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Preparation and properties of gel entrapped enzymes

  • F. O'Driscoll
Conference paper
Part of the Advances in Biochemical Engineering book series (ABE, volume 4)

Keywords

Immobilize Enzyme Enzyme Loading Suspension Polymerization Immobilization Technique Internal Mass Transfer 
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.

Nomenclature

D

diffusion coefficient of substrate in gel

[E]gel

active enzyme concentration per unit volume of gel

F

function defined by Eq. (3)

H

fractional extent of hydiation of gel

kc

catalytic constant of enzyme in gel

Km

Michaelis constant of enzyme in gel

l

membrane thickness

M

molecular weight of substrate

R

radius of spherical gel particles

[S]

substrate concentration in gel

υ

rate of enzyme catalyzed reaction per unit volume of gel

α

defined by Eq. (4)

β

Damköhler number =α 2 l 2, or =α 2 R 2

η

effectiveness factor, i. e.: rate catalyzed by gel entrapped enzyme relative to rate of free enzyme under equivalent conditions

φ

Thiele modulus (Eq. 6)

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References

  1. 1a.
    “Immobilized Enzymes: A Compendium of References...” Corning Glass Works, Corning, N. Y., 1972.Google Scholar
  2. 1b.
    Zaborsky, O. R.: “Immobilized Enzymes” CRC Press, Cleveland O., 1973.Google Scholar
  3. 2a.
    Yasuda, H., Peterlin, A., Colton, C. K., Smith, K. A., Merrill, E. W.: Makromol. Chem. 126, 177 (1969).CrossRefGoogle Scholar
  4. 2b.
    Yasuda, H., Lamaze, C. E., Peterling, A.: J. Polymer Sci. A-2, 9 1117 (1971).CrossRefGoogle Scholar
  5. 3.
    Bernfeld, P., Wan, J.: Science 142, 678, (1963).CrossRefGoogle Scholar
  6. 4.
    O'Driscoll, K. F., Izu, M., Korus, R.: Biotechnol. Bioeng. 14, 847, (1972).CrossRefGoogle Scholar
  7. 5.
    Miyamura, M., Suzuki, S.: Nippon Kagaku Kaishi, 7, 1274, (1972).Google Scholar
  8. 6a.
    Turkova, J., Hubalkova, O., Krivakova, M., Coupek, J.: Biochim. Biophys. Acta. 322, 1, (1973).Google Scholar
  9. .6b.
    Gould, F. E., Ronel, S. H.: Germ. Pat. No. 2, 305, 320 (1973).Google Scholar
  10. 7.
    Degani, Y., Miron, T.: Biochim. Biophys. Acta. 212, 362, (1970).Google Scholar
  11. 8.
    Korus, R., Ph. D. Thesis: University of Waterloo, Waterloo, Ontario, (1974).Google Scholar
  12. 9.
    O'Driscoll, K. F., Kapoulas, A.: unpublished work.Google Scholar
  13. 10.
    Nilsson, H., Mosbach, R., Mosbach, K.: Biochim. Biophys. Acta 268, 253, (1972).Google Scholar
  14. 11.
    Beck, S. R., Rase, H. F.: Ind. Eng. Chem. Prod. Res. Develop. 12, 260, (1973).CrossRefGoogle Scholar
  15. 12.
    Mosbach, K., Mosbach, R.: Acta Chem. Scand., 20, 2807, (1966).CrossRefGoogle Scholar
  16. 13.
    Mosbach, K., Larsson, P.-O.: Biotechnol. Bioeng. 12, 19, (1970).CrossRefGoogle Scholar
  17. 14.
    Slowinski, W., Charm, S. E.: Biotechnol. and Bioeng. 15, 973, (1973).CrossRefGoogle Scholar
  18. 15.
    Turkova, J., Hubalkova, O., Krivakova, M., Coupek, J.: Biochim. Biophys. Acta. 322, 1, (1973).Google Scholar
  19. 16.
