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. 2016 Jun 6;8(6):223.
doi: 10.3390/polym8060223.

Design and Preparation of Nano-Lignin Peroxidase (NanoLiP) by Protein Block Copolymerization Approach

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Free PMC article

Design and Preparation of Nano-Lignin Peroxidase (NanoLiP) by Protein Block Copolymerization Approach

Turgay Tay et al. Polymers (Basel). .
Free PMC article

Abstract

This study describes the preparation of nanoprotein particles having lignin peroxidase (LiP) using a photosensitive microemulsion polymerization technique. The protein-based nano block polymer was synthesized by cross-linking of ligninase enzyme with ruthenium-based aminoacid monomers. This type polymerization process brought stability in different reaction conditions, reusability and functionality to the protein-based nano block polymer system when compared the traditional methods. After characterization of the prepared LiP copolymer nanoparticles, enzymatic activity studies of the nanoenzymes were carried out using tetramethylbenzidine (TMB) as the substrate. The parameters such as pH, temperature and initial enzyme concentration that affect the activity, were investigated by using prepared nanoLip particles and compared to free LiP. The reusability of the nano-LiP particles was also investigated and the obtained results showed that the nano-LiP particles exhibited admirable potential as a reusable catalyst.

Keywords: ANADOLUCA; lignin peroxidase (LiP); nanoenzyme; photosensitive monomer; tetramethylbenzidine (TMB).

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Conflict of interest statement

The authors declare no conflict of interest.

Figures

Figure 1
Figure 1
Schematic depiction of the preparation of bis(2-2’-bipyridyl)(MATyr)2-Ruthenium (II).
Figure 2
Figure 2
Schematic illustration of the synthesized nano lignin peroxidase enzyme.
Figure 3
Figure 3
Size distrubition of the LiP nanoparticles.
Figure 4
Figure 4
pH effect on the activity of free and Nano-LiP.
Figure 5
Figure 5
Temperature effect on the activity of free and Nano-LiP.
Figure 6
Figure 6
Reusability of the Nano-LiP particles.
Figure 7
Figure 7
Activity of the nanoparticles prepared in different batches.
Figure 8
Figure 8
Linearity of free LiP and Nano-LiP.
Figure 9
Figure 9
Repeatability of free LiP and Nano-LiP particles.

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References

    1. Tien M., Kirk T.K. Lignin-degrading enzyme from the hymenomycete Phanerochaete chrysosporium burds. Science. 1983;221:661–663. doi: 10.1126/science.221.4611.661. - DOI - PubMed
    1. Tien M., Kirk T.K. Lignin-degrading enzyme from Phanerochaete chrysosporium: Purification characterization, and catalytic properties of a unique H2O2-requiring oxygenase. Proc. Natl. Acad. Sci. USA. 1984;81:2280–2284. doi: 10.1073/pnas.81.8.2280. - DOI - PMC - PubMed
    1. Pahujani S., Kanwar S.S., Chauhan G., Gupta R. Glutaraldehyde activation of polymer Nylon-6 for lipase immobilization: Enzyme characteristics and stability. Bioresour. Technol. 2008;99:2566–2570. doi: 10.1016/j.biortech.2007.04.042. - DOI - PubMed
    1. Yu H.W., Chen H., Wang X., Yang Y.Y., Ching C.B. Cross-linked enzyme aggregates with controlled particles: Application to Candida rugosa lipase. J. Mol. Catal. B Enzym. 2006;43:124–127. doi: 10.1016/j.molcatb.2006.07.001. - DOI
    1. Ye P., Jiang J., Xu Z.K. Adsorption and activity of lipase from Candida rugosa on the chitosan-modified poly(acrylonitrile-co-maleic acid) membrane surface. Colloids Surf. B Biointerface. 2007;60:62–67. doi: 10.1016/j.colsurfb.2007.05.022. - DOI - PubMed

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