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...
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Published in | Journal of agricultural and food chemistry Vol. 45; no. 8; pp. 2935 - 2941 |
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Main Authors | , , , , |
Format | Journal Article |
Language | English |
Published |
Washington, DC
American Chemical Society
01.08.1997
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Subjects | |
Online Access | Get full text |
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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 |
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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 |