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The Thermal Stability of the Fusarium solani pisi Cutinase as a Function of pH.

Petersen SB, Fojan P, Petersen EI, Petersen MT - J. Biomed. Biotechnol. (2001)

Bottom Line: The ratio between the calorimetric enthalpy (DeltaH(cal)) and the van't Hoff enthalpy (DeltaH(v)) obtained, is far from unity, indicating that cutinase does not exhibit a simple two state unfolding behaviour.The role of pH on the electrostatic contribution to the thermal stability was assessed using TITRA.We propose a molecular interpretation for the pH-variation in enzymatic activity.

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ABSTRACT
We have investigated the thermal stability of the Fusarium solani pisi cutinase as a function of pH, in the range from pH 2-12. Its highest enzymatic activity coincides with the pH-range at which it displays its highest thermal stability. The unfolding of the enzyme as a function of pH was investigated by microcalorimetry. The ratio between the calorimetric enthalpy (DeltaH(cal)) and the van't Hoff enthalpy (DeltaH(v)) obtained, is far from unity, indicating that cutinase does not exhibit a simple two state unfolding behaviour. The role of pH on the electrostatic contribution to the thermal stability was assessed using TITRA. We propose a molecular interpretation for the pH-variation in enzymatic activity.

No MeSH data available.


Peak halfwidth of cutinase over the observed pH range.
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Figure 4: Peak halfwidth of cutinase over the observed pH range.

Mentions: The influence of the scanrate on the apparent Tm at pH 4.0, 6.0, and 8.5 was also investigated (Figure 3). As is seen from Figure 3, the higher the scanrate, the higher the apparent Tm. However, the shift of Tm observed over the scanrates applied in the present study (10°C/h to 90°C/h) varied from 3°C at pH 8.5 to about 1°C at pH 6.0. When plotting the peak half width (T1/2) of the calorimetric transitions observed against pH (Figure 4) a minimum is displayed at around pH 6.0 where the least variation in scanrate dependence has been observed.


The Thermal Stability of the Fusarium solani pisi Cutinase as a Function of pH.

Petersen SB, Fojan P, Petersen EI, Petersen MT - J. Biomed. Biotechnol. (2001)

Peak halfwidth of cutinase over the observed pH range.
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC113781&req=5

Figure 4: Peak halfwidth of cutinase over the observed pH range.
Mentions: The influence of the scanrate on the apparent Tm at pH 4.0, 6.0, and 8.5 was also investigated (Figure 3). As is seen from Figure 3, the higher the scanrate, the higher the apparent Tm. However, the shift of Tm observed over the scanrates applied in the present study (10°C/h to 90°C/h) varied from 3°C at pH 8.5 to about 1°C at pH 6.0. When plotting the peak half width (T1/2) of the calorimetric transitions observed against pH (Figure 4) a minimum is displayed at around pH 6.0 where the least variation in scanrate dependence has been observed.

Bottom Line: The ratio between the calorimetric enthalpy (DeltaH(cal)) and the van't Hoff enthalpy (DeltaH(v)) obtained, is far from unity, indicating that cutinase does not exhibit a simple two state unfolding behaviour.The role of pH on the electrostatic contribution to the thermal stability was assessed using TITRA.We propose a molecular interpretation for the pH-variation in enzymatic activity.

View Article: PubMed Central - HTML - PubMed

ABSTRACT
We have investigated the thermal stability of the Fusarium solani pisi cutinase as a function of pH, in the range from pH 2-12. Its highest enzymatic activity coincides with the pH-range at which it displays its highest thermal stability. The unfolding of the enzyme as a function of pH was investigated by microcalorimetry. The ratio between the calorimetric enthalpy (DeltaH(cal)) and the van't Hoff enthalpy (DeltaH(v)) obtained, is far from unity, indicating that cutinase does not exhibit a simple two state unfolding behaviour. The role of pH on the electrostatic contribution to the thermal stability was assessed using TITRA. We propose a molecular interpretation for the pH-variation in enzymatic activity.

No MeSH data available.