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NISCAIR ONLINE PERIODICALS REPOSITORY (NOPR) >
NISCAIR PUBLICATIONS >
Research Journals >
Indian Journal of Biochemistry and Biophysics (IJBB) >
IJBB Vol.49 [2012] >
IJBB Vol.49(2) [April 2012] >
| Title: | Purification and some properties of rose (Fructus cynosbati) hips invertase |
| Authors: | Sacan, Ozlem
Yanardag, Refiye |
| Keywords: | Invertase
Rose Hips
Fructus Cynosbati
Purification
Properties |
| Issue Date: | Apr-2012 |
| Publisher: | NISCAIR-CSIR, India |
| Abstract: | Invertase was
purified from rose (Fructus cynosbati)
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 Km for sucrose was 14.55 mM and the optimum pH 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, 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 HgCl2,
MnCl2, MnSO4, FeCl3, Pb(NO3)2,
ammonium heptamolybdate, iodoacetamide and pyridoxine hydrochloride. It was
also inhibited by Ba(NO3)2 (86.32%), NH4Cl
(84.91%), MgCl2 (74.45%), urea (71.63%), I2 (69.64%),
LiCl (64.99%), BaCl2 (50.30%), Mg(NO3)2 (49.90%),
CrCl3 (31.90%) and CuSO4 (21.45%) and
but was activated by Tris (73.99%) and methionine (12.47%). |
| Page(s): | 109-114 |
| CC License: |  CC Attribution-Noncommercial-No Derivative Works 2.5 India |
| ISSN: | 0975-0959 (Online); 0301-1208 (Print) |
| Source: | IJBB Vol.49(2) [April 2012]
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