One step purification of the grape vacuolar invertase.
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.
Jégou
Sandrine
S
Laboratoire d'Oenologie et Chimie Appliquée, Université de Reims Champagne-Ardenne, URVVC UPRES EA 2069, BP 1039, 51687 Reims Cedex 2, France. sandrine.jegou@univ-reims.fr
Conreux
Alexandra
A
Villaume
Sandra
S
Hovasse
Agnès
A
Schaeffer
Christine
C
Cilindre
Clara
C
Van Dorsselaer
Alain
A
Jeandet
Philippe
P
D000595:Amino Acid Sequence; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D008969:Molecular Sequence Data; D010936:Plant Extracts / Q000737:chemistry; D053719:Tandem Mass Spectrometry; D027843:Vitis / Q000201:enzymology*; D043324:beta-Fructofuranosidase / Q000737:chemistry / Q000302:isolation & purification*
D010936:Plant Extracts; D043324:beta-Fructofuranosidase