Laccase immobilization on titania nanoparticles and titania-functionalized membranes

Bio-catalytic degradation of recalcitrant micropollutants with enzymes such as laccase provides an environmentally attractive alternative to the conventional filtration and adsorption processes. However, enzyme loss and denaturation remain key challenges for their potential use in water treatment ap...

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Published inJournal of membrane science Vol. 452; pp. 229 - 240
Main Authors Hou, Jingwei, Dong, Guangxi, Ye, Yun, Chen, Vicki
Format Journal Article
LanguageEnglish
Published Amsterdam Elsevier B.V 01.02.2014
Elsevier
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Abstract Bio-catalytic degradation of recalcitrant micropollutants with enzymes such as laccase provides an environmentally attractive alternative to the conventional filtration and adsorption processes. However, enzyme loss and denaturation remain key challenges for their potential use in water treatment applications. In this work, laccase immobilization on TiO2 nanoparticles and TiO2 blended polyethersulfone (PES) membranes were investigated due to TiO2's chemical stability, ease of functionalization, and architecture. Different surface modification and functionalization strategies on support materials were compared based on enzyme loading, apparent activity, activity recovery, and stability. When coupling agent 3-aminopropyltriethoxysilane (APTES) and cross-linker glutaraldehyde (GLU) were applied sequentially, effective coupling of laccase was achieved based on 2,2′-azino-bis-(3-ethyl benzothiazoline-6-sulfonic acid) (ABTS) assays. TiO2 functionalized PES membrane showed better enzyme immobilization efficiency than the non-functionalized membrane. Optimal performance was observed for PES membrane containing 4wt% TiO2, where TiO2 not only provided the enzyme coupling sites but also affected the membrane surface morphology and hydrophilicity to favor the enzyme immobilization. These bio-catalytic membranes also displayed good enzyme stability, tolerance to wider pH range and vigorous filtration conditions required for water treatment applications. Kinetic study also indicated that the enzyme affinity to assay substrate was maintained after immobilization when compared with packed bed and batch reactors. [Display omitted] •Laccase is immobilized on TiO2 nanoparticles and TiO2 functionalized membranes.•TiO2 loading has significant effect on bio-catalytic membrane performance.•Bio-catalytic membrane stability is mainly determined by immobilization technique.•Laccase on membrane has higher affinity to ABTS than batch and packed bed reactors.
AbstractList Bio-catalytic degradation of recalcitrant micropollutants with enzymes such as laccase provides an environmentally attractive alternative to the conventional filtration and adsorption processes. However, enzyme loss and denaturation remain key challenges for their potential use in water treatment applications. In this work, laccase immobilization on TiO2 nanoparticles and TiO2 blended polyethersulfone (PES) membranes were investigated due to TiO2's chemical stability, ease of functionalization, and architecture. Different surface modification and functionalization strategies on support materials were compared based on enzyme loading, apparent activity, activity recovery, and stability. When coupling agent 3-aminopropyltriethoxysilane (APTES) and cross-linker glutaraldehyde (GLU) were applied sequentially, effective coupling of laccase was achieved based on 2,2′-azino-bis-(3-ethyl benzothiazoline-6-sulfonic acid) (ABTS) assays. TiO2 functionalized PES membrane showed better enzyme immobilization efficiency than the non-functionalized membrane. Optimal performance was observed for PES membrane containing 4wt% TiO2, where TiO2 not only provided the enzyme coupling sites but also affected the membrane surface morphology and hydrophilicity to favor the enzyme immobilization. These bio-catalytic membranes also displayed good enzyme stability, tolerance to wider pH range and vigorous filtration conditions required for water treatment applications. Kinetic study also indicated that the enzyme affinity to assay substrate was maintained after immobilization when compared with packed bed and batch reactors. [Display omitted] •Laccase is immobilized on TiO2 nanoparticles and TiO2 functionalized membranes.•TiO2 loading has significant effect on bio-catalytic membrane performance.•Bio-catalytic membrane stability is mainly determined by immobilization technique.•Laccase on membrane has higher affinity to ABTS than batch and packed bed reactors.
Bio-catalytic degradation of recalcitrant micropollutants with enzymes such as laccase provides an environmentally attractive alternative to the conventional filtration and adsorption processes. However, enzyme loss and denaturation remain key challenges for their potential use in water treatment applications. In this work, laccase immobilization on TiO2 nanoparticles and TiO2 blended polyethersulfone (PES) membranes were investigated due to TiO2's chemical stability, ease of functionalization, and architecture. Different surface modification and functionalization strategies on support materials were compared based on enzyme loading, apparent activity, activity recovery, and stability. When coupling agent 3-aminopropyltriethoxysilane (APTES) and cross-linker glutaraldehyde (GLU) were applied sequentially, effective coupling of laccase was achieved based on 2,2'-azino-bis-(3-ethyl benzothiazoline-6-sulfonic acid) (ABTS) assays. TiO2 functionalized PES membrane showed better enzyme immobilization efficiency than the non-functionalized membrane. Optimal performance was observed for PES membrane containing 4 wt% TiO2, where TiO2 not only provided the enzyme coupling sites but also affected the membrane surface morphology and hydrophilicity to favor the enzyme immobilization. These bio-catalytic membranes also displayed good enzyme stability, tolerance to wider pH range and vigorous filtration conditions required for water treatment applications. Kinetic study also indicated that the enzyme affinity to assay substrate was maintained after immobilization when compared with packed bed and batch reactors.
Author Chen, Vicki
Ye, Yun
Hou, Jingwei
Dong, Guangxi
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Keywords TiO2 nanoparticles
Bio-catalytic membrane
Laccase immobilization
Catalytic reaction
Biocatalysis
Nanoparticle
Transition element compounds
Immobilization
Enzymatic catalysis
Ethersulfone polymer
nanoparticles
Membrane
TiO
Titanium oxide
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Snippet Bio-catalytic degradation of recalcitrant micropollutants with enzymes such as laccase provides an environmentally attractive alternative to the conventional...
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SubjectTerms Bio-catalytic membrane
Biological and medical sciences
Catalysis
Chemistry
Colloidal state and disperse state
Coupling agents
Enzymes
Exact sciences and technology
Filtration
Fundamental and applied biological sciences. Psychology
General and physical chemistry
Immobilization
Laccase
Laccase immobilization
Mechanisms. Catalysis. Electron transfer. Models
Membranes
Molecular biophysics
Physical and chemical studies. Granulometry. Electrokinetic phenomena
Physical chemistry in biology
Surface chemistry
Theory of reactions, general kinetics. Catalysis. Nomenclature, chemical documentation, computer chemistry
TiO2 nanoparticles
Titanium dioxide
Title Laccase immobilization on titania nanoparticles and titania-functionalized membranes
URI https://dx.doi.org/10.1016/j.memsci.2013.10.019
https://search.proquest.com/docview/1520365145
https://search.proquest.com/docview/1642304906
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