Ester-exchange catalyzed by lipase modified with polyethylene glycol.
Lipoprotein lipase was modified with 2,4-bis(O-methoxypolyethylene glycol)-6-chloro-s-triazine; forty-six percent out of seven amino groups in the molecule were substituted. The modified lipase catalyzed ester-exchange reactions between an ester and an alcohol, between an ester and an acid, and between two esters. The modified enzyme catalyzed these reactions not only in organic solvents, but also in straight hydrophobic substrates. As the modified enzyme was extremely stable at elevated temperature, for example at 70 degrees C, this can find many practical applications.
D002208:Caproates / Q000378:metabolism; D002264:Carboxylic Acids / Q000378:metabolism*; D007851:Dodecanol / Q000378:metabolism; D004355:Drug Stability; D004952:Esters / Q000378:metabolism*; D006358:Hot Temperature; D007848:Laurates / Q000378:metabolism; D019787:Linoleic Acid; D008041:Linoleic Acids / Q000378:metabolism; D008071:Lipoprotein Lipase / Q000378:metabolism*; D011092:Polyethylene Glycols; D013329:Structure-Activity Relationship; D013379:Substrate Specificity
D002208:Caproates; D002264:Carboxylic Acids; D004952:Esters; D007848:Laurates; D008041:Linoleic Acids; D007851:Dodecanol; D011092:Polyethylene Glycols; C046397:amyl laurate; C029761:2,4-bis(O-methoxypolyethylene glycol)-6-chloro-s-triazine; D019787:Linoleic Acid; C046398:butyl caprylate; D008071:Lipoprotein Lipase