Catalysis and stability of an extracellular α- amylase from a haloalkaliphilic bacterium as a function of the organic solvents at different pH, salt concentrations and temperatures
IR@NISCAIR: CSIR-NISCAIR, New Delhi - ONLINE PERIODICALS REPOSITORY (NOPR)
View Archive Info| Field | Value | |
| Title |
Catalysis and stability of an extracellular α- amylase from a haloalkaliphilic bacterium as a function of the organic solvents at different pH, salt concentrations and temperatures
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| Creator |
Pandey, Sandeep
Sharma, Amit K. Solanki, Kiran P. Singh, Satya P. |
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| Subject |
Haloalkaliphilic bacteria
Organic solvent tolerance α-amylase Non-aqueous enzyme catalysis |
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| Description |
240-248
The Ve1-10-8<sub>2</sub> amylase displayed significant tolerance against methanol, propanol and n-hexane. At the lower concentrations of the solvents, the enzyme catalysis was comparable to control. The enzyme had a broader range of alkaline pH for catalysis, the optimum being at pH 10-11. This pH range was higher than many reported amylases of the alkaliphilic <em>Bacillus</em> species. At the alkaline pH, the enzyme was stable for 3 hrs in the presence of 20 % (v/v) methanol. Optimal temperature at 60 ºC for the catalysis remained unaltered in organic solvents. However, the enzyme was active for up to 70 ºC with 5 and 10 % (v/v) methanol. The enzyme catalysis was optimum with 2 M Salt in most of the tested solvents and it retained significant activity at 4 M salt. To the best of our knowledge, this report is the first on the organic solvent tolerance of the extracellular amylase from the haloalkaliphilic bacteria. |
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| Date |
2018-01-15T07:14:26Z
2018-01-15T07:14:26Z 2018-01 |
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| Type |
Article
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| Identifier |
0975-1033 (Online); 0379-5136 (Print)
http://nopr.niscair.res.in/handle/123456789/43431 |
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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 |
IJMS Vol.47(01) [January 2018]
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