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Protein Removal

Deproteinization and structural characterization of bioactive exopolysaccharides from Ganoderma sinense mycelium

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Pages 359-369 | Received 29 Oct 2014, Accepted 20 Aug 2015, Published online: 22 Dec 2015
 

Abstract

Deproteinization was comparatively employed for the purification of crude exopolysaccharide (CEP) of Ganoderma sinense mycelium. Results showed that ammonium sulfate (70% saturation) salting out could remove 95% proteins of CEP, whereas 20% trichloroacetic acid precipitation was best with a polysaccharide loss less than 20%. Protein-bound polysaccharides could be removed by both methods, and polysaccharides with high molecular weight dominated in the lost polysaccharides. Through anion-exchange chromatography, a highly branched α-(1→6)-D-mannan and a protein-bound heteropolysaccharide were prepared from CEP. Both fractions could inhibit the in vitro proliferation of tumor cells BEL-7402, and induce TNF-α secretion of murine splenocytes.

Additional information

Funding

This work was supported by a grant from the National Natural Science Foundation of China (No.30800193).

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