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<span style="font-size:11.0pt;font-family: "Times New Roman";mso-fareast-font-family:"Times New Roman";mso-bidi-font-family: Mangal;color:black;mso-ansi-language:EN-GB;mso-fareast-language:EN-US; mso-bidi-language:HI" lang="EN-GB">P<span style="font-size:11.0pt; font-family:"Times New Roman";mso-fareast-font-family:"Times New Roman"; mso-bidi-font-family:Mangal;color:black;mso-ansi-language:EN-GB;mso-fareast-language: EN-IN;mso-bidi-language:HI" lang="EN-GB">urification, characterization and properties of phytase from <i>Shigella </i>sp. CD2</span></span>

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Title Purification, characterization and properties of phytase from Shigella sp. CD2
 
Creator Roy, Moushree Pal
Poddar, Madhumita
Singh, Kamal Krishna
Ghosh, Shilpi
 
Subject Phytase
Phytate
Shigella
Phosphorous
 
Description 266-271
Phytases catalyze the release of phosphate from phytic
acid. In this study, a phytase producing bacterial strain Shigella sp. CD2 was isolated from the wheat rhizosphere. Phytase
production started from the exponential phase of bacterial growth, showing the
highest activity during the stationary phase. The enzyme activity was detected
in both periplasmic and intracellular fractions. The enzyme was purified by
about 133-fold with specific activity 780 U mg-1 protein. The
optimum pH and temperature of the enzyme was 5.5 and 60oC,
respectively. The enzyme was thermostable and retained 100% and 75% of its
activity on pre-incubation at 70o and 80oC for 30 min,
respectively. The Km value
for the substrate sodium phytate was 0.25 mM. The enzyme was highly specific to
substrate phytate, and no activity was detected in presence of other
phosphorylated substrates, such as ATP, ADP, glucose 6-phosphate, fructose
6-phosphate and p-nirophenyl
phosphate. The activity declined dramatically in presence of Cu2+,
Zn2+ and Fe2+ and SDS, whereas Mg2+ and Co2+
slightly enhanced the enzyme activity. The addition of other metal ions or
chemicals had little or no effect
on phytase activity. The enzyme was resistant to both pepsin and trypsin. Due
to high specific activity, substrate specificity, good pH profile, protease
insensitivity and thermostability, phytase encoding gene from Shigella sp. CD2 could be an interesting
candidate for industrial applications. Further studies on cloning and
expression of Shigella phytase gene
are currently in progress.
 
Date 2012-08-07T11:23:06Z
2012-08-07T11:23:06Z
2012-08
 
Type Article
 
Identifier 0975-0959 (Online); 0301-1208 (Print)
http://hdl.handle.net/123456789/14543
 
Language en_US
 
Rights CC Attribution-Noncommercial-No Derivative Works 2.5 India
 
Publisher NISCAIR-CSIR, India
 
Source IJBB Vol.49(4) [August 2012]