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Multienzymatic immobilization of laccases on polymeric microspheres: A strategy to expand the maximum catalytic efficiency

Vera, M., Fodor, C., Garcia, Y., Pereira, E., Loos, K. & Rivas, B. L., 1-Jul-2020, In : Journal of Applied Polymer Science. 11 p., 49562.

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  • Multienzymatic immobilization of laccases on polymeric microspheres: A strategy to expand the maximum catalytic efficiency

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DOI

  • Myleidi Vera
  • Csaba Fodor
  • Yadiris Garcia
  • Eduardo Pereira
  • Katja Loos
  • Bernabe L. Rivas

Laccase enzymes of were covalently coimmobilized on poly(glycidyl methacrylate) microspheres. The objective of this work was to create a biocatalyst that works efficiently in a wide range of pH. The coimmobilization was performed using two different strategies to compare the most efficient. The results showed that by correctly selecting the enzymes and concentrations involved in the commobilization, it is possible to obtain a biocatalyst that works efficiently at a wide pH range (2.0-7.0). The maximum activity values reached per gram of support for the obtained biocatalyst were 41.90 U (pH 3.0), 40.89 U (pH 4.0), and 39.54 U (pH 6.0). Moreover, the thermal, storage, and mechanical stabilities were improved compared to the free and single-immobilized laccases. It was concluded that enzymatic coimmobilization is an excellent alternative to obtain a robust biocatalyst that works in a wide pH range, with potential environmental and industrial applications.

Original languageEnglish
Article number49562
Number of pages11
JournalJournal of Applied Polymer Science
Publication statusE-pub ahead of print - 1-Jul-2020

    Keywords

  • bioengineering, biomaterials, catalysts, morphology, proteins, ENZYME-ACTIVITY, DEGRADATION

ID: 130888699