Multienzymatic immobilization of laccases on polymeric microspheres: A strategy to expand the maximum catalytic efficiencyVera, M., Fodor, C., Garcia, Y., Pereira, E., Loos, K. & Rivas, B. L., 1-Jul-2020, In : Journal of Applied Polymer Science. 11 p., 49562.
Research output: Contribution to journal › Article › Academic › peer-review
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.
|Number of pages||11|
|Journal||Journal of Applied Polymer Science|
|Publication status||E-pub ahead of print - 1-Jul-2020|
- bioengineering, biomaterials, catalysts, morphology, proteins, ENZYME-ACTIVITY, DEGRADATION