A pH-response Polyacrylate Amphiphilic Copolymer as The Carrier to Immobilize Laccase

Tingting Yu; Xuejun Cao

doi:10.54097/6dbq7m13

Authors

Tingting Yu
Xuejun Cao

DOI:

https://doi.org/10.54097/6dbq7m13

Keywords:

pH-response copolymer; Laccase; Immobilization.

Abstract

In this study, a pH-response polyacrylate amphiphilic copolymer P_MDB was used as the carrier to immobilize laccase from trametes versicolor. Under optimized conditions, the activity recovery of the immobilized laccase is 71.90%. The infrared spectroscopy results indicate laccase is successfully immobilized on the polymer P_MDB. Also the properties of the immobilized laccase were studied. The recovery of the immobilized laccase is 96.8% (wt%) by adjusting the pH of the immobilized laccase solution to 3.3. And the immobilized laccase remains 78.13% of the initial activity after 5 batches reactions. Compare to the free laccase, the stabilities like thermal and storage stabilities of the immobilized laccase are enhanced. Moreover, the relative activity of immobilized laccase is nearly 110% when the concentration of urea in the solution is 0.02 M. The work in this manuscript can provide valuable references for enzyme immobilization.

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References

Peng, X., Yuan, X. Z., Liu, H., Zeng, G. M. and Chen, X. H. (2015) Degradation of Polycyclic Aromatic Hydrocarbons (PAHs) by Laccase in Rhamnolipid Reversed Micellar System. Applied Biochemistry and Biotechnology, 176, 45-55.

Darvishi, F., Moradi, M., Madzak, C. and Jolivalt, C. (2017) Production of Laccase by Recombinant Yarrowia lipolytica from Molasses: Bioprocess Development Using Statistical Modeling and Increase Productivity in Shake-Flask and Bioreactor Cultures. Applied Biochemistry and Biotechnology, 181, 1228-1239.

Ben Younes, S., Bouallagui, Z. and Sayadi, S. (2012) Catalytic behavior and detoxifying ability of an atypical homotrimeric laccase from the thermophilic strain Scytalidium thermophilum on selected azo and triarylmethane dyes. Journal of Molecular Catalysis B-Enzymatic, 79, 41-48.

Xie, X. M. and Stahl, S. S. (2015) Efficient and Selective Cu/Nitroxyl-Catalyzed Methods for Aerobic Oxidative Lactonization of Diols. Journal of the American Chemical Society, 137, 3767-3770.

Steffensen, C. L., Andersen, M. L., Degn, P. E. and Nielsen, J. H. (2008) Cross-Linking Proteins by Laccase-Catalyzed Oxidation: Importance Relative to Other Modifications. Journal of Agricultural and Food Chemistry, 56, 12002-12010.

Duran, N., Rosa, M. A., D'Annibale, A. and Gianfreda, L. (2002) Applications of laccases and tyrosinases (phenoloxidases) immobilized on different supports: a review. Enzyme and Microbial Technology, 31, 907-931.

Wang, F., Guo, C., Yang, L. R. and Liu, C. Z. (2010) Magnetic mesoporous silica nanoparticles: Fabrication and their laccase immobilization performance. Bioresource Technology, 101, 8931-8935.

Lin, J. H., Wen, Q. L., Chen, S., Le, X. Y., Zhou, X. H. and Huang, L. M. (2017) Synthesis of amine-functionalized Fe3O4@C nanoparticles for laccase immobilization. International Journal of Biological Macromolecules, 96, 377-383.

Goldstein, L. (1976). Kinetic behavior of immobilized enzyme systems. Methods in Enzymology, 44, 397-443.

Liang, W. J. and Cao, X. J. (2012) Preparation of a pH-sensitive polyacrylate amphiphilic copolymer and its application in cellulase immobilization. Bioresource Technology, 116, 140-146.

Zhou, J. Q. and Wang, J. W. (2009) Immobilization of alliinase with a water soluble-insoluble reversible N-succinyl-chitosan for allicin production. Enzyme and Microbial Technology, 45, 299-304.

Yu, X. X., Zou, F. X., Yao, P. P., Huang, X. R. and Qu, Y. B. (2014) Gold nanoparticles tune the activity of laccase in anionic reverse micelles. Soft Matter, 10, 6425-6432.

Zhang, Y., Xu, J. L., Li, D. and Yuan, Z. H. (2010) Preparation and properties of an immobilized cellulase on the reversibly soluble matrix Eudragit L-100. Biocatalysis and Biotransformation, 28, 313-319.

Wang, Y., Zhang, D., He, F. R. and Chen, X. C. (2012) Immobilization of laccase by Cu2+ chelate affinity interaction on surface modified magnetic silica particles and its use for the removal of pentachlorophenol. Chinese Chemical Letters, 23, 197-200.

Lee, K. M., Kalyani, D., Tiwari, M. K., Kim, T. S., Dhiman, S. S., Lee, J. K. and Kim, I. W. (2012) Enhanced enzymatic hydrolysis of rice straw by removal of phenolic compounds using a novel laccase from yeast Yarrowia lipolytica. Bioresource Technology, 123, 636-645.

Sari, M., Akgol, S., Karatas, M. and Denizli, A. (2006) Reversible immobilization of catalase by metal chelate affinity interaction on magnetic beads. Industrial & Engineering Chemistry Research, 45, 3036-3043.

Chen, S. H., Yen, Y. H., Wang, C. L. and Wang, S. L. (2003) Reversible immobilization of lysozyme via coupling to reversibly soluble polymer. Enzyme and Microbial Technology, 33, 643-649.

Zhou, B., Wan, J. F., Wang, J. Z. and Cao, X. J. (2012) Effect of chaotropes in reverse micellar extraction of kallikrein. Process Biochemistry, 47, 229-233.

Yu, T. and Cao, X. (2014) Effect of Chaotropes on Lipase Back Extraction Recovery in the Process of Reverse Micellar Extraction. Applied Biochemistry and Biotechnology, 172, 3287-3296.

Makas, Y. G., Kalkan, N. A., Aksoy, S., Altinok, H. and Hasirci, N. (2010) Immobilization of laccase in kappa-carrageenan based semi-interpenetrating polymer networks. Journal of Biotechnology, 148, 216-220.

Tukel, S. S. and Alptekin, O. (2004) Immobilization and kinetics of catalase onto magnesium silicate. Process Biochemistry, 39, 2149-2155.