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Paper-based Photocatalysts Immobilization without Coffee Ring Effect for Photocatalytic Water Purification.

ABSTRACT: Photocatalytic water purification is important for the degradation of organic pollutants, attracting intensive interests. Photocatalysts are preferred to be immobilized on a substrate in order to reduce the laborious separation and recycling steps. To get uniform irradiation, the photocatalysts are preferred to be even/uniform on the substrate without aggregation. Generally, the "coffee ring effect" occurs on the substrate during solvent evaporation, unfortunately resulting in the aggregation of the photocatalysts. This aggregation inevitably blocks the exposure of active sites, reactant exchange, and light absorption. Here, we reported a paper-based photocatalyst immobilization method to solve the "coffee ring" problem. We also used a "drop reactor" to achieve good photocatalytic efficiency with the advantages of large surface area, short diffusion lengths, simple operation, and uniform light absorption. Compared with the coffee ring type, the paper-based method showed higher water purification efficiency, indicating its potential application value in the future.

SUBMITTER: Li Q

PROVIDER: S-EPMC7143163 | biostudies-literature | 2020 Feb

REPOSITORIES: biostudies-literature

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Paper-based Photocatalysts Immobilization without Coffee Ring Effect for Photocatalytic Water Purification.

Li Qingwei Q Lin Huichao H Huang Xiaowen X Lyu Maocui M Zhang Hongxia H Zhang Xiaoning X Wang Ruiming R

Micromachines 20200226 3

Photocatalytic water purification is important for the degradation of organic pollutants, attracting intensive interests. Photocatalysts are preferred to be immobilized on a substrate in order to reduce the laborious separation and recycling steps. To get uniform irradiation, the photocatalysts are preferred to be even/uniform on the substrate without aggregation. Generally, the "coffee ring effect" occurs on the substrate during solvent evaporation, unfortunately resulting in the aggregation of ...[more]

PMID: 32111056

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Project description:Site-specific chemical modification of proteins is important for many applications in biology and biotechnology. Recently, our laboratory and others have exploited the high specificity of the enzyme protein farnesyltransferase (PFTase) to site-specifically modify proteins through the use of alternative substrates that incorporate bioorthogonal functionality including azides and alkynes. In this study, we evaluate two aldehyde-containing molecules as substrates for PFTase and as reactants in both oxime and hydrazone formation. Using green fluorescent protein (GFP) as a model system, we demonstrate that the purified protein can be enzymatically modified with either analogue to yield aldehyde-functionalized proteins. Oxime or hydrazone formation was then employed to immobilize, fluorescently label, or PEGylate the resulting aldehyde-containing proteins. Immobilization via hydrazone formation was also shown to be reversible via transoximization with a fluorescent alkoxyamine. After characterizing this labeling strategy using pure protein, the specificity of the enzymatic process was used to selectively label GFP present in crude E. coli extract followed by capture of the aldehyde-modified protein using hydrazide-agarose. Subsequent incubation of the immobilized protein using a fluorescently labeled or PEGylated alkoxyamine resulted in the release of pure GFP containing the desired site-specific covalent modifications. This procedure was also employed to produce PEGylated glucose-dependent insulinotropic polypeptide (GIP), a protein with potential therapeutic activity for diabetes. Given the specificity of the PFTase-catalyzed reaction coupled with the ability to introduce a CAAX-box recognition sequence onto almost any protein, this method shows great potential as a general approach for selective immobilization and labeling of recombinant proteins present in crude cellular extract without prior purification. Beyond generating site-specifically modified proteins, this approach for polypeptide modification could be particularly useful for large-scale production of protein conjugates for therapeutic or industrial applications.

Dataset Information

Paper-based Photocatalysts Immobilization without Coffee Ring Effect for Photocatalytic Water Purification.

Publications

Paper-based Photocatalysts Immobilization without Coffee Ring Effect for Photocatalytic Water Purification.

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