| Autor: |
Radha, Remya, Gummadi, Sathyanarayana N. |
| Předmět: |
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| Zdroj: |
Indian Chemical Engineer; Oct2021, Vol. 63 Issue 4, p425-434, 10p |
| Abstrakt: |
pH and temperature are the most predominant parameters affecting protein macromolecular properties like activity and stability. Optimisation of these parameters is crucial for their industrial applications. L-asparaginase because of its broad use in food industry and chemotherapy become an ideal candidate for intensive research. Present study focused the influence of temperature and pH on activity and stability of Vibrio cholerae L-asparaginase using response surface methodology. Experimental data were fitted into the quadratic model and the optimal conditions for enzyme activity and stability were found out. Optimum pH and temperature for specific activity were found to be 7.1 and 38.5 °C and for half-life time it was 6.9 and 23°C. Validation at optimised conditions improved the enzyme activity and stability to 1536 ± 55 U/mg and 1077.4 ± 77 min respectively. The variation in the secondary structure of protein by Far UV CD spectroscopy studies was found to be good enough to predict the changes in stability and activity with respect to the interaction effect of pH and temperature. Extreme lower conditions of pH and higher temperature caused a visible decrease in alpha-helical secondary signatures of protein and thereby reduced stability and activity of protein. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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