Adopting structural elements from intrinsically stable phytase— A promising strategy towards thermostable phytases
IR@NISCAIR: CSIR-NISCAIR, New Delhi - ONLINE PERIODICALS REPOSITORY (NOPR)
View Archive Info| Field | Value | |
| Creator |
Ushasree, Mrudula Vasudevan
Sumayya, Husaiba Beevi Salim Pandey, Ashok |
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| Date |
2011-10-31T10:35:34Z
2011-10-31T10:35:34Z 2011-10 |
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| Identifier |
0975-0967 (Online); 0972-5849 (Print)
http://hdl.handle.net/123456789/12983 |
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| Description |
458-467
Development of thermostable phytases through biotechnology is a key issue in food and feed industry. Phytases ought to be stable at elevated temperatures since it has to withstand feed and food processing steps. Thermostable catalysts have been an area of extensive research since long and several studies have focused on understanding the critical structural features contributing to their stability curve. Recently, the explosion of high resolution structure and availability of sequence information of stable phytases have enforced the researchers to implement similar strategies successfully to bring together these desirable traits into a single enzyme. Nature has tailored unique stabilizing features in diverse classes of phytase, understanding these critical elements and using a single or combination of potential <i style="">in vitro</i> evolutionary strategies would help phytase to reach the fitness peak in near future. Here we review some recent studies on structural elements contributing to thermostability in phytases of different microbial sources and to summarize the beneficial effect of diverse criterion taken up to generate optimized phytase. |
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| Language |
en_US
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| Publisher |
NISCAIR-CSIR, India
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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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| Source |
IJBT Vol.10(4) [October 2011]
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| Subject |
Histidine acid phosphatases
Intrinsic stability <img src='/image/spc_char/beta.gif' border=0>-propeller phytase |
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| Title |
Adopting structural elements from intrinsically stable phytase— A promising strategy towards thermostable phytases
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| Type |
Article
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