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Permeation chromatography on extracted Wolffia
Author(s) -
Ehwald Rudolf,
Klein Petra,
Jungnickel Fritz,
Dongowski Gerhard
Publication year - 1995
Publication title -
phytochemical analysis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.574
H-Index - 72
eISSN - 1099-1565
pISSN - 0958-0344
DOI - 10.1002/pca.2800060502
Subject(s) - chemistry , chromatography , permeation , size exclusion chromatography , arabinose , pectin , gel permeation chromatography , elution , macromolecule , colloid , filtration (mathematics) , membrane , xylose , organic chemistry , biochemistry , enzyme , polymer , statistics , mathematics , fermentation
Vesicular packing materials (VP) formed by the cell wall frame of denaturated and extracted Wolffia arrhiza and W. columbiana were investigated for possible applications in permeation chromatography. Two types of VP were studied: W 0 , being fronds extracted with ethanol and water, and W 1 , obtained from W 0 by treatment with pancreatic enzymes in order to remove the insoluble protoplast residues. The cell wall material of W. arrhiza is characterized by a high content of pectin which is rich in homogalacturonan with low contents of L ‐rhamnose, D ‐galactose and L ‐arabinose, and a low degree of esterification. In permeation chromatography on both W 0 and W 1 , excluded components formed a sharp peak at an elution volume which was 26‐30% of the total bed volume. The critical size, in terms of Stokes' diameter, for the exclusion of macromolecules by W 0 is about 5 nm, and this allows for complete exclusion of most proteins. At linear flow rates below 0.1 mL/cm 2 /min the column length necessary for complete separation of sugars or salts from excluded macromolecules may be less than 10 cm. Because of their smaller particle size the materials prepared from W. columbiana showed a smaller peak variance for permeable compounds. The potentially low price of the W 0 material suggests its use as an alternative to gel filtration media for the fast removal of low molecular weight solutes from proteins and other hydrophilic colloidal materials on a technical scale.