Journal of Food and Drug Analysis · 2014 · 43 citations · 37 references
Life SciencesBiochemistryPharmacologyBiochemical PharmacologyCarbohydrate ChemistryEnzymologyCholinergic NeurochemistryCholinergic PharmacologyEnzyme InhibitionPeptide ChemistryPolysaccharide PropertiesPolysaccharide StructureAche InhibitionAmino Sugar CompositionColumn ChromatographyCordyceps SpeciesHalf-maximal Inhibitory ConcentrationPolysaccharide CharacterizationPolysaccharide ExtractionPolysaccharide Separation
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 β-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.
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A new and rapid colorimetric determination of acetylcholinesterase activity
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