alpha-chymotrypsin has been researched along with galactomannan* in 2 studies
2 other study(ies) available for alpha-chymotrypsin and galactomannan
| Article | Year |
|---|---|
Improved functional properties of the ovoinhibitor by conjugating with galactomannan.
The chicken egg white ovoinhibitor, a multi-type proteinase inhibitor, was conjugated with galactomannan through the Maillard reaction in a controlled dry heating state at 60 degrees C and 65% relative humidity. The formation of an ovoinhibitor-galactomannan conjugate during dry heating was confirmed by SDS-PAGE. The resulting ovoinhibitor-galactomannan conjugate showed almost the same inhibitory activity toward trypsin, chymotrypsin and elastase as that of the untreated ovoinhibitor, while the conjugate showed stronger heat stability and better emulsifying properties than the untreated ovoinhibitor. These results suggest that the ovoinhibitor-galactomannan conjugate can be used as a protease inhibitor having heat stability and outstanding emulsifying properties for industrial application. Topics: Animals; Chickens; Chymotrypsin; Drug Stability; Egg Proteins, Dietary; Egg White; Electrophoresis, Polyacrylamide Gel; Emulsifying Agents; Galactose; Hot Temperature; Maillard Reaction; Mannans; Pancreatic Elastase; Serine Proteinase Inhibitors; Trypsin | 2003 |
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. Topics: Amino Acid Sequence; Chymotrypsin; Excipients; Galactose; Glycosylation; Maillard Reaction; Mannans; Molecular Sequence Data; Phosvitin | 1999 |