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Catalysts 2017, 7(12), 359; doi:10.3390/catal7120359

Approaching Immobilization of Enzymes onto Open Porous Basotect®

1
Laboratory for Biopolymers, Institute of Applied Chemistry, Brandenburg University of Technology Cottbus-Senftenberg, Universitätsplatz1, 01968 Senftenberg, Germany
2
Laboratory for Technical Microbiology, Institute of Biotechnology, Brandenburg University of Technology Cottbus-Senftenberg, Universitätsplatz1, 01968 Senftenberg, Germany
These authors contributed equally to this work.
*
Author to whom correspondence should be addressed.
Academic Editor: Peter Grunwald
Received: 17 October 2017 / Revised: 14 November 2017 / Accepted: 16 November 2017 / Published: 27 November 2017
(This article belongs to the Special Issue Immobilized Biocatalysts)
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Abstract

For the first time, commercial macroporous melamine formaldehyde foam Basotect® (BT) was used as a basic carrier material for both adsorptive and covalent enzyme immobilization. In order to access inherent amino groups, the Basotect® surface was pretreated with hydrochloric acid. The resulting material revealed 6 nmol of superficial amino groups per milligram Basotect®. Different optimized strategies for tethering the laccase from Trametes versicolor and the lipase from Thermomyces lanuginosus onto the pre-treated Basotect® surface were studied. Particularly, for covalent immobilization, two different strategies were pursued: lipase was tethered via a cross-linking method using 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide, and laccase was bound after functionalizing Basotect® with hydrophilic copolymer poly(ethylene-alt-maleic anhydride) (PEMA). Prior to laccase immobilization, the PEMA coating of Basotect® was verified by ATR-FTIR analysis. Subsequent quantification of available high-reactive PEMA anhydride moieties revealed an amount of 1028 ± 73 nmol per mg Basotect®. The surface-bound enzyme amounts were quantified as 4.1–5.8 μg per mg Basotect®. A theoretical surface-covered enzyme mass for the ideal case that an enzyme monolayer was immobilized onto the Basotect® surface was calculated and compared to the amount of adsorptive and covalently bound enzymes before and after treatment with SDS. Furthermore, the enzyme activities were determined for the different immobilization approaches, and the stability during storage over time and against sodium dodecyl sulfate treatment was monitored. Additionally, PEMA-BT-bound laccase was tested for the elimination of anthropogenic micropollutant bisphenol A from contaminated water in a cost-effective and environmentally-friendly way and resulted in a degradation rate higher than 80%. View Full-Text
Keywords: Basotect®; enzyme immobilization; laccase; lipase; PEMA; EDC; bisphenol A Basotect®; enzyme immobilization; laccase; lipase; PEMA; EDC; bisphenol A
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MDPI and ACS Style

Allertz, P.J.; Berger, S.; Sellenk, G.; Dittmer, C.; Dietze, M.; Stahmann, K.-P.; Salchert, K. Approaching Immobilization of Enzymes onto Open Porous Basotect®. Catalysts 2017, 7, 359.

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