The Effect of Attachment of Hydrophobic Modifiers on the Catalytic Activities of Lipase and Trypsin

作者: K. Ampon , M. Basri , C.N.A. Razak , W.M.Z. Yunus , A.B. Salleh

DOI: 10.1016/B978-0-444-89046-7.50052-7

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摘要: Abstract Several hydrophobic groups of different sizes and steric hindrance have been covalently attached to lipase trypsin. Attachments polyethylene glycol chemical modification by reductive alkylation amidination with aldehydes imidoesters, respectively, increased the ester synthesis activities these enzymes 2–6 folds compared native unmodified enzymes. The maximal esterification alkylated appeared depend on particular aldehyde degree modification.For example, required a lower more bulky (eg. dodecyldehyde) attain its activity that which was modified acetaldehyde. Excessive modifications result in decrease activity. Trypsins were derivatized their aldehydes, very similar hydrophobicity. Most thus prepared active thermostable anhydrous organic solvents used, particularly dimethyformamide (DMF) pyridine. Modifications imidoesters gave results those obtained aldehydes.

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