Relative Importance of Diffusion Layer Resistance and Microenvironmental Effects on the Effectiveness of Immobilized Enzyme Reactors

  • V. Kasche
  • A. Kapune
  • H. Schwegler


One goal of the physical-chemical description of immobilized enzyme reactors is to obtain enzyme independent relations where the efficiency and time dependence is expressed in terms of the properties of the environment (1). Previously the macro- and microenvironmental effects have been treated independently of each other instead of simultaneously. Therefore, it is necessary to describe the more realistic situation where the micro and macro effects are interrelated. The differential equations describing these systems do not have analytical solutions, so that numerical procedures must be applied. The collocation method has many advantages, as no restrictive assumptions are used and the solutions converge to the real solution (2). The aim of the present work was to investigate the relative importance of the macro- and micro-environmental factors for the steady-state effectiveness and time dependence (substrate conversion) of reactors with immobilized enzymes that catalyze the conversion of a single substrate by Michaelis-Menten kinetics. The theoretical results, obtained with the use of the collocation method, were compared with experimental data.


Diffusion Layer Collocation Method Sherwood Number Effectiveness Factor Substrate Conversion 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. 1.
    GOLDSTEIN, L. Meth. in Enzymology 44:397, 1976.CrossRefGoogle Scholar
  2. 2.
    RAMACHANDRAN, P.A. Biotechnol. Bioeng. 17: 211, 1975.CrossRefGoogle Scholar
  3. 3.
    SATTERFIELD, C.N. “Mass Transfer in Heterogenous Catalysts,” M.I.T. Press, Cambridge, Mass., 1970.Google Scholar
  4. 4.
    LEVICH, V.G. “Physicochemical Hydrodynamics,” Prentice Hall, Englewood Cliffs, N.J., 1962.Google Scholar
  5. 5.
    KASCHE, V., LUNDQVIST, H., BERGMAN, R. & AXEN, R. Biochem. Biophys. Res. Commun. 45: 615, 1971.CrossRefGoogle Scholar
  6. 6.
    KASCHE, V., AMNEUS, H., GABEL, D. & NASLUND, L. Biochim. Biophys. Acta 490: 1 1977.CrossRefGoogle Scholar
  7. 7.
    GABEL, D. & AXEN, R. Meth. in Enzymology 44:383, 1976.CrossRefGoogle Scholar
  8. 8.
    AXEN, R. MYRIN, P.A. & JANSON, J.C. Biopolymers 2: 401, 1970.CrossRefGoogle Scholar
  9. 9.
    RENKIN, E. J. Gen. Physiol. 38: 225, 1954.Google Scholar

Copyright information

© Plenum Press, New York 1978

Authors and Affiliations

  • V. Kasche
    • 1
  • A. Kapune
    • 1
  • H. Schwegler
    • 2
  1. 1.Biology DepartmentsUniversity of BremenBremenFederal Republic Germany
  2. 2.Physics DepartmentsUniversity of BremenBremenFederal Republic Germany

Personalised recommendations