Quick identification of a simple enzyme deactivation model for an extended-Michaelis-Menten reaction type. Exemplification for the D-glucose oxidation with a complex enzyme deactivation kinetics |
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| Affiliation: | 1. State Key Laboratory of Analytical Chemistry for Life Science, School of Chemistry and Chemical Engineering, Nanjing University, Collaborative Innovation Center of Chemistry for Life Sciences, Nanjing 210093, China;2. Institute of Microanalytical Systems, Department of Chemistry, Zhejiang University, Hangzhou 310058, China;1. Laboratory of Xenobiotic Metabolism, Department of Health Pharmacy, Yokohama University of Pharmacy, 601 Matano-cho, Totsuka-ku, Yokohama 245-0066, Japan;2. Laboratory of Environmental Toxicology, Department of Health Pharmacy, Yokohama University of Pharmacy, 601 Matano-cho, Totsuka-ku, Yokohama 245-0066, Japan;3. Laboratory of Hygienic Chemistry, Faculty of Pharmacy, Meijo University, 150 Yagotoyama, Tempaku-ku, Nagoya 468-8503, Japan;1. Department for Innovation in Biological, Agro-Food and Forest Systems, University of Tuscia, via S. Camillo de Lellis, 01100 Viterbo, Italy;2. Department of Ecological and Biological Sciences, University of Tuscia, via S. Camillo de Lellis, 01100 Viterbo, Italy |
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| Abstract: | One essential engineering problem when developing an industrial enzymatic process concerns the model-based design and optimal operation of the enzymatic reactor based on the process and enzyme inactivation kinetics. For a complex enzymatic system, the “default” used first-order enzyme deactivation model has been proved to lead to inadequate process design or sub-optimal operating policies. The present study investigates if a complex enzyme deactivation can be approximated with simple 1st, 2nd, or a novel proposed model with variable deactivation constant. The approached complex enzymatic system is those of the oxidation of D-glucose to 2-keto-D-glucose in the presence of pyranose 2-oxidase. The necessary “simulated experimental data” have been generated by means of an extended kinetic model from literature used to simulate a batch reactor under well-defined nominal conditions. The proposed enzyme deactivation model has been found to be the best lumping alternative, presenting several advantages: simplicity, flexibility, and a very good adequacy. |
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| Keywords: | Enzyme deactivation kinetics Kinetic model discrimination D-glucose oxidation Pyranose oxidase Pseudo first order deactivation |
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