دانلود رایگان مقاله طراحی غشای بیوراکتور بر عملکرد بیوکاتالیتیک گلوکز اکسیداز و کاتالاز

ABSTRACT

Membrane separation of xylose and glucose can be accomplished via oxidation of glucose to gluconic acid by enzymatic glucose oxidase catalysis. Oxygen for this reaction can be supplied via decomposition of hydrogen peroxide by enzymatic catalase catalysis. In order to maximize the biocatalytic productivity of glucose oxidase and catalase (gluconic acid yield per total amount of enzyme) the following system set-ups were compared: immobilization of glucose oxidase alone; co-immobilization of glucose oxidase and catalase; glucose oxidase and catalase free in the membrane bioreactor. Fouling-induced enzyme immobilization in the porous support of an ultrafiltration membrane was used as strategy for entrapment of glucose oxidase and catalase. The biocatalytic productivity of the membrane reactor was found to be highly related to the oxygen availability, which in turn depended on the reactor configuration, hydrogen peroxide concentration and catalase origin. When glucose oxidase and catalase (from Aspergillus niger) were free in themembrane bioreactor a total biocatalytic productivity of 122 mg gluconic acid/mg enzyme was obtained after five consecutive reaction cycles. The free enzymes showed superior performance compared to the immobilized systems as a result of limited substrate and product diffusion in the latter case.

4. Conclusions

A number of experiments were conducted to elucidate the impact of different parameters on the biocatalytic productivity of glucose oxidase and catalase in a membrane bioreactor. While productivity was found to depend on the oxygen availability which in turn depended on reactor configuration, hydrogen peroxide concentration and catalase origin, the contribution of other factors requires further evaluation in the particular enzyme systems that they influence. Robustness of the immobilized enzymes against local pH effects, hydrogen peroxide and other factors could possibly play a larger role than revealed in the stability studies of the free enzymes. The study contributes to explaining the differences in performance of free versus immobilized systems for glucose oxidase and catalase and other coupled enzyme reactions with similar characteristics.