Two-Step purification of pathogenesis-related proteins from grape juice and crystallization of thaumatin-like proteins

Steven C. Van Sluyter, Matteo Marangon, Samuel D. Stranks, Karlie A. Neilson, Yoji Hayasaka, Paul A. Haynes, R. Ian Menz, Elizabeth J. Waters

Research output: Contribution to journalArticlepeer-review

41 Citations (Scopus)

Abstract

Grape thaumatin-like (TL) proteins and chitinases play roles in plant-pathogen interactions and can cause protein haze in white wine unless removed prior to bottling. A two-step method is described that highly purified hundreds of milligrams of TL proteins and chitinases from two juices by strong cation exchange (SCX) and hydrophobic interaction chromatography (HIC). The method was fast and separated isoforms of TL proteins and chitinases from within the same juice, in most cases to >97% purity. The isolated proteins were identified by peptide nanoLC-MS/MS and crystallized using a high-throughput screening method. Crystals from three protein fractions produced highresolution X-ray crystallography data.

Original languageEnglish
Pages (from-to)11376-11380
Number of pages5
JournalJournal of Agricultural and Food Chemistry
Volume57
Issue number23
DOIs
Publication statusPublished - 9 Dec 2009

Fingerprint

Dive into the research topics of 'Two-Step purification of pathogenesis-related proteins from grape juice and crystallization of thaumatin-like proteins'. Together they form a unique fingerprint.

Cite this