Title of article
One step purification of the grape vacuolar invertase Original Research Article
Author/Authors
Sandrine Jégou، نويسنده , , Alexandra Conreux، نويسنده , , Sandra Villaume، نويسنده , , Agnès Hovasse، نويسنده , , Christine Schaeffer، نويسنده , , Clara Cilindre، نويسنده , , Alain Van-Dorsselaer، نويسنده , , Philippe Jeandet، نويسنده ,
Issue Information
روزنامه با شماره پیاپی سال 2009
Pages
4
From page
75
To page
78
Abstract
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.
Keywords
Ion exchange chromatography , mass spectrometry , protein , Purification , Invertase , Grape must
Journal title
Analytica Chimica Acta
Serial Year
2009
Journal title
Analytica Chimica Acta
Record number
1037216
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