Carrier-free co-immobilization of xylanase, cellulase and β-1,3-glucanase as combined cross-linked enzyme aggregates (combi-CLEAs) for one-pot saccharification of sugarcane bagasse

Periyasamy, Karthik; Santhalembi, Laishram; Mortha, Gérard; Aurousseau, M; Sivanesan, S.

doi:10.1039/c6ra00929h

Cited by 46 publications

(32 citation statements)

References 38 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Cellulases have previously been immobilized using the CLEA‐methodology, resulting in re‐usable enzymes with improved temperature, pH and storage stabilities . However, from our experience, the loss in activity throughout repeated use of the cellulase‐CLEAs is an issue that prevents the technology from being industrially applicable.…”

Section: Introductionmentioning

confidence: 99%

“…the cellulase‐CLEA lost 70% of the activity after one use. Several cellulase‐CLEAs have nevertheless been shown to perform better with regard to re‐usability . The limited understanding of the interplay between process parameters and cellulase‐CLEA with high activity throughout repeated use led us to investigate the optimization of the complete process.…”

Section: Introductionmentioning

confidence: 99%

“…Several cellulase-CLEAs have nevertheless been shown to perform better with regard to re-usability. 10,12,13 The limited understanding of the interplay between process parameters and cellulase-CLEA with high activity throughout repeated use led us to investigate the optimization of the complete process. We noted that the type of precipitants used to fabricate CLEA vary greatly among the different reports.…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Cellulase cross-linked enzyme aggregates (CLEA) activities can be modulated and enhanced by precipitant selection

Perzon

Dicko

Çobanoğlu³

et al. 2017

J. Chem. Technol. Biotechnol

View full text Add to dashboard Cite

BACKGROUND Crosslinked enzyme aggregates (CLEA) technology is a rapid and versatile method to produce immobilized enzymes via precipitation and cross‐linking. A direct relationship between CLEA final activity and process parameters is however yet to be clarified. To address the issue, we have used a factorial design to test the formation and optimization of CLEA made from technical grade cellulase (EC 3.2.1.4). Three types of precipitant (ammonium sulfate, polyethylene glycol, tert‐butyl alcohol) were used at varied levels of cross‐linker concentration, cross‐linking time, and temperature. RESULTS It was found that the CLEAs produced with tert‐butyl alcohol were inactive, whereas the polyethylene glycol‐ and ammonium sulfate‐CLEA, recovered 29 and 17% of the free enzyme activity, respectively. Testing for re‐usability, we observed that the polyethylene glycol‐CLEA maintained 40% of the initial activity after four cycles, in contrast the ammonium sulfate‐CLEA only maintained 10% of its activity after one cycle. CONCLUSION Our study highlights the importance of evaluating the effect of the precipitant on final CLEA activity rather than re‐solubilized enzyme activity. It was demonstrated that polyethylene glycol, despite not being able to precipitate the enzymes as readily as ammonium sulfate, resulted in better performing CLEA. © 2016 Society of Chemical Industry

show abstract

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Cellulase cross-linked enzyme aggregates (CLEA) activities can be modulated and enhanced by precipitant selection

Perzon

Dicko

Çobanoğlu³

et al. 2017

J. Chem. Technol. Biotechnol

View full text Add to dashboard Cite

show abstract

“…To be viable in IL media, the cellulase needs to be active and stable in the presence of ILs, and this has been demonstrated with [emim] [OAc]. [136] Hybrid cellulase CLEAs containing as ilica core, prepared by physical adsorption of cellulose CLEAs on ah ighly porous silica support, exhibited twice as much activity as the regular CLEA, and settled better after the hydrolysis, thus facilitating its separation. [136] Hybrid cellulase CLEAs containing as ilica core, prepared by physical adsorption of cellulose CLEAs on ah ighly porous silica support, exhibited twice as much activity as the regular CLEA, and settled better after the hydrolysis, thus facilitating its separation.…”

Section: Pretreatment and Saccharification Of Lignocellulose In Ilsmentioning

confidence: 99%

Biocatalysis and Biomass Conversion in Alternative Reaction Media

Sheldon

2016

Chemistry A European J

154

View full text Add to dashboard Cite

In this Minireview, the state of the art in the use of ionic liquids (ILs) and deep eutectic solvents (DESs) as alternative reaction media for biocatalytic processes and biomass conversion is presented. Initial, proof-of-concept studies, more than a decade ago, involved first-generation ILs based on dialkylimidazolium cations and non-coordinating anions, such as tetrafluoroborate and hexafluorophosphate. More recently, emphasis has switched to more environmentally acceptable second-generation ILs comprising cations, which are designed to be compatible with enzymes and, in many cases are derived from readily available, renewable resources, such as cholinium salts. Protic ionic liquids (PILs), prepared simply by mixing inexpensive amines and acids, are particularly attractive from both an environmental and economic viewpoint. DESs, prepared by mixing inexpensive salts with, preferably renewable, hydrogen-bond donors such as glycerol and amino acids, have also proved suitable reaction media for biocatalytic conversions. A broad range of enzymes can be used in ILs, PILs and DESs, for example lipases in biodiesel production. These neoteric solvents are of particular interest, however, as reaction media for biocatalytic conversions of substrates that have limited solubility in common organic solvents, such as carbohydrates, nucleosides, steroids and polysaccharides. This has culminated in the recent focus of attention on their use as (co)solvents in the pretreatment and saccharification of lignocellulose as the initial steps in the conversion of second-generation renewable biomass into biofuels and chemicals. They can similarly be used as reaction media in subsequent conversions of hexoses and pentoses into platform chemicals.

show abstract

“…[134] Cellulase has also been successfully immobilizeda saCLEA [135] and the use of ac ombi-CLEA containing xylanase, cellulase, and ab eta-1,3-glucanase for the one-pot pretreatment and saccharification of sugarcane bagasse was recently reported. [136] Hybrid cellulase CLEAs containing as ilica core, prepared by physical adsorption of cellulose CLEAs on ah ighly porous silica support, exhibited twice as much activity as the regular CLEA, and settled better after the hydrolysis, thus facilitating its separation. [137] The immobilization of cellulase [138] and xylanase [139] as magneticC LEAs has also been described.…”

Section: Pretreatment and Saccharification Of Lignocellulose In Ils Amentioning

confidence: 99%

ChemInform Abstract: Biocatalysis and Biomass Conversion in Alternative Reaction Media

Sheldon

2016

ChemInform

View full text Add to dashboard Cite

show abstract

Carrier-free co-immobilization of xylanase, cellulase and β-1,3-glucanase as combined cross-linked enzyme aggregates (combi-CLEAs) for one-pot saccharification of sugarcane bagasse

Abstract: Combined cross-linked enzyme aggregates (combi-CLEAs) of xylanase, cellulase and β-1,3-glucanase.

Cited by 46 publications

References 38 publications

Cellulase cross-linked enzyme aggregates (CLEA) activities can be modulated and enhanced by precipitant selection

Cellulase cross-linked enzyme aggregates (CLEA) activities can be modulated and enhanced by precipitant selection

Biocatalysis and Biomass Conversion in Alternative Reaction Media

ChemInform Abstract: Biocatalysis and Biomass Conversion in Alternative Reaction Media

Contact Info

Product

Resources

About