Diffusion and adsorption phenomena in an immobilized enzyme reactor using adsorbed polymer for attachment of the enzyme in porous alumina particles
✍ Scribed by Michael C. Hu; E.R. Haering; C.J. Geankoplis
- Publisher
- Elsevier Science
- Year
- 1985
- Tongue
- English
- Weight
- 888 KB
- Volume
- 40
- Category
- Article
- ISSN
- 0009-2509
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✦ Synopsis
Experiments were pcrfonned to study the effects of an immobilized enzyme on the adsorption capacity and on the diffusion in a poro& solid. The enzyme invertase was immobilized by covalently binding it to a polymer matrix adsorbed in the pores of alumina. The enzyme was found to hydrolyse sucrose to glucose plus fructose with an initial activity of 630~mol/min-g alumina. Data on the long-term stability showed a 14 % decrease in initial activity in 22 days. The adsorption of glucose, fructose, or sucrose alone on porous alumina and on porous ahunina containing polymer and immobilized invertase was investigated. The presence of immobilized invertase and polymer matrices decreased the adsorption capacity by about 75 %.
The presence of immobilized invert+ on the adsorbed polymer matrices also raised the experimental tortuosity factor for diffusion in the pores from 2.0 for plain alumina to 2.75 for invertase immobilized on alumina. The decrease of particle void fraction, the enzyme blockage effect, and an increase in pore restriction effect were used to explain the increase of the tortuosity factor.