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A graphical method of determining the Michaelis-Menten constant free of external mass transfer resistance for immobilized enzymes in a packed bed reactor

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Summary

A graphical method of determining the Michaelis-Menten constant free of the external mass transfer resistance for a packed bed immobilized enzyme system was illustrated with examples from 3 different enzyme reactions. The intercept at the ordinate obtained by the straight line extrapolation of data points in the plot of apparent Km value vs. the reciprocal of superficial velocity in column allowed an easy calculation of Km free of external mass transfer resistance. An asymptotic value of apparent Km value at infinite zero superficial velocity was ascribed to the fact that the mass transfer coefficient kL, approached a definite value at this condition.

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Abbreviations

Km :

Michaelis-Menten constant, M/L3

Km':

Km free of external mass transfer resistance in a given ionic strength, M/L3

Km":

apparent Km with external mass transfer resistance, M/L3

S:

substrate concentration, M/L3

So :

initial substrate concentration, M/L3

k2 :

rate constant, t-1

E:

enzyme concentration in support, M/L3

ɛ:

void volume per unit volume of reactor, dimensionless

u:

superficial velocity of substrate, L/t

KL :

mass transfer coefficient in liquid film, L/t

a:

external surface area of support per unit volume of reactor, L-1

ξ:

ratio of average channeling length to particle diameter, dimensionless

dp :

diameter of support particle, L

X:

fractional conversion of substrate, dimensionless

H:

partition coefficient, dimensionless

k:

a constant, 3 k2E(1-ɛ)ξdp/4

T:

space time, t

N:

molecular flux, M/L2t

r:

radius of immobilized enzyme particle, L

References

  1. Lilly, M.D. and Hornby, W.E. (1966) Biochem. J. 100, 718

    Google Scholar 

  2. Gelf, G. Thomas, D., Brown, G. and Kernevez, J.F. (1974) Biotechnol. Bioeng. 16, 315

    Google Scholar 

  3. Toda, K. (1975) Biotechnol. Bioeng. 17, 1729

    Google Scholar 

  4. Kobayashi, T. and Moo-Young, M. (1971) Biotechnol. Bioeng. 13, 893

    Google Scholar 

  5. Kobayashi, T. and Moo-Young, M. (1973) Biotechnol. Bioeng. 15, 47

    Google Scholar 

  6. Balasingham, K., Warburton, D., Dunnill, P. and Lilly, M.D. (1972) Biochim. Biophys. Acta 276, 250

    Google Scholar 

  7. Cole. M. (1969) Biochem. J. 115, 733

    Google Scholar 

  8. Park, Jong M., Choi, C.Y. Seong, B.L. and Han, M.H. to be Published

  9. Brian, P.L.T. and H.B. Hales (1969) AIChE J. 15, 419

    Google Scholar 

  10. Friedlander, S.K. (1957) AIChE J. 3, 43

    Google Scholar 

  11. Friedlander, S.K. (1961) AIChE J. 7, 347

    Google Scholar 

  12. Hornby, W.E., Lilly, M.D. and Crook, E.M. (1968) Biochem. J. 107, 669

    Google Scholar 

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Seong, B.L., Han, M.H., Park, J.M. et al. A graphical method of determining the Michaelis-Menten constant free of external mass transfer resistance for immobilized enzymes in a packed bed reactor. Biotechnol Lett 3, 607–612 (1981). https://doi.org/10.1007/BF00158687

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  • DOI: https://doi.org/10.1007/BF00158687

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