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|Title:||Purification and some properties of rose (<i style="">Fructus cynosbati)</i> hips invertase|
<i style="">Fructus Cynosbati</i>
|Abstract:||Invertase was purified from rose (<i style="">Fructus cynosbati</i>) hips by ammonium sulfate fractionation and hydroxyapatite column chromatography. The enzyme was obtained with a yield of 4.25% and about 10.48-fold purification and had a specific activity of 8.59 U/mg protein. The molecular mass of invertase was estimated to be 66.51 kDa by PAGE and 34 kDa by SDS-PAGE, indicating that the native enzyme was a homodimer. The enzyme was a glycoprotein and contained 5.86% carbohydrate. The <i style="">K<sub>m</sub></i> for sucrose was 14.55 mM and the optimum <i style="">p</i>H and temperature of the enzyme were 4.5 and 40°C, respectively. Sucrose was the most preferred substrate of the enzyme. The enzyme also hydrolyzed D(+) raffinose, D(+) trehalose and inulin (activity 39.88,<b style=""> </b>8.12 and 4.94%, respectively of that of sucrose), while D(+) lactose, cellobiose and D(+) maltose showed no effect on the enzyme. The substrate specificity was consistent with that for a β-fructofuranoside, which is the most popular type in the higher plants. The enzyme was completely inhibited by HgCl<sub>2</sub>, MnCl<sub>2</sub>, MnSO<sub>4</sub>, FeCl<sub>3</sub>, Pb(NO<sub>3</sub>)<sub>2</sub>, ammonium heptamolybdate, iodoacetamide and pyridoxine hydrochloride. It was also inhibited by Ba(NO<sub>3</sub>)<sub>2</sub> (86.32%), NH<sub>4</sub>Cl (84.91%), MgCl<sub>2 </sub>(74.45%), urea (71.63%), I<sub>2</sub> (69.64%),<sub> </sub>LiCl (64.99%), BaCl<sub>2</sub> (50.30%), Mg(NO<sub>3</sub>)<sub>2 </sub>(49.90%), CrCl<sub>3</sub> (31.90%)<sub> </sub>and<sub> </sub>CuSO<sub>4 </sub>(21.45%) and but was activated by Tris (73.99%) and methionine (12.47%).|
|ISSN:||0975-0959 (Online); 0301-1208 (Print)|
|Appears in Collections:||IJBB Vol.49(2) [April 2012]|
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