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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Main Authors: Lin eChen, Min eZou, Feng F. Hong
Format: Article
Language:English
Published: Frontiers Media S.A. 2015-11-01
Series:Frontiers in Microbiology
Subjects:
Online Access:http://journal.frontiersin.org/Journal/10.3389/fmicb.2015.01245/full
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spelling 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
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AT fengfhong evaluationoffungallaccaseimmobilizedonnaturalnanostructuredbacterialcellulose
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