Mathematical modelling and kinetic study for CD production catalysed by Toruzyme® and CGTase from Bacillus firmus strain 37

Mathematical modelling and kinetic study for CD production catalysed by Toruzyme® and CGTase... A new mathematical model was developed for the kinetics of α-, β- and γ-cyclodextrin production, expanding an existing model that only included the production of β- and γ-cyclodextrins, because a detailed kinetic modelling of the reactions involved allows the manipulation of the process yields. The kinetic behaviour of the commercial enzyme Toruzyme® was studied with maltodextrin as substrate at different concentrations and for CGTase from Bacillus firmus strain 37 at a concentration of 100 g L−1. The mathematical model showed a proper fit to the experimental data, within the 24-h period studied, confirming that the considered hypotheses represent the kinetic behaviour of the enzymes in the reaction medium. The kinetic parameters generated by the model allowed reproducing previous observed qualitative tendencies as it can be seen that changing experimental conditions in the reaction process such as enzyme and substrate concentrations results in large changes in the enzyme kinetics and using high substrate concentrations does not guarantee the highest conversion rates due to enzyme inhibition and reverse reactions. In addition, this new mathematical model complements previous qualitative observations enabling the manipulation of the direct and reverse reactions catalysed by the enzyme by adjusting the reaction conditions, to target quantitative results of increased productivity and better efficiency in the production of a desired cyclodextrin. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Bioprocess and Biosystems Engineering Springer Journals

Mathematical modelling and kinetic study for CD production catalysed by Toruzyme® and CGTase from Bacillus firmus strain 37

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Publisher
Springer Berlin Heidelberg
Copyright
Copyright © 2017 by Springer-Verlag Berlin Heidelberg
Subject
Chemistry; Biotechnology; Industrial and Production Engineering; Environmental Engineering/Biotechnology; Industrial Chemistry/Chemical Engineering; Food Science
ISSN
1615-7591
eISSN
1615-7605
D.O.I.
10.1007/s00449-017-1789-8
Publisher site
See Article on Publisher Site

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