Team:SCUT-China/Modeling/Overview

To prove the accuracy of kinetic equations of the related domains, we stacked the related equations according to the sequence of DEBS 1. When establishing the kinetic model of domain, we got into trouble. According to the analysis of reaction mechanism and kinetic equation we show before, the initial value of the kinetic equations on second AT domain depends on the concentration of DEBS 1, that is, the result of the kinetic equations on Module 2 are not affected by the result of previous domains.

However, if we have a further simplified model in which the second AT domain is ignored, the whole kinetic model stacked will be affected by the whole DEBS 1, including Loading, Module 1, Module 2.

Therefore, we establish two kinetic models stacked, and compare them with each other. Then we compare them with the kinetic model of the whole DEBS 1.

Aimed at the final goal of our project, we simulated the kinetic equations of chemical reactions occurring in each domain, including AT, ACP, KS, KR, ER, DH, and TE. Then we tested these equations and analyzed their feasibility.

DEBS 1 is the first part of the PKS which catalyzes and synthesizes 6dEB, the precursor of erythromycin. Its domain sequence is AT, ACP, KS, AT, KR, ACP, KS, AT, KR, ACP. Theoretically, the kinetic model of domains which have been stacked is match with the kinetic model of DEBS 1+TE.

In modeling section, we kept pace with the members who are responsible for experiment. We stacked the related equations according to the sequence of DEBS 1+TE. Meanwhile, we also simulated the kinetic equations of the whole DEBS 1+TE. Then we compared the equations of domains which have been stacked with the equation of DEBS 1+TE, and verified the feasibility of the model.