Purpose: The aim of the present study was to investigate antioxidant and antimicrobial effects of the methanol extract of Heracleum nepalense D.Don roots. Method: The antimicrobial effect was determined by agar dilution and disc diffusion method. The free radical scavenging potential was studied by using different antioxidants models of screening using vitamin E (5mM) as standard. Results: The crude methanol extract of H.nepalense root was found to be active against both Gram-positive and Gram-negative organisms. The ethyl acetate soluble fraction of the extract showed similar activity against these organisms. Similarly, the methanol extract at 1000 µg. ml -1 and the ethyl acetate fraction at 50 µg. ml -1 exhibited significant antioxidant activity in ferrous sulphate induced lipid peroxidation, 1,1-diphenyl-2-picryl hydrazyl (DPPH), Hydroxyl radical and Superoxide scavenging models. Conclusions: The study confirms the possible antioxidant and antimicrobial potentiality of the plant extract. Presence of flavonoid alone or in combination with its other components could be responsible for the activity.
This study was carried out to understand and establish the changes in physicochemical parameters of sago starch after acetylation. Highly substituted starch acetate was prepared by reaction with native sago starch and acetic anhydride in organic solvent. Their formation was confirmed by the titrimetric analysis and FT-IR. The presence of absorption band in FT-IR at 1748 cm À1 confirmed the carbonyl group attachment. The thermal behavior of native and acetyl substituted sago starch was investigated using thermo gravimetric analysis (TGA) and DSC. The results reveal that highly substituted starch acetate was more thermally stable as compared to native form. The XRD patterns showed loss of crystalline nature and its transformation into amorphous form. The SEM study suggested that the smooth surfaces of starch granules were changed into fibrous form after acetylation.
A proteolytic enzyme, curcain, has been extracted from the latex of Jatropha curcas Linn. The enzyme was purified by chromatography on carboxymethyl cellulose and gel filtration on Sephadex G-200. The homogeneity of protein associated with curcain was established by non-denatured polyacrylamide gel electrophoresis using a discontinuous buffer system. The molecular weight of curcain was estimated by Sephadex G-100 gel filtration using a calibration curve of standard proteins to be around 22,000 daltons.
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