Immobilized enzyme

Enzymes immobilised in beads of alginate gel

An immobilized enzyme is an enzyme that is attached to an inert, insoluble material such as calcium alginate (produced by reacting a mixture of sodium alginate solution and enzyme solution with calcium chloride). This can provide increased resistance to changes in conditions such as pH or temperature. It also allows enzymes to be held in place throughout the reaction, following which they are easily separated from the products and may be used again - a far more efficient process and so is widely used in industry for enzyme catalysed reactions. An alternative to enzyme immobilization is whole cell immobilization.[1][2]

Commercial use

Immobilized enzymes are very important for commercial uses as they possess many benefits to the expenses and processes of the reaction of which include:

In the past, biological washing powders and detergents would contain many proteases and lipases which would break down dirt. However, when the cleaning products would come into contact with the skin, it would create allergic reactions. This is why immobilization of enzymes are important, not just economically.

Immobilization of an Enzyme

There are various ways by which one can immobilize an enzyme:

Immobilization of a Substrate for Enzymatic Reactions

Another widely used application of the immobilization approach together with enzymes has been the enzymatic reactions on immobilized substrates. This approach facilitates the analysis of enzyme activities and mimics the performance of enzymes on e.g. cell walls.[6]

References

  1. Zaushitsyna, O.; Berillo, D.; Kirsebom, H.; Mattiasson, B. (2013). "Cryostructured and Crosslinked Viable Cells Forming Monoliths Suitable for Bioreactor Applications". Topics in Catalysis 57 (5): 339. doi:10.1007/s11244-013-0189-9.
  2. Aragão Börner, R.; Zaushitsyna, O.; Berillo, D.; Scaccia, N.; Mattiasson, B.; Kirsebom, H. (2014). "Immobilization of Clostridium acetobutylicum DSM 792 as macroporous aggregates through cryogelation for butanol production". Process Biochemistry 49: 10. doi:10.1016/j.procbio.2013.09.027.
  3. Wu, Hong; Liang, Yanpeng; Shi, Jiafu; Wang, Xiaoli; Yang, Dong; Jiang, Zhongyi (April 2013). "Enhanced stability of catalase covalently immobilized on functionalized titania submicrospheres". Materials Science and Engineering: C 33 (3): 1438–1445. doi:10.1016/j.msec.2012.12.048.
  4. Engelmark Cassimjee, K.; Kadow, M.; Wikmark, Y.; Svedendahl Humble, M.; Rothstein, M. L.; Rothstein, D. M.; Bäckvall, J. -E. (2014). "A general protein purification and immobilization method on controlled porosity glass: Biocatalytic applications". Chemical Communications 50 (65): 9134. doi:10.1039/C4CC02605E.
  5. Zucca, Paolo; Sanjust, Enrico (9 September 2014). "Inorganic Materials as Supports for Covalent Enzyme Immobilization: Methods and Mechanisms". Molecules 19 (9): 14139–14194. doi:10.3390/molecules190914139.
  6. Gray, C. J.; Weissenborn, M. J.; Eyers, C. E.; Flitsch, S. L. (2013). "Enzymatic reactions on immobilised substrates". Chemical Society Reviews 42 (15): 6378. doi:10.1039/C3CS60018A. PMID 23579870.
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