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• W2042103404 endingPage "2015" @default.
• W2042103404 startingPage "2008" @default.
• W2042103404 abstract "Cutinase from Fusarium solani pisi was encapsulated in sol−gel matrixes prepared using combinations of tetramethoxysilane and monoalkyl-methoxysilane precursors with different chain lengths (from methyltrimethoxysilane to n-octyltrimethoxysilane), in molar proportion of 1 to 5. The specific activity of the encapsulated cutinase in a model transesterification reaction in n-hexane has been correlated with the structure of the organically modified silica (ORMOSIL) support. The matrixes were characterized by diffuse reflectance infrared Fourier transform (DRIFT) spectroscopy and by solid-state 29Si and 1H nuclear magnetic resonance (NMR). The enhancement of the bioactivity with increasing alkyl chain lengths up to C4 was correlated with the nature of the ORMOSIL surface groups, namely, with a decrease in the hydrophilic−lipophilic balance (HLB) of the matrix. Such trend suggests that the kinetics of the catalyzed transesterification in n-hexane is a diffusion-controlled process. For coprecursors with longer alkyl chains (C6 and C8), the activity of encapsulated cutinase suddenly falls, despite the continuous decrease in the matrix HLB. For the ORMOSIL with n-hexyltrimethoxysilane, in particular, the enzyme activity is zero, due to the alkyl chain acting as a pore blocker. This effect is more moderate for n-octyltrimethoxysilane, because the alkyl chain has a higher mobility within the inorganic matrix." @default.
• W2042103404 created "2016-06-24" @default.
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• W2042103404 date "2008-01-19" @default.
• W2042103404 modified "2023-09-23" @default.
• W2042103404 title "Enhanced Biocatalytic Activity of ORMOSIL-Encapsulated Cutinase: The Matrix Structural Perspective" @default.
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• W2042103404 doi "https://doi.org/10.1021/jp0761867" @default.
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