A new mechanism and kinetic model for the enzymatic synthesis of short-chain fructooligosaccharides from sucrose |
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| Institution: | 1. School of Biochemical Engineering, Pontificia Universidad Católica de Valparaíso, Avenida Brasil 2147, Valparaíso, Chile;2. Department of Biochemistry, Faculty of Pharmacy and Biochemistry, Universidad Nacional Mayor de San Marcos, Jr. Puno 1002, Lima, Peru;3. Centro Regional de Estudios en Alimentos Saludables, Conicyt-Regional, Gore Región de Valparaíso, R06i1004, Blanco 1623, Oficina 1402, Valparaíso, Chile;1. Department of Exact and Land Sciences, Integrated Regional University of the Alto Uruguai and Missões (URI), Av Sete de Setembro 1621, Postal Code: 99700-000, Erechim, Rio Grande do Sul, Brazil;2. Department of Bioscience, Multidisciplinary Institute on Health (IMS), Federal University of Bahia campus Anísio Teixeira (CAT/UFBA), R. Rio de Contas, 80, Candeias, Postal Code: 45.029-094, Vitória da Conquista, Bahia, Brazil;3. Department of Engineering and Computer Science, Integrated Regional University of the Alto Uruguai and Missões (URI), Av Sete de Setembro 1621, Postal Code: 99700-000, Erechim, Rio Grande do Sul, Brazil;4. Department of Agricultural Science, Integrated Regional University of the Alto Uruguai and Missões (URI), Av Sete de Setembro 1621, Postal Code: 99.700-000, Erechim, Rio Grande do Sul, Brazil;5. Department of Food Engineer, Faculty of Food Engineer (FEA), University of Campinas (UNICAMP), R. Monteiro Lobato, 80, Cidade Universitária, Postal Code: 13083-862. Campinas, São Paulo, Brazil;1. Laboratory of Flavor and Chromatography Analysis, Biological Division, Federal University Sergipe, Sao Cristovao, 49100-000, Brazil;2. Department of Applied Microbiology and Biotechnology, Dr. Harisingh Gour University, Sagar 470003, MP, India;3. Department of Mathematics and Sciences, College of Arts and Applied Sciences, Dhofar University, Salalah, 2112509, Sultanate of Oman;1. Department of Chemical Engineering, Federal University of São Carlos, P.O. Box 676, São Carlos 13565-905, SP 310, Brazil;2. Department of Chemical and Biomedical Engineering, West Virginia University, 1306 Evansdale Drive, Morgantown, WV 26506, USA;1. Division of Chemistry, School of Science, University of Phayao, Phayao 56000, Thailand;2. School of Chemistry, Institute of Science, Suranaree University of Technology, Nakhon Ratchasima 30000, Thailand;3. Center for Biomolecular Structure, Function and Application, Suranaree University of Technology, Nakhon Ratchasima 30000, Thailand;4. Department of Chemistry, Faculty of Science, Kasetsart University, Bangkok 10900, Thailand;1. School of Biochemical Engineering, Pontificia Universidad Católica de Valparaíso, Avenida Brasil 2147, Valparaíso, Chile;2. Department of Biochemistry, Faculty of Pharmacy and Biochemistry, Universidad Nacional Mayor de San Marcos, Jr. Puno 1002, Lima, Peru;3. Centro Regional de Estudios en Alimentos Saludables, Conicyt-Regional, Gore Región de Valparaíso, R06i1004, Blanco 1623, Oficina 1402, Valparaíso, Chile |
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| Abstract: | A kinetic model based on a ping-pong mechanism was developed under the steady-state hypothesis to account for the short-chain fructooligosaccharides (sc-FOS) synthesis using the commercial cellulolytic enzyme preparation, Rohapect CM. This new mechanism takes into account the interactions between the enzyme species and potential substrates (sucrose and sc-FOS) as a single complex reaction, allowing a better understanding of the reaction kinetics.The initial reaction rate laws appropriately describe the kinetic profiles of the examined substrates. Whereas sucrose exhibited Michaelis–Menten behavior with substrate inhibition, 1-kestose and nystose followed Michaelis–Menten and sigmoid enzyme kinetics. In addition, the enzyme was competitively inhibited by glucose and exhibited significant hydrolytic activity in the presence of nystose.The overall model was simultaneously fitted to experimental data from three initial sucrose concentrations (0.5, 1.5 and 2.1 M) using a multi-response regression with kinetic parameters that have biochemical relevance and are independent of the enzyme concentration. According to the model, sucrose acts almost exclusively as a fructosyl donor substrate. The mathematical development described herein is expected to be suitable for modeling similar enzymatic reaction systems. |
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| Keywords: | Enzyme biocatalysis Kinetic parameters Modeling Fructooligosaccharides Multi-response regression Sucrose |
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