Kinetic studies on thermal denaturation of C-phycocyanin.
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 55 degrees C is found to be 4.37 x 10(-5) s(-1), which increases to 5.46 x 10(-1) s(-1) at pH 7.0. The denaturation rate is much higher at 65 degrees C 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 (65 degrees C).
Central Salt and Marine Chemicals Research Institute, Gijubhai Badheka Marg, Bhavnagar 364002, Gujarat, India.
Anamika
A
Patel
Richa
R
Pawar
Sandhya
S
Mishra
Shailendra
S
Sonawane
P K
PK
Ghosh
D000458:Cyanobacteria / Q000378:metabolism; D019277:Entropy; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D052979:Phycobiliproteins / Q000737:chemistry; D010798:Phycocyanin / Q000737:chemistry*; D053545:Spirulina / Q000378:metabolism; D013696:Temperature; D013997:Time Factors
D052979:Phycobiliproteins; D010798:Phycocyanin