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Purification and some properties of rose (<i style="">Fructus cynosbati)</i> hips invertase

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Title Purification and some properties of rose (Fructus cynosbati) hips invertase
 
Creator Sacan, Ozlem
Yanardag, Refiye
 
Subject Invertase
Rose Hips
Fructus Cynosbati
Purification
Properties
 
Description 109-114
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%).
 
Date 2012-04-17T08:54:58Z
2012-04-17T08:54:58Z
2012-04
 
Type Article
 
Identifier 0975-0959 (Online); 0301-1208 (Print)
http://hdl.handle.net/123456789/13842
 
Language en_US
 
Rights CC Attribution-Noncommercial-No Derivative Works 2.5 India
 
Publisher NISCAIR-CSIR, India
 
Source IJBB Vol.49(2) [April 2012]