Molecular mechanism of the excellent emulsifying properties of phosvitin-galactomannan conjugate.
J Agric Food Chem
; 47(6): 2262-6, 1999 Jun.
Article
em En
| MEDLINE
| ID: mdl-10794620
ABSTRACT
The emulsifying properties of native and N- and C-terminal-deleted phosvitin (protease digests) were compared after conjugation with galactomannan. The emulsifying properties of Maillard-type phosvitin-galactomannan conjugates were greatly improved, whereas those of the protease-digested phosvitin-galactomannan conjugates were not so dramatically improved. Phosvitin was highly glycosylated with galactomannan, whereas the protease-digested phosvitin conjugate consisting of a highly phosphorylated core peptide fragment was not. The results suggest that both N and C termini of the peptide moiety, digested by protease, were essential for the improvement of emulsifying properties of phosvitin-galactomannan conjugates. In addition, the role of N and C termini as anchors in oil droplets was supported from the comparative studies of native phosvitin, phosvitin-galactomannan conjugates, and protease-digested phosvitin-galactomannan conjugates.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Fosvitina
/
Excipientes
/
Mananas
Idioma:
En
Revista:
J Agric Food Chem
Ano de publicação:
1999
Tipo de documento:
Article