One step purification of the grape vacuolar invertase.
Fiche publication
Date publication
avril 2009
Auteurs
Membres identifiés du Cancéropôle Est :
Mme SCHAEFFER-REISS Christine, Dr VAN DORSSELAER Alain
Tous les auteurs :
Jegou S, Conreux A, Villaume S, Hovasse A, Schaeffer C, Cilindre C, Van Dorsselaer A, Jeandet P
Lien Pubmed
Résumé
Invertase is a major protein of grape juice and wine. Accordingly, in order to study the biochemical and structural characteristics of this protein and for a better understanding of its physico-chemical properties, large amounts of the pure protein are needed. A simple method for the purification of the grape vacuolar invertase in a preparative-scale is described in this work. The grape protein was isolated and purified from must by ultrafiltration and anion exchange chromatography. The identification and purity determination of the grape invertase fraction were assessed by SDS-PAGE, and were then confirmed using nanoLC-chip-MS/MS analysis. The laboratory fractionation procedure presented in this work generated large quantities of pure grape vacuolar invertase from must.
Référence
Anal Chim Acta. 2009 Apr 6;638(1):75-8