Immobilization of cellulase onto MnO2 nanoparticles for bioethanol production by enhanced hydrolysis of agricultural waste

Cherian, Elsa; Dharmendirakumar, M.; Baskar, G.

doi:10.1016/s1872-2067(15)60906-8

Cited by 158 publications

(27 citation statements)

References 34 publications

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“…Many previous studies have described the use of different CAZymes and supports for immobilization. Some have reported an optimum temperature increase of 5°C, an 80% increase in catalytic activity, a 22% increase in product yield, a 4‐fold increase in enzyme half‐life, and a retention of 92% of activity after 17 cycles of use . Therefore, enzyme immobilization may prove to be of some significance in biorefining, given its implications for reduced enzyme loading, making for a more efficient, robust, inexpensive, and market‐competitive process.…”

Section: Enzyme Immobilizationmentioning

confidence: 99%

Bringing plant cell wall‐degrading enzymes into the lignocellulosic biorefinery concept

Silva

Vaz

Filho

2017

Biofuels Bioprod Bioref

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Recent decades have seen the growth of immense interest in lignocellulosic biomass conversion technologies. This interest is motivated by their huge potential for energy and bioproduct generation and reduced dependency on non-renewable feedstocks, leading to improved air quality and reduced emission of greenhouse gases. It is in this context that the lignocellulose biorefi nery concept arises. Among the lignocellulose conversion technologies available, enzymatic conversion has emerged as a promising candidate, since it represents a biomass management approach that integrates recycling and remediation in an environmentally friendly manner. Although already in existence, biorefi neries employing enzymatic conversion of lignocellulose are at an incipient stage. There remain many operational diffi culties, resulting in a very costly overall process that is refl ected in product price, reducing market competitiveness. Therefore, much research is still needed to improve the operational and fi nancial feasibility of this process. This paper covers general biorefi nery concepts, as well as new and associated concepts, such as the circular economy, bioeconomy, and waste biorefi nery. Subsequently, the global outlook, including examples of currently existing enzyme-based lignocellulose biorefi neries and their status, is described. The main technical and economic challenges are also discussed, and various potential tools for the optimization of biomass degradation in enzyme-based biorefi neries are presented. Finally, the future perspectives for the sector are considered, and models of the ideal biorefi nery and globally integrated biorefi nery hubs are proposed. These models may contribute to the future establishment of such biorefi neries as competitive industries, consistent with the sustainable bioelectro economy paradigm. (Brazil). His research focuses on the valorization of Brazilian agroindustrial residues, mainly sugarcane bagasse, as substrate for enzyme synthesis and conversion into bioproducts. He is currently involved in the investigation of pretreatment technologies to enhance holocellulase production when employing lignocellulosic materials as substrate for filamentous fungi. Raissa P. VazRaissa P. Vaz is a PhD student at the Department of Cell Biology of the University of Brasília (Brazil). Her work is focused mainly on immobilization, characterization, and applications of lignocellulose-degrading enzymes. Edivaldo X.F. FilhoEdivaldo X.F. Filho is Professor of Biochemistry at the Department of Cell Biology of the University of Brasília (Brazil). He conducts research in the fields of biochemistry and biotechnology, investigating the production, purification, characterization, and biotechnology applications of lignocellulose-degrading enzymes from filamentous fungi.

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Section: Enzyme Immobilizationmentioning

confidence: 99%

Bringing plant cell wall‐degrading enzymes into the lignocellulosic biorefinery concept

Silva

Vaz

Filho

2017

Biofuels Bioprod Bioref

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“…Immobilization of cellulase on the solid support can provide a technique to increase stability and reusability [7][8]. The support which had been reported to be used as enzyme carrier were TiO2 [9], polyurethane foam [10], entrapped in silica gel membrane [11], MnO 2 [12], polyvinyl alcohol [13], chitosan [14], etc. Nevertheless, the mass transfer becomes the main obstacle since cellulose and immobilized enzyme are insoluble substrates.…”

Section: ■ Introductionmentioning

confidence: 99%

Synergistic Effect of Two Type Cellulase Immobilized on Chitosan Microparticle as Biocatalyst for Coconut Husk Hydrolysis

et al. 2019

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The effectivity of employing two types of cellulases from Aspergillus niger and Trichoderma resei covalently immobilized on chitosan microparticle was investigated. Reducing sugar from CMC yielded by immobilized cellulase from T. resei alone and A. niger alone was 0.316 g/L and 0.244 g/L, respectively. Simultaneous use of both cellulases shows a significant increase of reducing sugar produced to 1.020 g/L. The effective combination of this two types of cellulases also occurred when coconut husk was used as substrate. A very high enzyme coupling of 92.06% compared to free enzyme was obtained in the immobilization. Addition of GDA not only increased enzyme coupling to 100% but also improved sugar produced. Immobilized cellulase was successfully maintained its activity until 5 cycles

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“…The effects of nanomaterials on the thermal stability of enzyme have been reported in some of the studies. In one of the studies by Cherian et al (2015) , the cellulase immobilized on MnO 2 nanoparticles showed thermal stability for 2 h while the control (without immobilization) showed its thermal stability for 1 h, only. In one of the other study by Zhang et al (2015) , the cellulase immobilized at functionalized magnetic nanoparticles showed thermal stability about 97.8% at 40°C.…”

Section: Resultsmentioning

confidence: 99%

Application of ZnO Nanoparticles for Improving the Thermal and pH Stability of Crude Cellulase Obtained from Aspergillus fumigatus AA001

Srivastava

Mishra

et al. 2016

Front. Microbiol.

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Cellulases are the enzymes which are responsible for the hydrolysis of cellulosic biomass. In this study thermal and pH stability of crude cellulase has been investigated in the presence of zinc oxide (ZnO) nanoparticles. We synthesized ZnO nanoparticle by sol-gel method and characterized through various techniques including, X-ray Diffraction, ultraviolet-visible spectroscope, field emission scanning electron microscope and high resolution scanning electron microscope. The crude thermostable cellulase has been obtained from the Aspergillus fumigatus AA001 and treated with ZnO nanoparticle which shows thermal stability at 65°C up to 10 h whereas it showed pH stability in the alkaline pH range and retained its 53% of relative activity at pH 10.5. These findings may be promising in the area of biofuels production.

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Immobilization of cellulase onto MnO2 nanoparticles for bioethanol production by enhanced hydrolysis of agricultural waste

Cited by 158 publications

References 34 publications

Bringing plant cell wall‐degrading enzymes into the lignocellulosic biorefinery concept

Bringing plant cell wall‐degrading enzymes into the lignocellulosic biorefinery concept

Synergistic Effect of Two Type Cellulase Immobilized on Chitosan Microparticle as Biocatalyst for Coconut Husk Hydrolysis

Application of ZnO Nanoparticles for Improving the Thermal and pH Stability of Crude Cellulase Obtained from Aspergillus fumigatus AA001

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