Kinetic Behavior of Immobilized Tyrosinase on Carbon in a Simulated Packed-Bed Reactor

충전층에서 탄소에 고정시킨 Tyrosinase의 반응속도에 관한 연구

  • Received : 1996.08.01
  • Published : 1997.02.25

Abstract

Influence of the axial dispersion on immobilized enzyme catalytic bed was investigated in order to examine the kinetic behavior of the biocatalysis. The enzyme employed in this study was the tyrosinase(EC 1.14.18.1) immobilized on carbon support : this system requires two substrates of phenol and oxygen. This enzyme has potential application for phenol degradation in waste water. A simulated reactor was a packed-bed reactor of 2.54cm in diameter and 10cm long, loaded with the immobilized carbon particle with an average diameter of $550{\mu}m$. A phenol feed in the strength of 55.5mM(5220ppm) was used to observe the behavior of the immobilized enzyme column at three different dissolved oxygen levels of 0.08445mM(2.7ppm), 0.1689mM(5.4ppm) and 0.3378mM(9.5ppm) with the flow rates in the range of 60(1mL/s) to 180mL/min(3mL/s). Examination of the Biot number and Damkolher numbers of the immobilized system enables us to eliminate the contribution of external mass transfer to set of differential equations derived from the dispersion model. Solution of the equation was finally obtained numerically with the application of the Danckwert boundary conditions and the assumed zero-and first order rates on the non-linear two substrate enzyme kinetics. Higher conversion of phenol was observed at the low flow rates and at the higher oxygen concentration. Comparison of axial dispersion and plug flow model showed that no detectable difference was observed in the column outlet conversion between the axial and the plug flow models which was in complete agreement with the previous studies.

Keywords

axial dispersion;immobilized enzyme;tyrosinase;phenol;kinetics

Acknowledgement

Supported by : 청주대학교