A Modified Method for Extraction and Deproteinization of Mannan Oligosaccharides
Extraction of water soluble mannan oligosaccharides (MOS) from the cell wall of yeast and a modified method of deproteinization were studied. This method depends on the complete inactivation of residual proteins present after deproteinization by Sevage method (Staub 1965) using acetone. IR spectral analysis clearly indicated that the sample purified by modified Sevage method was found to be chemically mannan oligosaccharides. Proteins would have completely inactivated due to the breakdown of hydrogen bond by the electronegative oxygen atom present in the C=O group of acetone. The proposed method can be considered as an modified method of Sevage method. Sevage reagent contains poisonous chloroform which is environmentally disadvantageous (Huang et al., 2005) and the present method removes or inactivates the residual proteins and avoids the health and environmental hazards associated with chloroform by using it not more than once. Proteins and nucleic acids contamination were identified using UV spectra of the samples read between 200-600 nm. The concentration of MOS was carried out by Dubois method. In summary, we obtained highly purified MOS by the proposed method with low concentration of protein contaminants.
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