Thermal denaturation of pepsin at acidic media: Using DSC, MALDI-TOF MS and PAGE techniques
2013
Abstract The thermal stability of pepsin in a strong acid medium as a function of pH has been investigated using differential scanning calorimetry (DSC), UV absorbance, polyacrylamide gel electrophoresis (PAGE) and MALDI-TOF MS methods. The “two independent two-state transitions model” with view of physiological function of pepsin was used for analyzing thermal denaturation curves. The transition temperature ( T m ) values ranging from 305.15 to 319.15 K for the first transition and from 322.15 to 349.15 K for the second transition in the examined pH range implicating the higher stability at pH 4 are in good agreement with MALDI-TOF MS results. The corresponding maximum, Δ G °(25), was stability obtained at pH 4 with values of 65.3 kJ mol −1 .
Keywords:
- Matrix-assisted laser desorption/ionization
- Differential scanning calorimetry
- Polyacrylamide gel electrophoresis
- Denaturation (biochemistry)
- Ranging
- Thermal stability
- Pepsin
- Chemistry
- Absorbance
- Chromatography
- Analytical chemistry
- thermal denaturation
- Fourier transform infrared spectroscopy
- Transition temperature
- Correction
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- Cite
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