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<span style="font-size:15.0pt;mso-bidi-font-weight:bold" lang="EN-US">Purification and characterization of a phospholipase A<sub>2</sub>-IIA from common stingray (<i>Dasyatis pastinaca)</i> intestine </span>

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Title Purification and characterization of a phospholipase A2-IIA from common stingray (Dasyatis pastinaca) intestine
 
Creator Bacha, Abir Ben
Daihan, Sooad K
Moubayed, Nadine MS
Mejdoub, Hafedh
 
Subject Marine phospholipase A2
Characterization
Sequence
Stability
Organic solvent
Stingray
Dasyatis pastinaca
 
Description 186-195
A phospholipase A2 belonging to IIA group secretory PLA2
was isolated and purified to homogeneity from the intestine of common stingray
(Dasyatis pastinaca) using acidic treatment (pH 1.5) and ammonium
sulphate precipitation methods combined with single-column ion-exchange
chromatography. The purified enzyme was found to be a glycosylated monomeric
protein with a molecular mass of about 14 kDa. The stingray sPLA2-IIA
had optimum activity at 45°C, unlike known mammalian PLA2-IIAs,
which show optimum activity at 37°C. The purified enzyme exhibited a specific
activity of 290 U/mg at optimal conditions (pH 9.5 and 45°C) in the presence of
6 mM NaDC and 8 mM CaCl2 with egg yolk as substrate. The NH2-terminal
sequence of the enzyme and some protein fragments obtained from its tryptic
digestion were also determined. All sequences obtained were similar to those of
sPLA2-IIA. The enzyme also showed good stability in the presence of
organic solvents, acidic and alkaline pH media and high temperature conditions.
Thus, the purified enzyme exhibited a number of unique and promising
properties, making it a potential possible candidate for future applications in
the treatment of phospholipid-rich industrial effluents and synthesis of useful
preparations for the food production and processing industry.


 
Date 2013-06-04T12:57:15Z
2013-06-04T12:57:15Z
2013-06
 
Type Article
 
Identifier 0975-0959 (Online); 0301-1208 (Print)
http://hdl.handle.net/123456789/18687
 
Language en_US
 
Rights CC Attribution-Noncommercial-No Derivative Works 2.5 India
 
Publisher NISCAIR-CSIR, India
 
Source IJBB Vol.50(3) [June 2013]