Development and Characterization of a Silica Monolith Immobilized Enzyme Micro-bioreactor
Several 10-cm-long capillary tubes [made of poly(ether ether ketone) (PEEK)] with inside diameters of 0.1−2.0 mm were filled with silica monolith-immobilized protease derived by in situ sol−gel transition from a 1:4 mixture of tetramethoxysilane and methyltrimethoxysilane. Transesterification betwee...
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Veröffentlicht in: | Industrial & engineering chemistry research 2005-01, Vol.44 (1), p.236-240 |
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creator | Kawakami, Koei Sera, Yoshihide Sakai, Shinji Ono, Tsutomu Ijima, Hiroyuki |
description | Several 10-cm-long capillary tubes [made of poly(ether ether ketone) (PEEK)] with inside diameters of 0.1−2.0 mm were filled with silica monolith-immobilized protease derived by in situ sol−gel transition from a 1:4 mixture of tetramethoxysilane and methyltrimethoxysilane. Transesterification between 20 mM (S)-(−)-glycidol and 0.4 M vinyl n-butyrate in an organic solvent was used as the test reaction. The substrate solution flowed through the column at a flow rate of 0.0004−5.0 mL·min-1. The conversion in the micro-bioreactor was higher than that in the batch reactor at a high liquid flow rate. When three tubes were connected in series, the conversion at a fixed ratio of the mass of the enzyme to the liquid flow rate was increased by approximately 50%, because of the tripling of the flow rate as compared to the case with a single tube. Changes in the tube diameter had no influence on the conversion at a fixed superficial liquid velocity. Further, the conversion increased with a decrease in the enzyme content. These results were ascribed to the apparent effect of liquid−solid mass transfer and were analyzed quantitatively using a simple mathematical model. |
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Transesterification between 20 mM (S)-(−)-glycidol and 0.4 M vinyl n-butyrate in an organic solvent was used as the test reaction. The substrate solution flowed through the column at a flow rate of 0.0004−5.0 mL·min-1. The conversion in the micro-bioreactor was higher than that in the batch reactor at a high liquid flow rate. When three tubes were connected in series, the conversion at a fixed ratio of the mass of the enzyme to the liquid flow rate was increased by approximately 50%, because of the tripling of the flow rate as compared to the case with a single tube. Changes in the tube diameter had no influence on the conversion at a fixed superficial liquid velocity. Further, the conversion increased with a decrease in the enzyme content. 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Eng. Chem. Res</addtitle><date>2005-01-05</date><risdate>2005</risdate><volume>44</volume><issue>1</issue><spage>236</spage><epage>240</epage><pages>236-240</pages><issn>0888-5885</issn><eissn>1520-5045</eissn><abstract>Several 10-cm-long capillary tubes [made of poly(ether ether ketone) (PEEK)] with inside diameters of 0.1−2.0 mm were filled with silica monolith-immobilized protease derived by in situ sol−gel transition from a 1:4 mixture of tetramethoxysilane and methyltrimethoxysilane. Transesterification between 20 mM (S)-(−)-glycidol and 0.4 M vinyl n-butyrate in an organic solvent was used as the test reaction. The substrate solution flowed through the column at a flow rate of 0.0004−5.0 mL·min-1. The conversion in the micro-bioreactor was higher than that in the batch reactor at a high liquid flow rate. 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title | Development and Characterization of a Silica Monolith Immobilized Enzyme Micro-bioreactor |
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