RESUMEN
Acetylcholinesterase (AChE) inhibition enhances learning and cognitive ability for treatment of Alzheimer's disease. Polysaccharide-peptide complexes were identified in Cordyceps militaris (CPSPs) and characterized for their AChE inhibitory properties. Three polymers (CPSP-F1, -F2, and -F3) were extracted and separated by ultrasound-assisted extraction and diethylaminoethanol (DEAE)-Sepharose CL-6B column chromatography. Polysaccharide-peptide complexes were identified by DEAE-Sepharose CL-6B column chromatography and high-performance gel-filtration chromatography, Fourier transform infrared spectra, amino sugar composition analysis, and ß-elimination reaction to identify polysaccharide-peptide bond categories. Separation of CPSP can increase AChE inhibitory activity from the crude polysaccharide of C. militaris. CPSP-F1 and CPSP-F2 exhibited half maximal inhibitory concentrations of 32.2 ± 0.2 mg/mL and 5.3 ± 0.0 mg/mL. Thus, we identified polysaccharide-peptide complexes from C. militaris and suggest CPSP has great potential in AChE inhibition bioassay.
RESUMEN
Intracellular polysaccharides (iPs) were separated and purified from Coriolus versicolor LH1 mycelia and characterized for their α-glucosidase inhibitory properties. Three iP fractions (iPL-F5-2-1, iPL-F5-4-1, and iPL-F5-5-1) were extracted, separated, and purified from LH1 mycelia using microwave extraction technology, a DEAE-Sepharose CL-6B column, a Diaion HP20 macroporous adsorption column, and a Sephadex™ G-50 gel-permeation column. The principal constituents of iPL-F5-2-1, iPL-F5-4-1, and iPL-F5-5-1 were saponins and polyphenoic compound mixtures. The enzyme inhibition activity, IC(50) values, of these three fractions were 1.7, 1.8, and 0.8 mg/mL, respectively. The α-glucosidase inhibitory properties were related to the presence of α-(1,4) glycosidic linkages in the polysaccharide structure and the total relative percentage of d-glucose and d-galactose in the structure of polysaccharides, other than triterpenoids.