Isolation and Purification of Lysozyme Research Paper by miroslav

Isolation and Purification of Lysozyme
This paper looks at an experiment in an enzyme purification lab for the purification of lysozyme.
# 103271 | 2,117 words | 5 sources | APA | 2007 | CA
Published on May 01, 2008 in Biology (Molecular and Cell) , Chemistry (Biochemistry)


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Description:

The writer explains that in this experiment, lysozyme was purified from egg white solution into 24 fractions using gel column chromatography. The writer points out that the odd-numbered fractions were then assayed in order to determine the enzymatic activity of lysozyme, while the even-numbered fractions were assayed for total protein content, using the Bradford protein assay procedure. The writer notes that lysozyme is one of the most well-known enzymes, being abundant in mucus, tears, and albumen (commonly known as egg white).
The writer concludes that the purification of lysozyme from egg white was only somewhat successful since the estimated value of the molecular weight, 14.25 kDa, is practically the same as the known weight of 14.3 kDa. However, the specific activity, calculated at 400 units/mg, was significantly less than the expected specific activity of 25 000 units/mg of protein.

Outline:
Abstract
Introduction
Materials and Methods
Results
Calculations
Discussion
Conclusion

From the Paper:

"Lysozyme is itself composed of 129 amino acids, including four disulfide bridges and three sets of alpha helices. The enzyme's active site consists of a long groove that can hold as many as six polysaccharides. According to past experiments, specific activity of lysozyme from egg white is approximately 25 000 units/mg. This is the expected result for this experiment. However, one factor that influences the specific activity is the actual column and type of chromatography being used, since accuracy differs among the different types of chromatographies. Therefore, some are able to purify enzymes better than others, giving a more accurate specific activity. In addition to obtaining the specific activity, molecular weight of the enzyme can be determined by comparing the fraction in which most of the enzyme eluted with the fractionation range."

Sample of Sources Used:

  • Alderton, Gordon, Ward, W.H., and Fevold, H.L. (1944) Isolation of Lysozyme from Egg White. The Journal of Biological Chemistry 44(1): 43-58.
  • Altintas, E.B., Denizli, A. (2006) Monosize poly(glycidyl methacrylate) beads for dye-affinity purification of lysozyme. International Journal of Biological Macromolecules. 38(2): 99-106.
  • Cell Biology and Biochemistry I Laboratory Manual. SC/BIOL 2020 4.0. Toronto: York University. Department of Biology, Fall 2007.
  • "Egg Proteins". Online Art. Encyclopaedia Britannica Online. 21 Nov 2007 < http://www.britannica.com/eb/article-72561 >
  • Odabasi, M., Say, R., Denizli, A. (2007) Molecular imprinted particles for lysozyme purification. Materials Science & Engineering C-Biomimetic and Supramolecular Systems. 27(1): 90-99.

Cite this Research Paper:

APA Format

Isolation and Purification of Lysozyme (2008, May 01) Retrieved February 25, 2021, from https://www.academon.com/research-paper/isolation-and-purification-of-lysozyme-103271/

MLA Format

"Isolation and Purification of Lysozyme" 01 May 2008. Web. 25 February. 2021. <https://www.academon.com/research-paper/isolation-and-purification-of-lysozyme-103271/>

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