Improved Purity and Immunostimulatory Activity of β-(1→3)(1→6)-Glucan from Pleurotus sajor-caju Using Cell Wall-Degrading Enzymes.

Summary of "Improved Purity and Immunostimulatory Activity of β-(1→3)(1→6)-Glucan from Pleurotus sajor-caju Using Cell Wall-Degrading Enzymes."

The objective of this work was to improve the purity of β-(1→3)(1→6)-glucan in the native triple helical structure from the fruiting bodies of Pleurotus sajor-caju for effective biological function using cell wall-degrading enzymes. A crude carbohydrate was extracted with hot water, then treated with crude xylanase and cellulase from Paenibacillus curdlanolyticus B-6. β-Glucan in the extract was purified to homogeneity with a single and symmetrical peak using 650M DEAE Toyopearl and Sepharose CL-6B column chromatography. The purity of β-glucan was confirmed by high-performance size-exclusion chromatography. Purified β-glucan was obtained at a purity of up to 90.2%. The Congo red reaction and atomic force microscopy indicated that the purified β-glucan exhibited a triple helix conformation. Purified β-glucan was able to effectively up-regulate the functions of macrophages such as nitric oxide (NO) and tumor necrosis factor (TNF-α) production.


Division of Biochemical Technology, School of Bioresources and Technology, King Mongkut's University of Technology Thonburi , Bangkok 10150, Thailand.

Journal Details

This article was published in the following journal.

Name: Journal of agricultural and food chemistry
ISSN: 1520-5118
Pages: 5423-30


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Medical and Biotech [MESH] Definitions

1,4-alpha-D-Glucan-1,4-alpha-D-glucan 4-alpha-D-glucosyltransferase/dextrin 6 alpha-D-glucanohydrolase. An enzyme system having both 4-alpha-glucanotransferase (EC and amylo-1,6-glucosidase (EC activities. As a transferase it transfers a segment of a 1,4-alpha-D-glucan to a new 4-position in an acceptor, which may be glucose or another 1,4-alpha-D-glucan. As a glucosidase it catalyzes the endohydrolysis of 1,6-alpha-D-glucoside linkages at points of branching in chains of 1,4-linked alpha-D-glucose residues. Amylo-1,6-glucosidase activity is deficient in glycogen storage disease type III.

In glycogen or amylopectin synthesis, the enzyme that catalyzes the transfer of a segment of a 1,4-alpha-glucan chain to a primary hydroxy group in a similar glucan chain. EC

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An unbranched glucan in starch.

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