Secretion of cyclodextrin glucanotransferase in <i>E. coli</i> using <i>Bacillus subtilis</i> lipase signal peptide and optimization of culture medium
IR@NISCAIR: CSIR-NISCAIR, New Delhi - ONLINE PERIODICALS REPOSITORY (NOPR)
View Archive Info| Field | Value | |
| Title |
Secretion of cyclodextrin glucanotransferase in <i>E. coli</i> using <i>Bacillus subtilis</i> lipase signal peptide and optimization of culture medium
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| Creator |
Ayadi-Zouari, Dorra
Kammoun, Radhouane Jemli, Sonia Chouayekh, Hichem Bejar, Samir |
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| Subject |
<i><span style="font-size:11.0pt; font-family:"Times New Roman","serif";mso-fareast-font-family:"Times New Roman"; mso-bidi-font-family:Mangal;mso-ansi-language:EN-GB;mso-fareast-language:EN-US; mso-bidi-language:HI" lang="EN-GB">E</span></i><span style="font-size:11.0pt; font-family:"Times New Roman","serif";mso-fareast-font-family:"Times New Roman"; mso-bidi-font-family:Mangal;mso-ansi-language:EN-GB;mso-fareast-language:EN-US; mso-bidi-language:HI" lang="EN-GB">.<i> coli</i></span>
Optimization Recombinant CGTase Response surface methodology Secretion Signal peptide |
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| Description |
72-79
The cyclodextrin glycosyltransferase (CGTase) of <i>Paenibacillus pabuli</i> US132 was fused to the secretive lipase signal peptide of <i>B. subtilis</i>. This leads to an efficient secretion of the recombinant enzyme into the culture medium of<i> E. coli</i> as an active and soluble form contrasting with the native construction leading to a periplasmic production. In order to enhance the yield of CGTase production, an experimental design methodology was applied for the optimization of the culture composition. Hence, the media components were submitted to preliminary screening using a Plakett-Burman design. The concentrations of the major operating ones were then optimized to enhance the secretion of CGTase using response surface methodology. The findings revealed that concentrations of 0.5% potato starch, 3% yeast extract, 3% tryptone, 1.5% casein hydrolysate, 0.5% NaCl, 0.2% KH<sub>2</sub>PO<sub>4, </sub>and 0.02% MgSO<sub>4 </sub>were the optimal conditions for CGTase production. The experimental value (9.43 U/ml) obtained for CGTase activity was very close to the predicted value (9.27 U/ml). |
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| Date |
2012-01-02T06:00:33Z
2012-01-02T06:00:33Z 2012-01 |
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| Type |
Article
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| Identifier |
0975-1009 (Online); 0019-5189 (Print)
http://hdl.handle.net/123456789/13314 |
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| Language |
en_US
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| Rights |
<img src='http://nopr.niscair.res.in/image/cc-license-sml.png'> <a href='http://creativecommons.org/licenses/by-nc-nd/2.5/in' target='_blank'>CC Attribution-Noncommercial-No Derivative Works 2.5 India</a>
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| Publisher |
NISCAIR-CSIR, India
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| Source |
IJEB Vol.50(01) [January 2012]
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