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- W2435358328 abstract "The lipoprotein lipase from Pseudomonas fluorescens was modified with 2,4-bis(O-methoxypolyethylene glycol)-6-chloro-s-triazine. The modified lipase in which 55% of the amino groups in the enzyme molecule were coupled with polyethylene glycol was found to be soluble in benzene and catalyzed the reactions of ester synthesis, ester exchange, aminolysis and ester hydrolysis in benzene. The modified lipase had an extraordinary temperature-dependency: enzymic activity for methyl laurate synthesis from methyl alcohol and lauric acid increased with decreasing temperature and attained the maximum at the extremely low temperature of -3 degrees C. The optimum temperature for hydrolysis of methyl laurate was as low as -4 degrees C." @default.
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- W2435358328 date "1985-04-01" @default.
- W2435358328 modified "2023-09-23" @default.
- W2435358328 title "Ester synthesis at extraordinarily low temperature of -3 degrees C by modified lipase in benzene." @default.
- W2435358328 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/3927919" @default.
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