Evaluation of fungal laccase immobilized on natural nanostructured bacterial cellulose
The aim of this work was to assess the possibility of using native bacterial nanocellulose (BC) as a carrier for laccase immobilization. BC was synthesized by Gluconacetobacter xylinus, which was statically cultivated in a mannitol-based medium and was freeze-dried to form BC sponge after purificati...
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doaj-07a68a07ddc44580a8b26304487cc1e72020-11-24T23:45:15ZengFrontiers Media S.A.Frontiers in Microbiology1664-302X2015-11-01610.3389/fmicb.2015.01245165489Evaluation of fungal laccase immobilized on natural nanostructured bacterial celluloseLin eChen0Lin eChen1Min eZou2Feng F. Hong3Feng F. Hong4Donghua UniversityKey Laboratory of High Performance fibers & products, Ministry of Education, Donghua UniversityDonghua UniversityDonghua UniversityKey Laboratory of High Performance fibers & products, Ministry of Education, Donghua UniversityThe aim of this work was to assess the possibility of using native bacterial nanocellulose (BC) as a carrier for laccase immobilization. BC was synthesized by Gluconacetobacter xylinus, which was statically cultivated in a mannitol-based medium and was freeze-dried to form BC sponge after purification. For the first time, fungal laccase from Trametes versicolor was immobilized on the native nanofibril network-structured BC sponge through physical adsorption and cross-linking with glutaraldehyde. The properties including morphologic and structural features of the BC as well as the immobilized enzyme were thoroughly investigated. It was found that enzyme immobilized by cross-linking exhibited broader pH operation range of high catalytic activity as well as higher running stability compared to free and adsorbed enzyme. Using ABTS as substrate, the optimum pH value was 3.5 for the adsorption-immobilized laccase and 4.0 for the crosslinking-immobilized laccase. The immobilized enzyme retained 69% of the original activity after being recycled 7 times. Novel applications of the BC-immobilized enzyme tentatively include active packaging, construction of biosensors, and establishment of bioreactors.http://journal.frontiersin.org/Journal/10.3389/fmicb.2015.01245/fullAdsorptionImmobilizationLaccaseBacterial celluloseCross-linking |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Lin eChen Lin eChen Min eZou Feng F. Hong Feng F. Hong |
spellingShingle |
Lin eChen Lin eChen Min eZou Feng F. Hong Feng F. Hong Evaluation of fungal laccase immobilized on natural nanostructured bacterial cellulose Frontiers in Microbiology Adsorption Immobilization Laccase Bacterial cellulose Cross-linking |
author_facet |
Lin eChen Lin eChen Min eZou Feng F. Hong Feng F. Hong |
author_sort |
Lin eChen |
title |
Evaluation of fungal laccase immobilized on natural nanostructured bacterial cellulose |
title_short |
Evaluation of fungal laccase immobilized on natural nanostructured bacterial cellulose |
title_full |
Evaluation of fungal laccase immobilized on natural nanostructured bacterial cellulose |
title_fullStr |
Evaluation of fungal laccase immobilized on natural nanostructured bacterial cellulose |
title_full_unstemmed |
Evaluation of fungal laccase immobilized on natural nanostructured bacterial cellulose |
title_sort |
evaluation of fungal laccase immobilized on natural nanostructured bacterial cellulose |
publisher |
Frontiers Media S.A. |
series |
Frontiers in Microbiology |
issn |
1664-302X |
publishDate |
2015-11-01 |
description |
The aim of this work was to assess the possibility of using native bacterial nanocellulose (BC) as a carrier for laccase immobilization. BC was synthesized by Gluconacetobacter xylinus, which was statically cultivated in a mannitol-based medium and was freeze-dried to form BC sponge after purification. For the first time, fungal laccase from Trametes versicolor was immobilized on the native nanofibril network-structured BC sponge through physical adsorption and cross-linking with glutaraldehyde. The properties including morphologic and structural features of the BC as well as the immobilized enzyme were thoroughly investigated. It was found that enzyme immobilized by cross-linking exhibited broader pH operation range of high catalytic activity as well as higher running stability compared to free and adsorbed enzyme. Using ABTS as substrate, the optimum pH value was 3.5 for the adsorption-immobilized laccase and 4.0 for the crosslinking-immobilized laccase. The immobilized enzyme retained 69% of the original activity after being recycled 7 times. Novel applications of the BC-immobilized enzyme tentatively include active packaging, construction of biosensors, and establishment of bioreactors. |
topic |
Adsorption Immobilization Laccase Bacterial cellulose Cross-linking |
url |
http://journal.frontiersin.org/Journal/10.3389/fmicb.2015.01245/full |
work_keys_str_mv |
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