Abstract
AbstractThe esterification reaction of a long‐chain fatty acid and a fatty alcohol with a surfactant‐modified lipase in a microaqueousn‐hexane system was studied. Various lipases from different sources were first modified with a surfactant of the sugar ester type to improve their dispersibility in apolar organic solvents. This enzyme modification technique converted inactive crude lipases to highly active biocatalysts for the esterification of long‐chain fatty acids and fatty alcohols in a microaqueous n‐hexane system. The hydrophilic‐lipophilic balance value and chainlength of the fatty acid residue of the fatty acid sugar ester, used for modifying the lipases, significantly influenced the amount of precipitated lipase that was dissolved in the aqueous solution, the protein content of the lipase‐surfactant complex and its esterification activity.
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