| Autor: |
Saeed, Asma, Marwat, Muhammad Salim, Naz, Rubina, Baloch, Asif Latif, Gul, Jaweria, Awan, Inayatullah, Saeed, Ahmad |
| Zdroj: |
Pakistan Journal of Weed Science Research; 2016, Vol. 22 Issue 2, p211-226, 16p |
| Abstrakt: |
Acid phosphatases (EC 3.1.3.2) catalyze the hydrolysis of various phosphomonoesters at pH below 6.0. These enzymes from two sources, Avena fatua (wild oats) and Chnopodium album (common lambsquarters) seeds were partially purified by chromatography on DEAE-Cellulose and Sephadex G-100 columns to make an appropriate comparison of their properties and characteristics. Both enzymes had obtained specific activity in range of 460-1000 units/mg of protein with approximately 20-40 fold purification and had overall recovery of about 60 %. Both enzymes were found fully stable at pH 5-6 and 20-37° C. Both enzymes showed pH optima of 5.6, but the temperature optima of 55° C for C. album seeds and 60° C for A. factua seeds were obtained. The Km of enzymes against substrate, p.nitrophenyl phosphate was 0.3mM and 0.23mM, respectively. Substrate specificity indicated that p.nitrophenyl phosphate, phenyl phosphate, ATP and sodium pyrophosphate were found good substrates. Kinetic parameters suggested that the enzyme from C. album was more active than that of A. fatua. Phytochemical analysis of weed seed extracts was carried out. Alkaloids, saponins, glycosides, terpenoids, steroids, flavonoids and tannins were detected. Tannins and flavinoids were in high concentration while alkaloids and saponins were present in low concentrations. Flavonoids are water soluble polyphenolic molecules thought to provide antioxidant effects and these plants may be used to protect oxidative damage of biomolecules in human body. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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