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2020 | 142 | 135-149
Article title

Differential Transform Method for the Kinetic Analysis of Thermal Inactivation of Enzyme as Applied in Biotechnology

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EN
Abstracts
EN
In this work, approximate analytical solution is developed using differential transformation method for finding the molar concentration of the native and denatured enzyme in terms of second-order rate constant. Also, the obtained solutions are used to study the kinetics of thermal inactivation of enzyme as applied in biotechnology. The analytical solution was validated with numerical solution using fourth- order Runge-Kutta. Good agreement was established between the numerical and approximated analytical solutions.
Year
Volume
142
Pages
135-149
Physical description
Contributors
author
  • Department of System Engineering, University of Lagos, Akoka, Lagos, Nigeria
  • Department of Mechanical Engineering, University of Lagos, Akoka, Lagos, Nigeria
  • Department of Mathematics, University of Lagos, Akoka, Lagos, Nigeria
References
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  • [8] M. Hirai, R. Kawai-Hirai, T. Hirai, and T. Ueki. Structural change of jack bean urease induced by addition of surfactants studied with synchrotron-radiation small-angle X-ray scattering. European Journal of Biochemistry, vol. 215, no. 1, pp. 55-61, 1993
  • [9] R. W. Lencki, J. Arul, and R. J. Neufeld. Effect of subunit dissociation, denaturation, aggregation, coagulation, and decomposition on enzyme inactivation kinetics: II. Biphasic and grace period behavior. Biotechnology and Bioengineering, vol. 40, no. 11, pp. 1427-1434, 1992
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  • [12] S. J. Liao, Beyond Perturbation: Introduction to the Homotopy Analysis Method, Chapman and Hall, CRC Press, Boca Raton, Fla, USA, 1st Edition, 2003.
Document Type
article
Publication order reference
Identifiers
YADDA identifier
bwmeta1.element.psjd-acb93685-e622-432a-947f-52ef9502c46f
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