Advertisement

Chemistry of Natural Compounds

, Volume 22, Issue 5, pp 587–592 | Cite as

Immobilization of urease on modified styrene/polyvinylbenzene matrices

  • T. I. Davidenko
  • S. A. Koshelev
  • S. B. Makarova
Article
  • 22 Downloads

Abstract

With copolymers of styrene and divinylbenzene containing various modification groups and the use of glutaric dialdehyde for their activation, immobilized forms of urease for watermelon seeds and fromStaphylococcus saprophyticus have been obtained. The properties of the immobilized preparations have been studied: the pH optimum, the temperature optimum and thermal stability, the influence of stabilizing components, kinetic features of the hydrolysis of urea, and work under column and batch conditions. The high stability of the immobilized preparations has been shown.

Keywords

Immobilize Enzyme Urease Activity Divinylbenzene Immobilize Form Immobilize Preparation 

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

Literature cited

  1. 1.
    Yu. A. Leikin, T. A. Cherkasova, M. M. Yanina, V. Bogdanov, et al., in: Abstracts of Lectures at the Ist All-Union Conference on Soprtion Methods of Detoxification and Immunocorrection in Medicine [in Russian], Khar'kov (1982), p. 302.Google Scholar
  2. 2.
    T. A. Cherkasova, V. I. Bogdanov, A. Kh. Zitsmanis, et al., in: Abstracts of Lectures at the IVth All-Union Symposium on Engineering Enzymology [in Russian], Moscow, Vol. II (1983), p. 72.Google Scholar
  3. 3.
    T. I. Davidenko, E. V. Sevast'yanova, S. A. Koshelev, et al., in: Abstracts of Lectures at the VIth All-Union Symposium on Engineering Enzymology [in Russian], Moscow, Vol. II (1983), p. 32.Google Scholar
  4. 4.
    V. P. Torchilin, Zh. M. Litvak, T. N. Esina, et al., Bioorg. Khim.,1, 1231 (1975).Google Scholar
  5. 5.
    I. V. Berezin, N. F. Kazanskaya, and O. A. Kost, Bioorg. Khim.,1, 1337 (1975).Google Scholar
  6. 6.
    T. D. Khokhlova, M. M. Yanina, S. I. Dikhtyarev, and Yu. S. Nikitin, Prikl. Biokhim. Mikrobiol.,19, 378 (1983).PubMedGoogle Scholar
  7. 7.
    Z. Michaelis and M. Z. Menten, Biochem. Z.,49, 333 (1913).Google Scholar
  8. 8.
    G. V. Lyubinskii, V. V. Yanishpol'skii, V. A. Tertykh, and D. Yu. Yuodbal'kite, Ukr. Biokhim. Zh.,56, 24 (1984).Google Scholar
  9. 9.
    G. V. Lyubinskii, V. V. Yanishpol'skii, V. A. Tertykh, D. Yu. Yuodval'kite, and A. A. Glemzha, Ukr. Biokhim. Zh.,54, 145 (1982).Google Scholar
  10. 10.
    A. Cornish-Bowden, Principles of Enzyme Kinetics, Butterworths, London (1976) [Russian translation, Moscow (1979), p. 48].Google Scholar
  11. 11.
    O. H. Lowry, N. V. Rosebrough, A. A. Farr, and R. J. Randall, J. Biol. Chem.,193, 265 (1951).Google Scholar
  12. 12.
    R. L. Blekley, E. C. Webb, and B. Zerner, Biochemistry,8, 1984 (1969).CrossRefGoogle Scholar
  13. 13.
    G. B. Kristiakowsky, P. C. Mangelsdorf, and A. J. Rosenberg, J. Am. Chem. Soc.,74, 5015 (1952).CrossRefGoogle Scholar

Copyright information

© Plenum Publishing Corporation 1987

Authors and Affiliations

  • T. I. Davidenko
  • S. A. Koshelev
  • S. B. Makarova

There are no affiliations available

Personalised recommendations