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KMID : 0385519970100010066
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Analytical Science & Technology
1997 Volume.10 No. 1 p.66 ~ p.74
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Kinetic Behavior of Immobilized Tyrosinase on Carbon in a Simulated Packed-Bed Reactor
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Shin Sun-Kyung
Kim Kyeo-Keun
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Abstract
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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 pplication for phenol degradation in waste water. A simulated reactor was a packed-bed rep ctor of 2.54cm in diameter´ and l0cm long, loaded with the immobilized carbon particle with an average diameter of 550m. 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 0.08445mNl(2.7ppm), 01689mM(5.4ppm) and 01.3378mM(9.5ppm) with the flow rat-es in the range of 60(1mL/s) to l80mL/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.
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KEYWORD
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