Plasmin Hydrolysis of β-Casein:  Foaming and Emulsifying Properties of the Fractionated Hydrolysate

Bovine β-casein (βCN) was hydrolyzed by plasmin. The hydrolysate was fractionated by ultrafiltration and selective precipitation, which resulted in several peptide fractions of which the peptide composition was monitored by reversed-phase high-performance liquid chromatography. Poorly soluble, hydro...

Full description

Saved in:
Bibliographic Details
Published inJournal of agricultural and food chemistry Vol. 45; no. 8; pp. 2935 - 2941
Main Authors Caessens, Petra W. J. R, Gruppen, Harry, Visser, Servaas, van Aken, George A, Voragen, Alphons G. J
Format Journal Article
LanguageEnglish
Published Washington, DC American Chemical Society 01.08.1997
Subjects
Online AccessGet full text

Cover

Loading…
More Information
Summary:Bovine β-casein (βCN) was hydrolyzed by plasmin. The hydrolysate was fractionated by ultrafiltration and selective precipitation, which resulted in several peptide fractions of which the peptide composition was monitored by reversed-phase high-performance liquid chromatography. Poorly soluble, hydrophobic peptide fractions, containing peptides from the C-terminal half of the βCN sequence, possessed improved foam-forming and -stabilizing properties compared to those of intact βCN, especially at pH 4.0. Soluble peptide fractions, containing a variety of peptides from the “middle” part of the βCN sequence in different proportions, possessed improved emulsion-forming capacity at pH 6.7, compared to that of intact βCN, and showed large variations in emulsion stability. The fraction containing the hydrophilic N-terminal part of βCN showed inferior foam, emulsion, and surface-active properties, especially at pH 6.7. The differences in functionality found between the various peptide fractions may be attributed either to synergistic effects between peptides or to a specific functionality of some individual peptides. Keywords: β-Casein; peptides; plasmin; foam; emulsions
Bibliography:1997073976
Q05
istex:948ABCB973FDBD583EA277104EF3CCAEB6B688A7
ark:/67375/TPS-WJH9M8LD-X
Abstract published in Advance ACS Abstracts, July 15, 1997.
ISSN:0021-8561
1520-5118
DOI:10.1021/jf9700889