Glycosyl part identified within Balanites aegyptiaca fruit protease

R G Beka; V D Guiama; A Delmont; P Donn; M-C Slomianny; D G Libouga; C M Mbofung; D Guillochon; D Vercaigne-Marko

doi:10.1016/j.ijbiomac.2011.05.019

Glycosyl part identified within Balanites aegyptiaca fruit protease

Int J Biol Macromol. 2011 Oct 1;49(3):397-401. doi: 10.1016/j.ijbiomac.2011.05.019. Epub 2011 May 27.

Authors

R G Beka¹, V D Guiama, A Delmont, P Donn, M-C Slomianny, D G Libouga, C M Mbofung, D Guillochon, D Vercaigne-Marko

Affiliation

¹ Laboratoire de Biophysique et de Biochimie Alimentaire et Nutrition, Université de Ngaoundéré, BP 455-ENSAI-Ngaoundéré, Cameroun. bekarobertger2004@yahoo.fr

PMID: 21641925
DOI: 10.1016/j.ijbiomac.2011.05.019

Abstract

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Balanites / enzymology*
Fruit / enzymology*
Glycosylation
Monosaccharides / analysis
Monosaccharides / metabolism
Peptide Hydrolases / isolation & purification
Peptide Hydrolases / metabolism*
Uronic Acids / analysis
Uronic Acids / metabolism

Substances

Monosaccharides
Uronic Acids
Peptide Hydrolases