The Experts below are selected from a list of 24201 Experts worldwide ranked by ideXlab platform
Jose M Guisan - One of the best experts on this subject based on the ideXlab platform.
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high stabilization of immobilized rhizomucor miehei lipase by additional coating with hydrophilic crosslinked polymers poly allylamine aldehyde dextran
Process Biochemistry, 2020Co-Authors: Janaina Cejudosanches, Gloria Fernandezlorente, Alejandro H Orrego, Adriana Jaimemendoza, Rohollah Ghobadi, Sonia Morenoperez, Javier Rochamartin, Jose M GuisanAbstract:Abstract Immobilized enzymes have a very large surface region which is not in contact with the support surface and, thus, have potential as a target for novel stabilization strategies. In this paper, coating the surfaces of such enzymes with a highly hydrophilic and compact cross-linked poly-aminated polymer as a strategy to increase the thermal stability of the immobilized enzymes is proposed. In particular, Rhizomucor miehei lipase (RML) was immobilized by interfacial adsorption onto octyl-agarose and further coated with poly-allylamine (PAA), a polymer that is very rich in primary amino groups. Cross-linking of the PAA layer to coat the immobilized enzyme was carried out, in situ, by reaction with freshly oxidized dextran (aldehyde–dextran). The PAA layer only exerted moderate stabilizing effects (around 4-fold), but further cross-linking with aldehyde–dextran highly increased the stabilizing effects; the new derivative was 440-fold more stable than uncoated derivative at 55 °C and pH 7 and exhibited 6-fold more catalytic activity compared to the soluble enzyme used for immobilization. We hypothesize that the hydrophilicity of PAA Reduces the exposure of internal hydrophobic pockets to the enzyme surface at high temperatures. Besides, the compactness of the polymer may Reduce Distortion of the enzyme surface during inactivation.
Adriana Jaimemendoza - One of the best experts on this subject based on the ideXlab platform.
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high stabilization of immobilized rhizomucor miehei lipase by additional coating with hydrophilic crosslinked polymers poly allylamine aldehyde dextran
Process Biochemistry, 2020Co-Authors: Janaina Cejudosanches, Gloria Fernandezlorente, Alejandro H Orrego, Adriana Jaimemendoza, Rohollah Ghobadi, Sonia Morenoperez, Javier Rochamartin, Jose M GuisanAbstract:Abstract Immobilized enzymes have a very large surface region which is not in contact with the support surface and, thus, have potential as a target for novel stabilization strategies. In this paper, coating the surfaces of such enzymes with a highly hydrophilic and compact cross-linked poly-aminated polymer as a strategy to increase the thermal stability of the immobilized enzymes is proposed. In particular, Rhizomucor miehei lipase (RML) was immobilized by interfacial adsorption onto octyl-agarose and further coated with poly-allylamine (PAA), a polymer that is very rich in primary amino groups. Cross-linking of the PAA layer to coat the immobilized enzyme was carried out, in situ, by reaction with freshly oxidized dextran (aldehyde–dextran). The PAA layer only exerted moderate stabilizing effects (around 4-fold), but further cross-linking with aldehyde–dextran highly increased the stabilizing effects; the new derivative was 440-fold more stable than uncoated derivative at 55 °C and pH 7 and exhibited 6-fold more catalytic activity compared to the soluble enzyme used for immobilization. We hypothesize that the hydrophilicity of PAA Reduces the exposure of internal hydrophobic pockets to the enzyme surface at high temperatures. Besides, the compactness of the polymer may Reduce Distortion of the enzyme surface during inactivation.
Rohollah Ghobadi - One of the best experts on this subject based on the ideXlab platform.
