Isolation and Purification, Structural Characterization, Hypoglycemic Activity of Soluble β-Glucan from Cordyceps chrysanthemi
Soluble β-glucan from mushroom source had good biological activity, in order to develop and utilize β-glucan (CMBG) in Cordyceps chrysanthemi, this study used Cordyceps chrysanthemi substrate as raw material, and was purified by proteolytic enzyme digestion, adsorption of macroporous resin, and chro...
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| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | zho |
| Published: |
The editorial department of Science and Technology of Food Industry
2025-01-01
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| Series: | Shipin gongye ke-ji |
| Subjects: | |
| Online Access: | http://www.spgykj.com/cn/article/doi/10.13386/j.issn1002-0306.2024020067 |
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| Summary: | Soluble β-glucan from mushroom source had good biological activity, in order to develop and utilize β-glucan (CMBG) in Cordyceps chrysanthemi, this study used Cordyceps chrysanthemi substrate as raw material, and was purified by proteolytic enzyme digestion, adsorption of macroporous resin, and chromatography of DEAE ion-exchange columns, and the decolorization rate and β-glucan retention rate were weighted and scored to feel out the establishment of the optimal purification process conditions. The obtained β-glucan was structurally analyzed and its in vitro hypoglycemic activity was investigated. The results showed that the macroporous resin HPD-750 had the best adsorption effect, and the optimal conditions for adsorption were as follows: up-sample flow rate of 5 mL/min, up-sample concentration of 4 mg/mL, up-sample volume of 400 mL, and mass of the resin of 40 g. Two β-glucan fractions, CMBG-1 and CMBG-2, with relative molecular weights of 13.57×104 Da and 14.36×104 Da, respectively, were isolated using a DEAE-FF cellulose exchange column. Both consisted of three monosaccharides, Gal, Glc, and Man, with molar ratios of 1.28:5.27:1.01 and 0.71:4.43:0.80, respectively. The Congo red analysis showed that CMBG-1 had a triple-helix structure, while CMBG-2 had no triple-helix structure, and the inhibition rates of both of them on α-amylase and α-glucosidase were positively correlated with the concentrations of the samples, and the IC50 of their inhibition on α-amylase were 2.68 and 4.32 mg/mL, and those on α-glucosidase were 2.37 and 3.01 mg/mL, respectively. The hypoglycemic activity of CMBG-1, which possessed a triple-helix structure, was significantly higher than that of CMBG-2, which did not possess a triple-helix structure, and it had good prospects for the development of functional foods. |
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| ISSN: | 1002-0306 |