Kinetic studies on thermal denaturation of C-phycocyanin
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Title |
Kinetic studies on thermal denaturation of C-phycocyanin
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Creator |
Patel, Anamika
Pawar, Richa Mishra, Sandhya Sonawane, Shailendra Ghosh, P K |
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Subject |
Phycobiliproteins
Spirulina platensis C-Phycocyanin thermal denaturation first order kinetics |
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Description |
254-257
The kinetics of thermal denaturation of a biliprotein, C-phycocyanin (C-PC) isolated from Spirulina platensis were studied at different pH values, ranging from 4.0 to 8.0. The denaturation of C-PC follows the first order kinetics and rate constant at pH 5.0 and temperature 55ºC is found to be 4.37 X 10-5 s-1, which increases to 5.46 X 10-5 s-1 at pH 7.0. The denaturation rate is much higher at 65ºC and pH 7.0 (7.96 X 10-4), as compared to at pH 5.0 (1.46 X 10-4). The thermal stability of C-PC is more at pH 5.0, as compared to other pH values. The observed differences in entropy values at pH 5.0, as compared to other pH values indicate a considerably close fit structure of the protein at pH 5.0, which increases the stability of native structure, even at higher temperature (65ºC). |
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Date |
2009-04-02T09:39:17Z
2009-04-02T09:39:17Z 2004-10 |
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Type |
Article
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Identifier |
0301-1208
http://hdl.handle.net/123456789/3719 |
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Language |
en_US
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Relation |
A 23 J 3
20 A 61 K 35 80 |
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Publisher |
CSIR
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Source |
IJBB Vol.41(5) [October 2004]
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