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International Journal of Current Microbiology and Applied Sciences (IJCMAS)
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National Academy of Agricultural Sciences (NAAS)
NAAS Score: *5.38 (2020)
[Effective from January 1, 2020]
For more details click here

ICV 2019: 96.39
Index Copernicus ICI Journals Master List 2019 - IJCMAS--ICV 2019: 96.39
For more details click here

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PRINT ISSN : 2319-7692
Online ISSN : 2319-7706
Issues : 12 per year
Publisher : Excellent Publishers
Email : editorijcmas@gmail.com / submit@ijcmas.com
Editor-in-chief: Dr.M.Prakash
Index Copernicus ICV 2018: 95.39
NAAS RATING 2020: 5.38

Int.J.Curr.Microbiol.App.Sci.2021.10(6): 740-749
DOI: https://doi.org/10.20546/ijcmas.2021.1006.081


Thermodynamics and Kinetics of Thermal Inactivation of Polyphenol Oxidases and Peroxidase of Three Tissues (Cambium, Central Cylinder, Internal Bark) of Cassava Roots (Manihot esculenta CRANTZ) varietie Bonoua 2, Cultivated in Côte d’Ivoire
Yapi Jocelyn Constant1*, Djina Yves2, Gnanwa Mankambou Jacquesand Kouame Lucien Patrice2
1Department of Biochemistry and Microbiology, Agroforestry Unit, University Lorougnon Guede, BP 150 Daloa, (Côte d’Ivoire) 2Department of Biochemistry and Food Technology, University Nangui Abrogoua-02 BP 801 Abidjan 02, (Côte d’Ivoire)
*Corresponding author
Abstract:

The effect of heat treatment on polyphenoloxidases and peroxidase activities in three tissues (cambium, central cylinder and internal bark) of the varietie of cassava roots (Manihot esculenta CRANTZ) Bonoua 2 were studied over a range of 30 to 70 °C, using pyrogallol, 4-methylcatechol, dopamine and pyrocatechol as a substrates for polyphenol oxydase and guaiacol as a substrate for peroxidase. Optimal conditions for enzymatic studies were determined to between pH 8.6 and 9.6 for polyphenoloxydases and pH 6.6 and 7.6 for peroxidase and 25-45 °C. T1/2-values of enzymatic activities are between 2.22 and 4.27 min at 70 °C, they decreased with increasing temperature, indicating a difference thermostability of each enzyme. D- and k-values decreased and increased, respectively, with increasing temperature, indicating faster of these enzymes inactivation at higher temperatures. Results suggested that polyphenoloxydases and peroxidase were relatively thermostable enzymes with a Z-value which vary from 21.49 at 37.76 °C and Ea of 75.84 at 139.17 kJmol-1. Thermodynamic parameters were also calculated. The Gibbs free energy ΔG values range from 47.33 to 265.85 kJ/mol. These kinetic data can be used to predict prevention of browning in the cassava roots (Manihot esculenta CRANTZ) by thermal inactivation of enzymes.


Keywords: Cassava, polyphenol oxidases, peroxidase, enzymatic browning, thermal inactivation, thermodynamic and kinetics
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How to cite this article:

Yapi Jocelyn Constant, Djina Yves, Gnanwa Mankambou Jacques and Kouame Lucien Patrice. 2021. Thermodynamics and Kinetics of Thermal Inactivation of Polyphenol Oxidases and Peroxidase of Three Tissues (Cambium, Central Cylinder, Internal Bark) of Cassava Roots (Manihot esculenta CRANTZ) varietie Bonoua 2, Cultivated in Côte d’Ivoire.Int.J.Curr.Microbiol.App.Sci. 10(6): 740-749. doi: https://doi.org/10.20546/ijcmas.2021.1006.081