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high stabilization of immobilized rhizomucor miehei lipase by additional coating with hydrophilic crosslinked polymers poly allylamine aldehyde dextran
Process Biochemistry, 2020Co-Authors: Janaina Cejudosanches, Gloria Fernandezlorente, Alejandro H Orrego, Adriana Jaimemendoza, Rohollah Ghobadi, Sonia Morenoperez, Javier Rochamartin, Jose M GuisanAbstract:Abstract Immobilized enzymes have a very large surface region which is not in contact with the support surface and, thus, have potential as a target for novel stabilization strategies. In this paper, coating the surfaces of such enzymes with a highly hydrophilic and compact cross-linked poly-aminated polymer as a strategy to increase the thermal stability of the immobilized enzymes is proposed. In particular, Rhizomucor miehei lipase (RML) was immobilized by interfacial adsorption onto octyl-agarose and further coated with poly-allylamine (PAA), a polymer that is very rich in primary amino groups. Cross-linking of the PAA layer to coat the immobilized enzyme was carried out, in situ, by reaction with freshly oxidized dextran (aldehyde–dextran). The PAA layer only exerted moderate stabilizing effects (around 4-fold), but further cross-linking with aldehyde–dextran highly increased the stabilizing effects; the new derivative was 440-fold more stable than uncoated derivative at 55 °C and pH 7 and exhibited 6-fold more catalytic activity compared to the soluble enzyme used for immobilization. We hypothesize that the hydrophilicity of PAA Reduces the exposure of internal hydrophobic pockets to the enzyme surface at high temperatures. Besides, the compactness of the polymer may Reduce Distortion of the enzyme surface during inactivation.
Janaina Cejudosanches - One of the best experts on this subject based on the ideXlab platform.
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high stabilization of immobilized rhizomucor miehei lipase by additional coating with hydrophilic crosslinked polymers poly allylamine aldehyde dextran
Process Biochemistry, 2020Co-Authors: Janaina Cejudosanches, Gloria Fernandezlorente, Alejandro H Orrego, Adriana Jaimemendoza, Rohollah Ghobadi, Sonia Morenoperez, Javier Rochamartin, Jose M GuisanAbstract:Abstract Immobilized enzymes have a very large surface region which is not in contact with the support surface and, thus, have potential as a target for novel stabilization strategies. In this paper, coating the surfaces of such enzymes with a highly hydrophilic and compact cross-linked poly-aminated polymer as a strategy to increase the thermal stability of the immobilized enzymes is proposed. In particular, Rhizomucor miehei lipase (RML) was immobilized by interfacial adsorption onto octyl-agarose and further coated with poly-allylamine (PAA), a polymer that is very rich in primary amino groups. Cross-linking of the PAA layer to coat the immobilized enzyme was carried out, in situ, by reaction with freshly oxidized dextran (aldehyde–dextran). The PAA layer only exerted moderate stabilizing effects (around 4-fold), but further cross-linking with aldehyde–dextran highly increased the stabilizing effects; the new derivative was 440-fold more stable than uncoated derivative at 55 °C and pH 7 and exhibited 6-fold more catalytic activity compared to the soluble enzyme used for immobilization. We hypothesize that the hydrophilicity of PAA Reduces the exposure of internal hydrophobic pockets to the enzyme surface at high temperatures. Besides, the compactness of the polymer may Reduce Distortion of the enzyme surface during inactivation.
Gloria Fernandezlorente - One of the best experts on this subject based on the ideXlab platform.
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high stabilization of immobilized rhizomucor miehei lipase by additional coating with hydrophilic crosslinked polymers poly allylamine aldehyde dextran
Process Biochemistry, 2020Co-Authors: Janaina Cejudosanches, Gloria Fernandezlorente, Alejandro H Orrego, Adriana Jaimemendoza, Rohollah Ghobadi, Sonia Morenoperez, Javier Rochamartin, Jose M GuisanAbstract:Abstract Immobilized enzymes have a very large surface region which is not in contact with the support surface and, thus, have potential as a target for novel stabilization strategies. In this paper, coating the surfaces of such enzymes with a highly hydrophilic and compact cross-linked poly-aminated polymer as a strategy to increase the thermal stability of the immobilized enzymes is proposed. In particular, Rhizomucor miehei lipase (RML) was immobilized by interfacial adsorption onto octyl-agarose and further coated with poly-allylamine (PAA), a polymer that is very rich in primary amino groups. Cross-linking of the PAA layer to coat the immobilized enzyme was carried out, in situ, by reaction with freshly oxidized dextran (aldehyde–dextran). The PAA layer only exerted moderate stabilizing effects (around 4-fold), but further cross-linking with aldehyde–dextran highly increased the stabilizing effects; the new derivative was 440-fold more stable than uncoated derivative at 55 °C and pH 7 and exhibited 6-fold more catalytic activity compared to the soluble enzyme used for immobilization. We hypothesize that the hydrophilicity of PAA Reduces the exposure of internal hydrophobic pockets to the enzyme surface at high temperatures. Besides, the compactness of the polymer may Reduce Distortion of the enzyme surface during inactivation.