Thermodynamic Characterization of Saccharomyces cerevisiae Catalyzed Fermentation of Cane Sugar

Egharevba Felix, Ogbebor Clara, Akpoveta Oshevwiyo Vincent

Department of Chemistry, Ambrose Alli University, Ekpoma, Nigeria.

DOI: 10.4236/ojpc.2014.41004                

Abstract

The rate of cane sugar fermentation with Saccharomyces cerevisiae was studied at temperatures between 30°C and 42°C in order to characterize the process using thermodynamic parameters such as enthalpy (ΔH^*), activation energy (ΔE^*), entropy (ΔS^*), Gibbs free energy (ΔG^*) and equilibrium constant (K). The parameters were evaluated on the basis of a consideration of Arrhenius, Eyring and Van’t Hoff’s equations. The results obtained are ΔH^*, 91.85 KJ·mol^-1; ΔE^*, 91.85 KJ·mol^-1, ΔS^*, 2763 J·mol^-1K^-1; ΔG^*, -762.09 KJ·mol^-1, and equilibrium constant, K, 1.34 dm³·mol^-1. These values were subsequently used to obtain by calculation the rate constant of the fermentation k, 1.43 × 10¹¹ min^-1, Arrhenius constant A (pre-exponential or frequency factor), 4.79 × 10²⁶ min^-1, orientation parameter, P, 4.48 × 10¹⁵ and the collision frequency Z, 1.07 × 10¹¹ min^-1. Finally the fermentation efficiency calculated on the basis of a complete combustion of glucose is 377.8%. The results showed that though the fermentation process is kinetically controlled, it is suggested that the positive impact of the feasible thermodynamics is limited by other process variables.

Keywords

Fermentation; Substrate Concentration; Kinetics; Cane sugar; Thermodynamic Parameters

Conflicts of Interest

The authors declare no conflicts of interest.

References

[1]	R. Chang, “Physical Chemistry with Applications to Biological Systems,” Macmillan, New York, 1990, pp. 251-253.
[2]	R. D. Levine, “Molecular Reaction Dynamics,” Cambridge Univ. Press, London, 2005, pp. 78-82. http://dx.doi.org/10.1017/CBO9780511614125
[3]	I. Haq, M. M. Javid, U. Hamid and F. Adnan, “Kinetic and Thermodynamic Studies of Alpha Amylose from Bacillus Licheniformic Mutant, Park,” Journal of Botany, Vol. 42, No. 5, 2010, pp. 3507-3516.
[4]	C. Duy and J. Fitter, “Thermostability and Irreversible Unfolding Amylases Analyzed by Unfolding Kinetics,” Journal of Biological Chemistry, Vol. 280, No. 45, 2005, pp. 37360-37365. http://dx.doi.org/10.1074/jbc.M507530200
[5]	R. Eisenthal, M. J. Danson and D.W. Hough, “Catalytic Efficiency and Kcat/Km: A Useful Comparator?” Trends in Biotechnology, Vol. 25, No. 6, 2007, pp. 247-249. http://dx.doi.org/10.1016/j.tibtech. 2007.03.010
[6]	H. Eyring, “The Activated Complex in Chemical Reactions,” The Journal of Chemical Physics, Vol. 3, No. 2, 1935, p. 107.
[7]	A. S. Negi and S. C. Anand, “A Textbook of Physical Chemistry,” New Age Publiishing, New Delhi, 2007, pp. 714-718.
[8]	C. Blanch and R. Clark, “The Effect of Temperature and pH on Enzyme Kinetics,” In: C.-W. Park and E. Zipp, Eds., Introduction to Biochemical Engineering, Harwood, London, 2000, 1997, pp. 120-125.
[9]	S. Arrhenius, In: E. L. Gaden, Ed., Fermentation Process Kinetics, Biotechnology and Bioengineering, Vol. 67, No. 6, 1889, pp. 116-118.
[10]	J. H. Van’t Hoff, In: P. Atkins and J. De Paula, Eds., Physical Chemistry, 8th Edition, Freeman & c. New York, 2006, p. 212.
[11]	K. J. Laidler and M. C. King, “The Development of Transistion State Theory,” Journal of Physical Chemistry, Vol. 87, No. 15, 1983, pp. 2657-2664. http://dx.doi.org/10.1021/j100238a002
[12]	L. R. Lynd, J. H. Cushman, R. J. Nicholas and C. E. Wyman, “Fuel Ethanol from Cellulosic Biomass,” Science, Vol. 251, No. 4999, 1991, pp. 1318-1323. http://dx.doi.org/10.1126/science.251.4999.1318
[13]	J. B. Doran, H. C. Aldrich and L. O. Ingram, “Sacharification and Fermentation of Sugar Cane Bagasse by Klebsiella Oxytoca Containing Chromosomally Integrated Genes Encoding the Zymomonas Mobilis Ethanol Pathway,” Biotechnology and Bioengineering, Vol. 44, No. 2, 1994, pp. 240-247. http://dx.doi.org/10.1002/bit.260440213
[14]	R. A. Copeland, “Enzymes: A Practical Introduction to Structure and Mechanism and Data Analysis,” 2nd Edition, Wiley VCH, New York, 2000, pp. 78-84. http://dx.doi.org/10.1002/0471220639
[15]	M. Riaz, R. Parveen, M. R. Javed, H. Nadeem and M. H. Rashi, “Kinetics and Thermodynamic Properties of Noval Glucoamylase from Humicola sp. Enzyme,” Microbial Technology, Vol. 41, No. 5, 2007, pp. 558-564. http://dx.doi.org/10.1016/j.enzmictec.2007.05.010
[16]	A. Tanaka and E. Hoshino, “Secondary Calcium Binding Parameter of Bacillus Amyloliquefacions Amylase Obtained from Inhibition Kinetics,” Journal of Biosciences and Bioengineering, Vol. 96, No. 3, 2003, pp. 262-268.
[17]	J. J. Malinowski, “Two Phase Partitioning Bioreactors in Fermentation Technology,” Biotechnol Advances, Vol. 19, No. 7, 2001, pp. 525-538. http://dx.doi.org/10.1016/S0734-9750(01)00080-5
[18]	Y. A. Pisarenko, L. A. Serafimov, C. A. Cardona, O. E. Efromov and A. S. Schuwalov, “Reactive Distillation Design: Analysis of the Process Design,” Review in Chemical Engineering, Vol. 17, No. 4, 2001, p. 253. http://dx.doi.org/10.1515/REVCE.2001.17.4.253
[19]	N. Leksawasdi, L. A. Joachimsthal and P. L. Rogers, “Mathematical Modeling of Ethanol Production from Glucose/Xylose Mixtures by Recombinant Zymomonas Mowbilis,” Biotechnology Letters, Vol. 23, No. 13, 2001, pp. 1087-1093. http://dx.doi.org/10.1023/A:1010599530577