobulin (beta-lg) with hydrolyzed with trypsin in an ultrafiltration reactor (PM30). The total hydrolysate (TH) was further fractionated (PM1), resulting in a mixture of polypeptides (MP) and a fraction of amino acids and small peptides (AA). Peptides in each fraction were analyzed by rev...

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Bibliographic Details
Published in:Journal of agricultural and food chemistry 1992-04, Vol.40 (4), p.669-675
Main Authors: Turgeon, Sylvie L, Gauthier, Sylvie F, Molle, Daniel, Leonil, Joelle
Format: Article
Language:English
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Summary:beta-Lactoglobulin (beta-lg) with hydrolyzed with trypsin in an ultrafiltration reactor (PM30). The total hydrolysate (TH) was further fractionated (PM1), resulting in a mixture of polypeptides (MP) and a fraction of amino acids and small peptides (AA). Peptides in each fraction were analyzed by reversed-phase high-performance liquid chromatography (RP-HPLC) and identified by their amino acid composition. The MP fraction was further purified in six fractions by anion-exchange chromatography. Interfacial properties of beta-lg, its TH, MP, and AA fractions, and the purified fractions were measured at pH 4 and 7 at two ionic strengths (micro = 0 and 0.6). Peptides responsible for improved interfacial properties of the MP fraction were identified (beta-lg 21-40, beta-lg 41-60), and structure-function relationships (molecular weight and hydrophobicity) are discussed. Characteristics essential to good interfacial properties are clustering of hydrophilic and hydrophobic residues in distinct zones and a minimum molecular weight allowing this distribution
ISSN:0021-8561
1520-5118
DOI:10.1021/jf00016a030