Please use this identifier to cite or link to this item: http://nopr.niscair.res.in/handle/123456789/14543
Title: <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>
Authors: Roy, Moushree Pal
Poddar, Madhumita
Singh, Kamal Krishna
Ghosh, Shilpi
Keywords: Phytase
Phytate
<i><span style="font-size:9.0pt;font-family: "Times New Roman";mso-fareast-font-family:"Times New Roman";color:black; mso-ansi-language:EN-GB;mso-fareast-language:EN-IN;mso-bidi-language:HI" lang="EN-GB">Shigella</span></i>
Phosphorous
Issue Date: Aug-2012
Publisher: NISCAIR-CSIR, India
Abstract: Phytases catalyze the release of phosphate from phytic acid. In this study, a phytase producing bacterial strain <i style="mso-bidi-font-style: normal">Shigella </i>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<sup>-1</sup> protein. The optimum pH and temperature of the enzyme was 5.5 and 60<sup>o</sup>C, respectively. The enzyme was thermostable and retained 100% and 75% of its activity on pre-incubation at 70<sup>o</sup> and 80<sup>o</sup>C for 30 min, respectively. The <i style="mso-bidi-font-style:normal">K</i><sub>m</sub> 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 <i style="mso-bidi-font-style:normal">p</i>-nirophenyl phosphate. The activity declined dramatically in presence of Cu<sup>2+</sup>, Zn<sup>2+</sup> and Fe<sup>2+</sup> and SDS, whereas Mg<sup>2+</sup> and Co<sup>2+</sup> slightly enhanced the enzyme activity. The addition of other metal ions or chemicals had little or no <span style="mso-bidi-font-family: " times="" new="" roman";color:black"="" lang="EN-GB">e<span style="mso-fareast-font-family: " arial="" unicode="" ms";mso-hansi-font-family:"arial="" ms";mso-bidi-font-family:="" "times="" new="" roman";color:black"="" lang="EN-GB">ff<span style="mso-bidi-font-family: " times="" new="" roman";color:black"="" lang="EN-GB">ect 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 <i style="mso-bidi-font-style:normal">Shigella </i>sp. CD2 could be an interesting candidate for industrial applications. Further studies on cloning and expression of <i style="mso-bidi-font-style:normal">Shigella</i> phytase gene are currently in progress. </span></span></span>
Description: 266-271
URI: http://hdl.handle.net/123456789/14543
ISSN: 0975-0959 (Online); 0301-1208 (Print)
Appears in Collections:IJBB Vol.49(4) [August 2012]

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