Triglyceride hydrolysis and stability of a recombinant cutinase from Fusarium solani in AOT-iso-octane reversed micelles.
A recombinant cutinase from Fusarium solani was encapsulated in AOT reversed micelles. Physicochemical parameters of the system were optimized relative to triolein hydrolysis. Kinetic studies of triglyceride hydrolysis showed a decrease in specificity with increase of the acyl chain length. Stability of cutinase in the system under study is lower than in aqueous solution and decreases with increase in the water content in the system (W0 = [H2O]/[AOT]). The products of triolein hydrolysis had little effect on the cutinase stability. Although glycerol did not alter the stability, oleic acid decreases the enzyme stability. The increase in log P of solvent (from iso-octane to n-dodecane) decreased the stability. Deactivation profiles were fitted with the Henley and Sadana model (1).
Melo
E P
EP
Laboratório de Engenharia Bioquímica, Instituto Superior Técnico, Lisbon, Portugal.
Aires-Barros
M R
MR
Cabral
J M
JM
D002265:Carboxylic Ester Hydrolases / Q000737:chemistry*; D004143:Dioctyl Sulfosuccinic Acid; D004795:Enzyme Stability; D005670:Fusarium / Q000201:enzymology*; D006868:Hydrolysis; D007700:Kinetics; D008823:Micelles; D009795:Octanes; D011994:Recombinant Proteins / Q000737:chemistry; D014280:Triglycerides / Q000737:chemistry*
D008823:Micelles; D009795:Octanes; D011994:Recombinant Proteins; D014280:Triglycerides; D004143:Dioctyl Sulfosuccinic Acid; D002265:Carboxylic Ester Hydrolases; C019952:cutinase; C045798:2,2,4-trimethylpentane