Glycosyl part identified within Balanites aegyptiaca fruit protease

The many milk-clotting proteases from plant are glycosylated; attachment of monosaccharides to enzyme is an advantage for its activity and stability. In this study, gas chromatography coupled to mass spectrometry-electrospray ionization was used to identify glycans bond to proteases purified from Ba...

Full description

Saved in:
Bibliographic Details
Published in:International journal of biological macromolecules 2011-10, Vol.49 (3), p.397-401
Main Authors: Beka, R.G., Guiama, V.D., Delmont, A., Donn, P., Slomianny, M.-C., Libouga, D.G., Mbofung, C.M., Guillochon, D., Vercaigne-Marko, D.
Format: Article
Language:English
Subjects:
arabinose
B. aegyptiaca
Balanites - enzymology
Balanites aegyptiaca
cation exchange chromatography
Chromatography
Fruit - enzymology
fruits
galactose
gas chromatography
glucuronic acid
Glycosylation
ionization
mannose
Mass spectrometry
milk clotting
Monosaccharides
Monosaccharides - analysis
Monosaccharides - metabolism
Peptide Hydrolases - isolation & purification
Peptide Hydrolases - metabolism
polysaccharides
Protease
proteinases
pulp
rhamnose
Uronic Acids - analysis
Uronic Acids - metabolism
xylose
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:The many milk-clotting proteases from plant are glycosylated; attachment of monosaccharides to enzyme is an advantage for its activity and stability. In this study, gas chromatography coupled to mass spectrometry-electrospray ionization was used to identify glycans bond to proteases purified from Balanites aegyptiaca fruits pulp through cation exchange chromatography. Carbohydrates were identified according to the retention time and the ion at m/ z after derivation by heptafluorobutyric acid. The chromatograms obtained from monosaccharides analysis revealed the presence of galactose, mannose, arabinose, xylose, rhamnose and glucuronic acid. The mass spectrometry-electrospray ionization spectra corroborated these findings.
ISSN:0141-8130
1879-0003
DOI:10.1016/j.ijbiomac.2011.05.019