Cellulase immobilization on superparamagnetic nanoparticles for reuse in cellulosic biomass conversion

Current cellulosic biomass hydrolysis is based on the one-time use of cellulases. Cellulases immobilized on magnetic nanocarriers offer the advantages of magnetic separation and repeated use for continuous hydrolysis. Most immobilization methods focus on only one type of cellulase. Here, we report c...

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Main Authors: Fernando Segato, Mark Wilkins, Rolf Prade, Yu Mao, Qing Song
Format: Article
Language:English
Published: AIMS Press 2016-07-01
Series:AIMS Bioengineering
Subjects:
Online Access:http://www.aimspress.com/Bioengineering/article/869/fulltext.html
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spelling doaj-466fe79522284f20aca9d7dbab5bf4f52020-11-25T01:14:57ZengAIMS PressAIMS Bioengineering2375-14952016-07-013326427610.3934/bioeng.2016.3.264bioeng-03-00264Cellulase immobilization on superparamagnetic nanoparticles for reuse in cellulosic biomass conversionFernando Segato0Mark Wilkins1Rolf Prade2Yu Mao3Qing Song4Department of Microbiology and Molecular Genetics, Oklahoma State University, Stillwater, OK 74078, USADepartment of Biosystems Engineering, Oklahoma State University, Stillwater, OK 74078, USADepartment of Microbiology and Molecular Genetics, Oklahoma State University, Stillwater, OK 74078, USADepartment of Biosystems Engineering, Oklahoma State University, Stillwater, OK 74078, USADepartment of Immunology, Institute of Tuberculosis Control, Institute of Human Virology, Zhongshan School of Medicine, Sun Yat-sen University, Guangzhou 510080, China; Key Laboratory of Tropical Diseases Control (Sun Yat-sen University), Ministry of Education, Guangzhou 510080, ChinaCurrent cellulosic biomass hydrolysis is based on the one-time use of cellulases. Cellulases immobilized on magnetic nanocarriers offer the advantages of magnetic separation and repeated use for continuous hydrolysis. Most immobilization methods focus on only one type of cellulase. Here, we report co-immobilization of two types of cellulases, β-glucosidase A (BglA) and cellobiohydrolase D (CelD), on sub-20 nm superparamagnetic nanoparticles. The nanoparticles demonstrated 100% immobilization efficiency for both BglA and CelD. The total enzyme activities of immobilized BglA and CelD were up to 67.1% and 41.5% of that of the free cellulases, respectively. The immobilized BglA and CelD each retained about 85% and 43% of the initial immobilized enzyme activities after being recycled 3 and 10 times, respectively. The effects of pH and temperature on the immobilized cellulases were also investigated. Co-immobilization of BglA and CelD on MNPs is a promising strategy to promote synergistic action of cellulases while lowering enzyme consumption.http://www.aimspress.com/Bioengineering/article/869/fulltext.htmlenzyme co-immobilizationβ-glucosidasecellobiohydrolasesuperparamagnetic nanoparticlescellulase reuse
collection DOAJ
language English
format Article
sources DOAJ
author Fernando Segato
Mark Wilkins
Rolf Prade
Yu Mao
Qing Song
spellingShingle Fernando Segato
Mark Wilkins
Rolf Prade
Yu Mao
Qing Song
Cellulase immobilization on superparamagnetic nanoparticles for reuse in cellulosic biomass conversion
AIMS Bioengineering
enzyme co-immobilization
β-glucosidase
cellobiohydrolase
superparamagnetic nanoparticles
cellulase reuse
author_facet Fernando Segato
Mark Wilkins
Rolf Prade
Yu Mao
Qing Song
author_sort Fernando Segato
title Cellulase immobilization on superparamagnetic nanoparticles for reuse in cellulosic biomass conversion
title_short Cellulase immobilization on superparamagnetic nanoparticles for reuse in cellulosic biomass conversion
title_full Cellulase immobilization on superparamagnetic nanoparticles for reuse in cellulosic biomass conversion
title_fullStr Cellulase immobilization on superparamagnetic nanoparticles for reuse in cellulosic biomass conversion
title_full_unstemmed Cellulase immobilization on superparamagnetic nanoparticles for reuse in cellulosic biomass conversion
title_sort cellulase immobilization on superparamagnetic nanoparticles for reuse in cellulosic biomass conversion
publisher AIMS Press
series AIMS Bioengineering
issn 2375-1495
publishDate 2016-07-01
description Current cellulosic biomass hydrolysis is based on the one-time use of cellulases. Cellulases immobilized on magnetic nanocarriers offer the advantages of magnetic separation and repeated use for continuous hydrolysis. Most immobilization methods focus on only one type of cellulase. Here, we report co-immobilization of two types of cellulases, β-glucosidase A (BglA) and cellobiohydrolase D (CelD), on sub-20 nm superparamagnetic nanoparticles. The nanoparticles demonstrated 100% immobilization efficiency for both BglA and CelD. The total enzyme activities of immobilized BglA and CelD were up to 67.1% and 41.5% of that of the free cellulases, respectively. The immobilized BglA and CelD each retained about 85% and 43% of the initial immobilized enzyme activities after being recycled 3 and 10 times, respectively. The effects of pH and temperature on the immobilized cellulases were also investigated. Co-immobilization of BglA and CelD on MNPs is a promising strategy to promote synergistic action of cellulases while lowering enzyme consumption.
topic enzyme co-immobilization
β-glucosidase
cellobiohydrolase
superparamagnetic nanoparticles
cellulase reuse
url http://www.aimspress.com/Bioengineering/article/869/fulltext.html
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AT yumao cellulaseimmobilizationonsuperparamagneticnanoparticlesforreuseincellulosicbiomassconversion
AT qingsong cellulaseimmobilizationonsuperparamagneticnanoparticlesforreuseincellulosicbiomassconversion
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