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The rates of an enzyme catalyzed reaction generally changes with change in enzyme concentration, substrate concentration, temperature, pH, time, and presence of enzyme inhibitors. For this particular experiment, the determination of enzyme activity, Trypsin, was obtained by changing the concentration of its substrate concentration (1). For these purposes, the Michaelis-Menten equation was used in combination with a double-reciprocal or Lineweaver-Burke plot to plot obtained data and the enzymatic activity of Trypsin was measured through the colormetric Lowry's assay and spectrophotometer absorbance readings...
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Common topics in this essay:
- J Curve
- Stephanie Maria Graph
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- Bell Curve
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