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Received June 1, 2020
Accepted August 21, 2020
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Kinetic study of activation and deactivation of adsorbed cellulase during enzymatic conversion of alkaline peroxide oxidation-pretreated corn cob to sugar
Augustine Omoniyi Ayeni†
Oluranti Agboola
Michael Olawale Daramola1
Bianca Grabner2
Babalola Aisosa Oni
Damilola Elizabeth Babatunde
Joseph Evwodere
College of Engineering, Department of Chemical Engineering, Covenant University, Canaan land, Ota, Nigeria 1Department of Chemical Engineering, Faculty of Engineering, Built Environment and Information Technology, University of Pretoria, Hatfield, Pretoria 0028, South Africa 2Institute of Process and Particle Engineering, Graz University of Technology, Graz, Austria
Korean Journal of Chemical Engineering, January 2021, 38(1), 81-89(9), 10.1007/s11814-020-0667-2
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Abstract
Corn cob lignocellulosic biomass is one of the useful precursors for the alternative production of fuels and chemicals. Understanding the kinetics of enzymatic conversion of corn cob through kinetic models could provide indepth knowledge and increase the predictive ability for process design and optimization. In this study, models based on the semi-mechanistic rate equations, first-order decay exponential function of time for adsorbed enzymes, structural and diffusion coefficient for adsorption were used to estimate kinetic parameters for the enzymatic conversion of alkaline peroxide oxidation (APO) pretreated corn cob to sugar. Fitting a first-order inactivation model of adsorbed cellulases to account for experimental hydrolysis data, the apparent hydrolysis rate constant (k2=29.51 min-1), the inactivation rate constant (k3=0.269min-1), and reactivation rate constant (k4=0.0048min-1) were estimated. Regressed values of apparent maximum rate, Vmax, app, for adsorbed enzymes reduced appreciably with time to more than 98% at 96 h. The diffusion limit model showed that the diffusion resistance increased with increasing enzyme concentrations.
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Makarova EI, Budaeva VV, Kukhlenko AA, Orlov SE, 3 Biotech, 7, 317 (2017)
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Zhang Y, Xu JL, Xu HJ, Yuan ZH, Guo Y, Bioresour. Technol., 101(21), 8261 (2010)
Huang C, Lin W, Lai C, Li X, Jin Y, Yong Q, Bioresour. Technol., 285, 121355 (2019)
Jalak J, Valjamae P, Biotechnol. Bioeng., 106(6), 871 (2010)
Peri S, Karra S, Lee YY, Karim MN, Biotechnol. Prog., 23(3), 626 (2007)
Gan Q, Allen SJ, Taylor G, Process Biochem., 38(7), 1003 (2003)
Asenjo JA, Biotechnol. Bioeng., 25, 3185 (1983)
Hong J, Ye XH, Zhang YHP, Langmuir, 23(25), 12535 (2007)
Briggs GE, Haldane JB, Biochem. J., 19, 338 (1925)
Chrastil J, Wilson JT, Int. J. Biochem., 14, 1 (1982)
Chrastil J, Int. J. Biochem., 20, 683 (1988)
Gould JM, Biotechnol. Bioeng., 26, 46 (1984)
Ayeni AO, Omoleye JA, Mudliar S, Hymore FK, Pandey RA, Korean J. Chem. Eng., 31(7), 1180 (2014)
Miller GL, Anal. Chem., 31, 426 (1959)
Ayeni AO, Omoleye JA, Hymore FK, Pandey RA, Braz. J. Chem. Eng., 33, 33 (2016)
Yoo CG, Lee CW, Kim TH, Biomass Bioenergy, 35, 4901 (2011)
Lemos MA, Teixeira JA, Domingues MRM, Mota M, Gama FM, Microb. Technol., 32, 35 (2003)
Lloyd D, J. Mol. Evolut., 45, 370 (1997)
Bian J, Peng F, Peng XP, Peng P, Xu F, Sun RC, BioResources, 7, 4626 (2012)
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Holtzapple MT, Caram HS, Humphrey AE, Biotechnol. Bioeng., 26, 775 (1984)
Matsuno R, Taniguchi M, Tanaka M, Kamikubo T, Enz. Eng., 7, 158 (1984)