Encyclopedia of Membranes

2016 Edition
| Editors: Enrico Drioli, Lidietta Giorno

Urease Immobilization on Membranes

Reference work entry
DOI: https://doi.org/10.1007/978-3-662-44324-8_1241

Enzyme immobilization within membrane pores or onto membrane surface has gained growing interest due to controllable transport of reaction substrates and products through the membrane. This is particularly important when the product acts as an inhibitor. Also, high surface area of the membranes offers a potentially higher enzyme loading. Urease is an enzyme most extensively studied for immobilization and catalyzes the hydrolysis of urea to ammonium and carbon dioxide. Nonenzymatic urea hydrolysis requires high temperatures and pressures and biological conversion of urea nitrogen to dinitrogen suffers from instabilities of microbial bed. The method based on the hydrolysis of urea by urease immobilized on a suitable support material is an attractive and an alternative removal method.

The choice of a support material for enzyme immobilization is important to minimize the loss of enzyme activity. The membrane material should have high affinity to proteins, available reactive functional...

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References

  1. Guedidi S, Yurekli Y, Deratani A, Dejardin P, Innocent C, Altinkaya SA, Roudesli S, Yemenicioglu A (2010) Effect of enzyme location on activity and stability of trypsin and urease immobilized on porous membranes by using layer-by-layer self-assembly of polyelectrolyte. J Membr Sci 365:59CrossRefGoogle Scholar
  2. Krajewska B (2009) Properties and their customizing by enzyme immobilizations: a review. J Mol Catal B Enzym 59:22CrossRefGoogle Scholar
  3. Smuleac V, Butterfield DA, Bhattacharyya D (2006) Layer-by-layer-assembled microfiltration membranes for biomolecule immobilization and enzymatic catalysis. Langmuir 22:10118CrossRefGoogle Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 2016

Authors and Affiliations

  1. 1.Department of Chemical EngineeringIzmir Institute of TechnologyUrlaTurkey