Please use this identifier to cite or link to this item: http://repositorio.ufla.br/jspui/handle/1/49704
Title: Extraction, purification by cation exchange supermacroporous cryogel and physico-chemical characterization of γ-conglutin from lupin seeds (Lupinus Albus L.)
Keywords: Mass spectrometry
Supermacroporous cryogel
White lupin
Y-conglutin purification
Issue Date: 23-Oct-2021
Publisher: Wiley
Citation: SILVA, R. M. da et al. Extraction, purification by cation exchange supermacroporous cryogel and physico-chemical characterization of γ-conglutin from lupin seeds (Lupinus Albus L.). Journal of Separation Science, [S.l.], v. 45, n. 2, p. 401-410, 2021. DOI: 10.1002/jssc.202100675.
Abstract: This study focused on the extraction, purification, and physicochemical characterization of γ-conglutin, a protein present in lupin seeds with properties of reducing blood glucose levels. Total protein was extracted with an alkaline-saline solvent, followed by isoelectric precipitation. Chromatographic purification of the precipitated fraction was performed using a cation exchange supermacroporous cryogel column. Electrophoresis of the eluted fraction from chromatography presented a single band of ∼48 kDa under non-reducing conditions (two bands of ∼30 and ∼17 kDa, under reducing conditions) confirming the success of the purification protocol. Liquid chromatography-tandem mass spectrometry analysis confirmed the identity of the protein as γ-conglutin. The purified γ-conglutin had an isoelectric point of 7.51, β-sheets prevailing as a secondary structure, and denaturation temperature close to 68°C. The outcome of this work showed that γ-conglutin was obtained with a high degree of purity. The proposed purification protocol is simple and can be easily scaled up.
URI: https://analyticalsciencejournals.onlinelibrary.wiley.com/doi/10.1002/jssc.202100675
http://repositorio.ufla.br/jspui/handle/1/49704
Appears in Collections:DCA - Artigos publicados em periódicos

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