    Dobo, J.: Acta. Chim. Acad. Sci. Hung. 63, 453, (1970) through CA 72: 96979 m (1970).Google Scholar
  20. 17.
    Maeda, H., Yamauchi, A., Suzuki, H.: Biochim. Biophys. Acta. 315, 18, (1973).Google Scholar
  21. 18.
    Dickey, F. H.: J. Phys. Chem., 59, 695, (1955).CrossRefGoogle Scholar
  22. 19.
    Johnson, P., Whateley, T. L.: J. Colloid Interface Sci. 37, 557, (1971).CrossRefGoogle Scholar
  23. 20a.
    Brown, H. D., Patel, A. B., Chattopadhyay, S. K.: J. Biomed. Mater. Res. 2, 231, (1968).CrossRefGoogle Scholar
  24. 20b.
    Pennington, S. N., Brown, H. D., Patel, A. B., Knowles, C. O.: Biochim. Biophys. Acta. 167, 479, (1968).Google Scholar
  25. 20c.
    Pennington, S. N., Brown, H. D., Patel, A. B., Chattopadhyay, S. K.: J. Biomed. Mater. Res. 2, 443,(1968).CrossRefGoogle Scholar
  26. 21.
    Guilbault, G. G., Das, J.: Anal. Biochem. 33, 341, (1970).CrossRefGoogle Scholar
  27. 22a.
    Bauman, E. K., Goodson, L. H., Guilbault, G. G., Kramer, D. N.: Anal. Chem. 37, 1378 (1965).CrossRefGoogle Scholar
  28. 22b.
    Guilbault, G. G., Kramer, D. N.: Anal. Chem., 37, 1675, (1965).CrossRefGoogle Scholar
  29. 23.
    Maeda, H., Suzuki, H., Yamauchi, A.: Biotechnol. Bioeng. 15, 607, 827, (1973).CrossRefGoogle Scholar
  30. 24.
    Horvath, C, Sovak, M.: Biochim. Biophys. Acta. 298, 850, (1973).CrossRefGoogle Scholar
  31. 25.
    Wang, S. S., Vieth, W. R.: Biotechnol. Bioeng. 15, 93, (1973).CrossRefGoogle Scholar
  32. 26.
    Brown, G., Thomas, D., Domurado, D., Berjonneau, A., Guillon, G.: Biotechnol. Bioeng. 15, 359,(1973).CrossRefGoogle Scholar
  33. 27a.
    Chang, T. M. S.: Science 146, 524 (1964).CrossRefGoogle Scholar
  34. 27b.
    Chang, T. M. S.: “Artificial Cells”, C. C. Thomas Publ., Springfield III., (1972).Google Scholar
  35. 27c.
    Gregoriadis, G., Leathwood, P. D., Ryman, B. E.: FEBS Letters 14, 95, (1971).CrossRefGoogle Scholar
  36. 28.
    Dinish, K. N., Shivaram, K. N., Stegeman, H.: Z. Anal. Chem. 263, 27, (1973).CrossRefGoogle Scholar
  37. 29.
    Dinelli, D.: Process Biochemistry 7(8), 13, (1972).Google Scholar
  38. 30.
    Kobayashi, T., Laidler, K. J.: Biotechnol. Bioeng. 16, 77, (1974).CrossRefGoogle Scholar
  39. 31a.
    Smith, N. L., Amundson, N. R.: Ind. and Eng. Chem. 43, 2156, (1951).CrossRefGoogle Scholar
  40. 31b.
    Hamilton, B. K., Gardner, C. R., Colton, C. K.: A. E. Ch. E. J. 20, 503, (1974).CrossRefGoogle Scholar
  41. 32a.
    Goldman, R., Kedem, O., Katchalski, E.: Biochem. 7, 4518, (1968).CrossRefGoogle Scholar
  42. 32b.
    Sundaram, P. V., Tweedale, A., Laidler, K. J.: Can. J. Chem. 48, 1498, (1970).CrossRefGoogle Scholar
  43. 33.
    O'Driscoll, K. F., Hinberg, I., Korus, R., Kapoulas, A.: J. Polymer Sci. C46, 227 (1974).Google Scholar
  44. 34.
    Moo-Young, M., Kobayashi, T.: Can. J. Chem. Eng. 50, 162, (1972).CrossRefGoogle Scholar
  45. 35.
    Fink, D. J., Na., T. Y., Schultz, J. S.: Biotechnol Bioeng. 15, 879, (1973).CrossRefGoogle Scholar
  46. 36.
    Engasser, J. M., Horvath, C: J. Theor. Biol. 42, 137, (1973).CrossRefGoogle Scholar
