DSC studies of Fusarium solani pisi cutinase: consequences for stability in the presence of surfactants.
The application of cutinase from Fusarium solani pisi as a fat-stain removing ingredient in laundry washing is hampered by its lack of stability in the presence of anionic surfactants. We postulate that the stability of cutinase towards anionics can be improved by mutations increasing its temperature stability. Thermal unfolding as measured with DSC, appears to be irreversible, though the thermograms are more symmetric than predicted by a simple irreversible model. In the presence of taurodeoxycholate (TDOC), the unfolding temperature is lower and the unfolding is reversible. We conclude that an early reversible unfolding intermediate exists in which a number of additional hydrophobic patches are exposed to the solvent, or preferentially are covered with TDOC. Improvement of the stability of cutinase with respect to both surfactants and thermal denaturation, should thus be directed toward the prevention of exposure of hydrophobic patches in the early intermediate.
Creveld
L D
LD
Unilever Research, Olivier van Noortlaan 120, 3133 AT Vlaardingen, The Netherlands.
Meijberg
W
W
Berendsen
H J
HJ
Pepermans
H A
HA
D000465:Algorithms; D002152:Calorimetry, Differential Scanning; D002265:Carboxylic Ester Hydrolases / Q000737:chemistry*; D005670:Fusarium / Q000201:enzymology*; D008956:Models, Chemical; D017510:Protein Folding; D011994:Recombinant Proteins / Q000737:chemistry; D012967:Sodium Dodecyl Sulfate; D013501:Surface-Active Agents / Q000737:chemistry*; D013657:Taurodeoxycholic Acid; D013696:Temperature
D011994:Recombinant Proteins; D013501:Surface-Active Agents; D012967:Sodium Dodecyl Sulfate; D013657:Taurodeoxycholic Acid; D002265:Carboxylic Ester Hydrolases; C019952:cutinase