Latest News on Immobilization : May 2020

Latest News on Immobilization : May 2020

Immobilization of Enzymes and Cells
The technology for immobilization of cells and enzymes evolved steadily for the first 25 years of its existence (1), but in recent years it has reached a plateau, if not a slight decline. However, the expansion of biotechnology, and the expected developments that will accrue from advances in genetic technology, has revitalized enthusiasm for immobilization of enzymes and cells (2). Research and development work has provided a bewildering array of support materials and methods for immobilization. [1]

Review: Hydrogels for cell immobilization

Hydrogels are being investigated for mammalian cell immobilization. Their material properties can be engineered for biocompatibility, selective permeability, mechanical and chemical stability, and other requirements as specified by the application including uniform cell distribution and a given membrane thickness or mechanical strength. These aqueous gels are attractive for analytical and tissue engineering applications and can be used with immobilization in therapies for various diseases as well as to generate bioartificial organs. Recent advances have broadened the use of hydrogel cell immobilization in biomedical fields. To provide an overview of available technology, this review surveys the current developments in immobilization of mammalian cells in hydrogels. Discussions cover hydrogel requirements for use in adhesion, matrix entrapment, and microencapsulation, the respective processing methods, as well as current applications. © 1996 John Wiley & Sons, Inc. [2]

Nitrogen Mineralization, Immobilization, and Nitrification

This chapter outlines the methodologies and the concepts used to assess soil internal nitrogen(N)‐cycle processes. It discusses laboratory and field methods for determining gross and net N‐transformation rates. Three 15N techniques have been used to study gross N‐ transformation processes: 15N natural abundance techniques, where slight differences in isotopic enrichment of soil pools, resulting from biological discrimination, are observed over time; 15N tracer techniques, where a substrate pool is labeled and movement of the isotope through the system is monitored over time; and 15N isotope‐dilution techniques, where a product pool is labeled and the rate at which production alters the isotopic enrichment of the pool is monitored. Tracer techniques have been widely used to determine directions of mass flow and connections among ecosystem compartments, but they have also been used to measure gross rates of flows. [3]

Studies on Immobilization of Cutinases from Thermobifida fusca on Glutaraldehyde Activated Chitosan Beads

Studies on Immobilization of Cutinases from Thermobifida fusca on Glutaraldehyde Activated Chitosan Beads

Aims: To evaluate and optimize the activity and stability performance of two recombinant cutinases of Thermobifida fusca, Cut1 and Cut2 on glutaraldehyde activated chitosan beads.

Place and Duration of Study: Biochemical Engineering Laboratory, Department of Biotechnology, Indian Institute of Technology Guwahati, Assam India. Experiment conducted as a partial fulfillment to PhD degree from December, 2010 to January, 2014. [4]

Characteristics of Penicillin G Acylase Immobilized onto Iron Oxide Nanoparticles

Penicillin G acylase was immobilized onto iron oxide nanoparticles coated with polyethyleneimine and then cross linked with glutaraldehyde solution. The FTIR spectrum of immobilized enzyme showed peak at 1648cm-1 which can be attributed to the C=N bonds of Schiff’s base linkage formed between glutaraldehyde and amino group of penicillin G acylase. By considering the FTIR spectrum of nano particle coated with polyethyleneimine, adsorption of penicillin G acylase has taken place and then glutaraldehyde cross linked enzyme onto activated support. Catalytic properties of nano penicillin G acylase were improved upon immobilization as compared to its free counterpart. The optimal pH and temperature were determined to be 7.0, 10.0, 50 and 75ºC for free and immobilized penicillin G acylase, respectively. Thermal stabilities of both nano and free penicillin G acylase were studied .The Km value of immobilized nanozyme was calculated from Lineweaver Burck plot to be 0.23 μM while that of free penicillin G acylase was 0.28μM. In this way nano penicillin G acylase with improved catalytic properties was developed as compared to its soluble counterpart. [5]

Reference :
[1] Bickerstaff, G.F., 1997. Immobilization of enzymes and cells. In Immobilization of enzymes and cells (pp. 1-11). Humana press.

[2] Jen, A.C., Wake, M.C. and Mikos, A.G., 1996. Hydrogels for cell immobilization. Biotechnology and bioengineering, 50(4), pp.357-364.

[3] Hart, S.C., Stark, J.M., Davidson, E.A. and Firestone, M.K., 1994. Nitrogen mineralization, immobilization, and nitrification. Methods of Soil Analysis: Part 2 Microbiological and Biochemical Properties, 5, pp.985-1018.

[4] Hegde, K. and Dasu Veeranki, V. (2014) “Studies on Immobilization of Cutinases from Thermobifida fusca on Glutaraldehyde Activated Chitosan Beads”, Biotechnology Journal International, 4(10), pp. 1049-1063. doi: 10.9734/BBJ/2014/12558.

[5] Seyed Bahman, M., Seyed Mohammad, A., Akbarzadeh, A., Mona, S., Hatami Gigloo, S., Ali, F. and Dariush, N. (2013) “Characteristics of Penicillin G Acylase Immobilized onto Iron Oxide Nanoparticles”, Biotechnology Journal International, 3(3), pp. 367-376. doi: 10.9734/BBJ/2013/2987.

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