4.7 Article

One step purification of the grape vacuolar invertase

期刊

ANALYTICA CHIMICA ACTA
卷 638, 期 1, 页码 75-78

出版社

ELSEVIER SCIENCE BV
DOI: 10.1016/j.aca.2009.02.003

关键词

Grape must; Protein; Invertase; Purification; Ion exchange chromatography; Mass spectrometry

资金

  1. Association Recherche Oenologie Champagne et Universite (Reims, France)

向作者/读者索取更多资源

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 abetter 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. (c) 2009 Published by Elsevier B.V.

作者

我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。

评论

主要评分

4.7
评分不足

次要评分

新颖性
-
重要性
-
科学严谨性
-
评价这篇论文

推荐

暂无数据
暂无数据