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- aggregation classification "C1".
- aggregation creator B101076.
- aggregation creator B101077.
- aggregation creator person.
- aggregation creator person.
- aggregation creator person.
- aggregation creator person.
- aggregation date "2008".
- aggregation hasFormat 430633.bibtex.
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- aggregation isPartOf urn:issn:978-972-97810-4-9.
- aggregation language "eng".
- aggregation publisher "Universidade do Minho, Departamento de Engenharia Biológica".
- aggregation subject "Biology and Life Sciences".
- aggregation title "A graphical approach for rationalization of bi-enzymatic reactions based on a kinetic model".
- aggregation abstract "A model and a graphical method have been developed to describe and visualize the interaction between two enzymes with a redox mediator. In this bi-enzymatic process, the enzyme cellobiose dehydrogenase (CDH; EC 1.1.99.18) oxidizes lactose at the C-1 position of the reducing sugar moiety to lactobionolactone, which spontaneously hydrolyzes to lactobionic acid. 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) diammonium salt (ABTS) is used as electron acceptor and is continuously regenerated by laccase (EC 1.10.3.2). Oxygen is the terminal electron acceptor and is fully reduced to water by laccase, a copper containing oxidase. Oxygen is added to the system by means of bubble-free oxygenation. The general aim is to assist in understanding the process and to provide a tool for rational design of similar biocatalytic processes leading to intensification and/or a more efficient use of the biocatalysts and redox mediator. This can be accomplished by describing the reaction system with differential equations and integrating them over a desired time interval. Hence, the simulation of reactions of much greater complexity can be attained in comparison with addressing a Michaelis–Menten, steady-state approach. We focused on elaborating a methodology to determine the influence of the limiting rate of cellobiose dehydrogenase and laccase and the initial ABTS concentration on the productivity for a given oxygen mass transfer coefficient. This way, the use of the enzymes and the redox mediator ABTS can be rationalized. Using the model, the productivity of the process is investigated by simultaneous solution of the rate equations for varying enzyme quantities and redox mediator concentrations, solved with the aid of a numerical solution. The isocharts developed in this work, provide a novel and easy-to-use graphical tool to determine optimal process conditions. The used methodology can be extended for similar and other enzymatic conversions with cofactor regeneration. The accuracy of the model has been assessed and is in good agreement with experimental data.".
- aggregation authorList BK259738.
- aggregation endPage "785".
- aggregation startPage "784".
- aggregation isDescribedBy 430633.
- aggregation similarTo LU-430633.