  47. 37.
    O'Driscoll, K. F., Korus, R.: Can. J. Chem. Eng. 52, N 775 (1974).Google Scholar
  48. 38.
    Goldman, R., Goldstein, L., Katchalski, E.: “Biochemical Aspects of Reaction on Solid Supports”, G. R. Stark, Ed., Chap. 1, Acad. Press, N. Y. (1971).Google Scholar
  49. 39.
    Hinberg, I., Kapoulas, A., Korus, R., O'Driscoll, K.: Biotechnol. Bioeng. 16, 159, (1974).CrossRefGoogle Scholar
  50. 40.
    Ollis, D. F.: Biotechnol. Bioeng. 14, 871, (1972).CrossRefGoogle Scholar
  51. 41.
    Horvath, C, Engasser, J. M: Ind. Eng. Chem. Fundam. 12, 229, (1973).CrossRefGoogle Scholar
  52. 42.
    Regan, D. L., Dunnill, P., Lilly, M. D.: Biotechnol. Bioeng. 16, 333 (1974).CrossRefGoogle Scholar
  53. 43a.
    Brown, H. D., Patel, A. B., Chattopadhyay, S. K.: J. Chromatogr., 35, 103, (1968).CrossRefGoogle Scholar
  54. 43b.
    Broun, G., Thomas, D., Selegny, E.: J. Membrane Biol. 8, 313, (1972).CrossRefGoogle Scholar
  55. 44a.
    Mosbach, K., Mattiasson, B.: Acta Chem. Scand. 24, 2093, (1970).CrossRefGoogle Scholar
  56. 44b.
    Brown, H. D., Patel, A. B., Chattopadhyay, S. K.: J. Chromatogr. 35, 103, (1968).CrossRefGoogle Scholar
  57. 44c.
    Mattiason, B., Mosbach, K.: Biochim. Biophys. Acta 235, 253, (1971).Google Scholar
  58. 44d.
    Gestrelius, S., Mattiasson, B., Mosbach, K.: Biochim. Biophys. Acta 276, 339, (1972).Google Scholar
  59. 44e.
    Gestrelius, S., Mattiasson, B., Mosbach, K.: Euro. J. Biochem 36, 89, (1973).CrossRefGoogle Scholar
  60. 44f.
    Srere, P. A., Mattiasson, B., Mosbach, K.: Proc. Nat. Acad. Sci. U.S.A. 70, 2534, (1973).CrossRefGoogle Scholar
  61. 45.
    Lawrence, R. L., Okay, V.: Biotechn. Bioeng. 15, 217, (1973).CrossRefGoogle Scholar
  62. 46a.
    von der Ploeg, M., van Duijn, P.: J. Roy. Microscop. Soc. 83, 415, (1964).Google Scholar
  63. 46b.
    von Duijn, P., Pascoe, E., von der Ploeg, M.: J. Histochem. Cytochem. 15, 631, (1967).Google Scholar
  64. 47.
    Hicks, G. P., Updike, S. J.: Anal. Chem. 38, 762, (1966), “also U. S. Patent 3, 788, 950 (1974).”CrossRefGoogle Scholar
  65. 48.
    Gough, D. A., Amdrake, J. D.: Science 180, 380, (1973).CrossRefGoogle Scholar
  66. 49.
    Towshend, A.: Process Biochemistry, 8 (3), 23, (1973).Google Scholar
  67. 50.
    “Enzyme Therapy in Genetic Diseases”, D. Bergsma Ed., National Foundation — March of Dimes, White Plains, N. Y., (1973).Google Scholar
  68. 51.
    Chang, T. M. S.: Enzyme 14, 95, (1972/73).Google Scholar
  69. 52.
    Ohnuma, T., O'Driscoll, K., Korus, R., Wolczak, I.: J. Pharm. Exper. Therap. 195, 382 (1975).Google Scholar
  70. 53.
    Updike, S., Prieve, C, Magnuson, J.: Enzyme 14, 77, (1972/73).Google Scholar
  71. 54.
    Rubin, D. H.: “A Technology Assessment Methodology: Enzymes (Industrial)”, National Technical Information Service, Springfield, Va., (1971).Google Scholar

Copyright information

© Springer-Verlag 1976

Authors and Affiliations

  • F. O'Driscoll
    • 1
  1. 1.Dept. of Chemical EngineeringUniversity of WaterlooWaterlooCanada

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