Abstract: A glycan-protein complex (GLM-A) was isolated from the Ganoderma lucidum with phosphate buffer solution at 80 ℃. The carbohydrate in GLM-Ais almost constituted by glucose, and the content of protein is about 13%. The molecular weight M_w dependences of intrinsic viscosity [η] and root mean square radius of gyration 〈 S²〉^1/2 of GLM Ain the 1∶1 water diluted cadoxen at 30 ℃ are [ η ]=5.1×10^-2 M_w^0.60 (cm³·g^-1 ) and 〈 S²〉^1/2=3.9×10^-2M_w^0.50(nm), respectively. According to Bohdanecky's method based on Yamakawa Fujii Yoshizakis theory for worm like chain cylinder, molar mass per unit contour length M L, persistence length q , and chain diameter d were estimated to be (530±10) nm^-1 , (2.8±0.2) nm, and 0.75 nm, respectively, in the 1∶1 water-diluted cadoxen. The results indicated that the glycan protein complex exists as a random coil in the aqueous solution.

Key words: Ganoderma lucidum mycelia, Chemical component, Molecular weight, Chain stiffness, Solution property