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Fabrication and Optimization of a Lipase Immobilized Enzymatic Membrane Bioreactor based on Polysulfone Gradient-Pore Hollow Fiber Membrane
Enzymatic membrane bioreactors (EMBRs) possess the characteristic of combining catalysis with separation, and therefore have promising application potentials. In order to achieve a high-performance EMBR, membrane property, as well as operating parameters, should give special cause for concerns. In t...
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Published in: | Catalysts 2019-06, Vol.9 (6), p.495 |
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description | Enzymatic membrane bioreactors (EMBRs) possess the characteristic of combining catalysis with separation, and therefore have promising application potentials. In order to achieve a high-performance EMBR, membrane property, as well as operating parameters, should give special cause for concerns. In this work, an EMBR based on hollow fiber polysulfone microfiltration membranes with radial gradient pore structure was fabricated and enzyme immobilization was achieved through pressure-driven filtration. Lipase from Candida rugosa was used for immobilization and EMBR performance was studied with the enzymatic hydrolysis of glycerol triacetate as a model reaction. The influences of membrane pore diameter, substrate feed direction as well as operational parameters of operation pressure, substrate concentration, and temperature on the EMBR activity were investigated with the production of hydrolysates kinetically fitted. The complete EMBR system showed the highest activity of 1.07 × 104 U⋅g−1. The results in this work indicate future efforts for improvement in EMBR. |
doi_str_mv | 10.3390/catal9060495 |
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In order to achieve a high-performance EMBR, membrane property, as well as operating parameters, should give special cause for concerns. In this work, an EMBR based on hollow fiber polysulfone microfiltration membranes with radial gradient pore structure was fabricated and enzyme immobilization was achieved through pressure-driven filtration. Lipase from Candida rugosa was used for immobilization and EMBR performance was studied with the enzymatic hydrolysis of glycerol triacetate as a model reaction. The influences of membrane pore diameter, substrate feed direction as well as operational parameters of operation pressure, substrate concentration, and temperature on the EMBR activity were investigated with the production of hydrolysates kinetically fitted. The complete EMBR system showed the highest activity of 1.07 × 104 U⋅g−1. 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The results in this work indicate future efforts for improvement in EMBR.</description><subject>Acids</subject><subject>Adsorption</subject><subject>Aqueous solutions</subject><subject>Bioreactors</subject><subject>Catalysis</subject><subject>Catalysts</subject><subject>Chemical reactions</subject><subject>Efficiency</subject><subject>enzymatic membrane bioreactor</subject><subject>Enzymes</subject><subject>Feed direction</subject><subject>filtration</subject><subject>gradient-pore membrane</subject><subject>Hollow fiber membranes</subject><subject>Hydrolysates</subject><subject>hydrolysis</subject><subject>Immobilization</subject><subject>Influence</subject><subject>Lipase</subject><subject>Membranes</subject><subject>Microfiltration</subject><subject>Morphology</subject><subject>Optimization</subject><subject>Parameters</subject><subject>Permeability</subject><subject>Polysulfone resins</subject><subject>Pore size</subject><subject>Substrates</subject><issn>2073-4344</issn><issn>2073-4344</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2019</creationdate><recordtype>article</recordtype><sourceid>PIMPY</sourceid><sourceid>DOA</sourceid><recordid>eNpNkc1OwzAMxysEEtPYjQeIxJVC2iRteoRpX9LQdtg9chMXZWqbknZC2yvw0gSG0HyxZf_8ty1H0X1Cnxgr6LOGAeqCZpQX4ioapTRnMWecX1_Et9Gk7_c0WJEwmYhR9DWH0tvQa11LoDVk0w22sadzwlUEyNp20CNZNY0rbW1PaMisPR2bgGjyhk3poUXyap1H0IPzpAy4IaF96-pjf6grF-oLD8ZiO8TbwJGlq2v3Sea2RP-vcRfdVFD3OPnz42g3n-2my3i9WaymL-tYsywf4hw4MlklOQgEmgI1BYdwEc9ogholF1UhKaYUcyHLlMkMuC5QJ0mlsUQ2jlZnWeNgrzpvG_BH5cCq34Tz7wp8uK1GRREklUhzk3EOWEAl0GAqaGaMyFgetB7OWp13HwfsB7V3B9-G7VUqeC6Y4DIL1OOZ0t71vcfqf2pC1c_z1OXz2DdO648Q</recordid><startdate>20190601</startdate><enddate>20190601</enddate><creator>Chen, Peng-Cheng</creator><creator>Ma, Zhen</creator><creator>Zhu, Xue-Yan</creator><creator>Chen, Da-Jing</creator><creator>Huang, Xiao-Jun</creator><general>MDPI AG</general><scope>AAYXX</scope><scope>CITATION</scope><scope>7SR</scope><scope>8BQ</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>HCIFZ</scope><scope>JG9</scope><scope>KB.</scope><scope>PDBOC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>DOA</scope><orcidid>https://orcid.org/0000-0003-4682-7364</orcidid></search><sort><creationdate>20190601</creationdate><title>Fabrication and Optimization of a Lipase Immobilized Enzymatic Membrane Bioreactor based on Polysulfone Gradient-Pore Hollow Fiber Membrane</title><author>Chen, Peng-Cheng ; 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subjects | Acids Adsorption Aqueous solutions Bioreactors Catalysis Catalysts Chemical reactions Efficiency enzymatic membrane bioreactor Enzymes Feed direction filtration gradient-pore membrane Hollow fiber membranes Hydrolysates hydrolysis Immobilization Influence Lipase Membranes Microfiltration Morphology Optimization Parameters Permeability Polysulfone resins Pore size Substrates |
title | Fabrication and Optimization of a Lipase Immobilized Enzymatic Membrane Bioreactor based on Polysulfone Gradient-Pore Hollow Fiber Membrane |
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