期刊
JOURNAL OF FOOD AND DRUG ANALYSIS
卷 23, 期 1, 页码 63-70出版社
FOOD & DRUG ADMINSTRATION
DOI: 10.1016/j.jfda.2014.05.006
关键词
acetylcholinesterase; Cordyceps militaris; Fourier transform infrared spectra; high-performance gel-filtration chromatography; polysaccharide peptide complexes
Acetylcholinesterase (AChE) inhibition enhances learning and cognitive ability for treatment of Alzheimer's disease. Polysaccharide peptide complexes were identified in Cordyceps milltaris (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 beta-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 mgimL 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. Copyright (C) 2014, Food and Drug Administration, Taiwan. Published by Elsevier Taiwan LLC. All rights reserved.
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