Molecular mechanism of the excellent emulsifying properties of phosvitin-galactomannan conjugate.
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.
Kahn
M A
MA
Department of Biological Chemistry, Yamaguchi University, Japan.
Babiker
E E
EE
Azakami
H
H
Kato
A
A
D000595:Amino Acid Sequence; D002918:Chymotrypsin; D005079:Excipients; D005690:Galactose / Q000031:analogs & derivatives; D006031:Glycosylation; D015416:Maillard Reaction; D008351:Mannans / Q000737:chemistry*; D008969:Molecular Sequence Data; D010774:Phosvitin / Q000737:chemistry*
D005079:Excipients; D008351:Mannans; C012990:galactomannan; D010774:Phosvitin; D002918:Chymotrypsin; D005690:Galactose