Ion Exchange Chromatography Lab Report

Abstract: Using Ion Exchange Chromatography, cellulase was purified. After purification, it was analyzed using a DNS test. The purified protein did not respond to the DNS the way it was expected to.
Introduction: Purifying proteins is an important part of biology because it can help identify the function of that protein. Once a protein’s function has been identified, it can be manipulated to see how the function would change if the protein was changed. A common way to purify a protein is through Ion Exchange Chromatography, which is where charged proteins will bind to the beads in the column to purify it from the solution (Berg JM, 2002). The purpose of this experiment is to use Ion Exchange Chromatography to purify cellulase.
Materials and Methods: An ion exchange chromatography column was obtained and set up for purification with the addition of 0.5 ml ion exchange matrix. 1 ml

Ideally the purified cellulase that was in test tube 4, which was 50 mg/ml, should have had a higher absorbance, but for unknown reasons, the cellulase has not been working all semester long. Test tube 2 had cellulase at a 1 mg/ml concentration. Next time, instead of a 1-hour incubation period at 50°C, there should be a 3-hour incubation period at 55°C. This would give the cellulase more time to break down the filter paper at a higher temperature.
Works Cited
Berg JM, T. J. (2002, January 1). Biochemistry. 5th edition. Retrieved from NCBI: