Ester-exchange catalyzed by lipase modified with polyethylene glycol.
K Takahashi, Y Kodera, T Yoshimoto, A Ajima, A Matsushima, Y Inada
Index: Biochem. Biophys. Res. Commun. 131(2) , 532-6, (1985)
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Abstract
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.
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