Structural characterization and antioxidant activity of a novel heteropolysaccharide from the submerged fermentation mycelia of Ganoderma capense.
Yating Huang, Naisheng Li, Jian-Bo Wan, Dezhi Zhang, Chunyan Yan
Index: Carbohydr. Polym. 134 , 752-60, (2015)
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Abstract
A novel heteropolysaccharide (GCPB-2) with a molecular mass of 1.03×10(5)Da was isolated from the submerged fermentation culturing mycelia powder of Lingzhi, Ganoderma capense, by DEAE-52 cellulose, DEAE Sepharose CL-6B, and Sephadex G-75 column chromatography. Its chemical structure was characterized for the first time. The antioxidant activity was evaluated by two antioxidant assay methods. The result of this study introduced G. capense as a possible valuable source that helped to exhibit some antioxidant properties. The homogeneous polysaccharide was composed of xylose and arabinose in the molar ratio of 1:1, and showed a specific optical rotation of [α]D(25)=+161° (c 1.0, H2O). Monosaccharide analysis, partial acid hydrolysis, periodic acid oxidation, methylation analysis, gas chromatography-mass spectrometry (GC-MS), Fourier transform-infrared spectroscopy (FT-IR), and nuclear magnetic resonance (NMR) spectroscopy ((1)H, (13)C, HMQC and HMBC) were conducted to elucidate its structure. The backbone of GCPB-2 was composed of (1 → 4)-linked-β-D-xylopyranose residues which branched at O-3. The two branches consisted of (1 → 3)-linked-β-L-arabinopyranose terminated with β-D-xylopyranose residues, and (1 → 4)-linked-β-L-arabinopyranose terminated with β-D-arabinopyranose residues. In the in vitro antioxidant assay, GCPB-2 was found to possess 1-diphenyl-2-picryl-hydrazyl (DPPH) radical-scavenging activity with an EC50 value of 0.379 μM. The findings of this study indicated that GCPB-2 possesses the hydroxyl radical-scavenging activity, which provided an experimental evidence to support the G. capense as functional foods in some Asian countries. To understand better the bioactivity of GCPB-2, the antioxidant activity should be further investigated to find out its mechanism in future work.Copyright © 2015 Elsevier Ltd. All rights reserved.
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