Point by point analysis: how ionic liquid affects the enzymatic hydrolysis of native and modified cellulose

Engel, Philip; Mladenov, Radoslav; Wulfhorst, Helene; Jäger, Gernot; Spieß, Antje C.

doi:10.1039/c0gc00135j

Cited by 124 publications

(107 citation statements)

References 61 publications

Supporting

Mentioning

104

Contrasting

Order By: Relevance

“…S10), its activity was measured in the presence of the ionic liquids 1, 3-dimethylimidazolium dimethyl phosphate (DMIM)DMP) and 1-ethyl-3-methylimidazole acetate ((EMIM)OAc), which could potentially be used to pretreat substrates like Miscanthus 17 . The concentrations tested, 25 and 50% (v/v), are well above the expected residual ionic liquid of 10-15% that may be carried over after pretreatment 18 . CMCase activity was demonstrated in zymograms, incubated at 90 °C in 25% (v/v) of either ionic liquid (pH 6.8) (data not shown).…”

Section: Enrichment and Extraction Of Native Proteinmentioning

confidence: 85%

Identification and characterization of a multidomain hyperthermophilic cellulase from an archaeal enrichment

et al. 2011

View full text Add to dashboard Cite

Despite extensive studies on microbial and enzymatic lignocellulose degradation, relatively few Archaea are known to deconstruct crystalline cellulose. Here we describe a consortium of three hyperthermophilic archaea enriched from a continental geothermal source by growth at 90 °C on crystalline cellulose, representing the first instance of Archaea able to deconstruct lignocellulose optimally above 90 °C. Following metagenomic studies on the consortium, a 90 kDa, multidomain cellulase, annotated as a member of the TIm barrel glycosyl hydrolase superfamily, was characterized. The multidomain architecture of this protein is uncommon for hyperthermophilic endoglucanases, and two of the four domains of the enzyme have no characterized homologues. The recombinant enzyme has optimal activity at 109 °C, a halflife of 5 h at 100 °C, and resists denaturation in strong detergents, high-salt concentrations, and ionic liquids. Cellulases active above 100 °C may assist in biofuel production from lignocellulosic feedstocks by hydrolysing cellulose under conditions typically employed in biomass pretreatment.

show abstract

Section: Enrichment and Extraction Of Native Proteinmentioning

confidence: 85%

Identification and characterization of a multidomain hyperthermophilic cellulase from an archaeal enrichment

et al. 2011

View full text Add to dashboard Cite

show abstract

“…It was demonstrated that the activity of cellobiase quickly decreased by 66.5% in aqueous-[EMIM]Ac medium after 6 h incubation. It is presumed that the decrease of enzyme stability in the ionic liquid was attributable to combined effects of high viscosity, salinity, and ionic strength of aqueousILs solvents (Engel et al 2010). Moreover, Kudou et al (2014) reported that the structural change of water clusters induced by [EMIM] + and Ac -resulted in the inhibition of glucosidase.…”

Section: Resultsmentioning

confidence: 99%

In Situ Saccharification of Cellulose using a Cellulase Mixture and Supplemental β-glucosidase in Aqueous-Ionic Liquid Media

Zhu¹,

Guo²,

Guo³

et al. 2016

BioResources

View full text Add to dashboard Cite

In situ enzymatic saccharification is one promising approach to efficiently convert non-food biomass to glucose as a platform chemical. The goal of the present research was to illustrate the catalytic behaviors and deactivation mechanisms of cellulase and cellobiase in an aqueous-ionic liquid (IL) media. The hydrolysis reaction rate was considerably increased because of the increased porosity and reduced crystallinity of the substrate. To lower the inhibitory effect of accumulated cellobiose on cellulase, a multi-enzyme synergetic system was explored. Compared with the single cellulase saccharification, addition of cellobiase resulted in a substantial increase in total reducing sugars (TRS) yield (88.0% vs. 59.1%) and glucose yield (40.6% vs. 28.9%) when the activity unit ratio of cellobiase/cellulase was 0.95. Cellulase showed a higher stability in aqueous 1-ethyl-3-methylimidazolium acetate ([EMIM]Ac) media. However, the activity of cellobiase quickly decreased, by 66.5%, after 6 h of incubation.

show abstract

“…Hydrophilic ILs, such as 1-butyl-3-methylimidazolium chloride and 1-allyl-3-methylimidazolium chloride, are applied to dissolve cellulose. ILs have been tested in combination with cellulases, with one study showing that cellulases retain 30 % activity in the presence of 10 % (v/v) 1,3-dimethylimidazolium dimethylphosphate [105]. Several glycosyl hydrolases have been discovered to be tolerant to IL treatments [106,107].…”

Section: Identification Of Glycosyl Hydrolases Adapted To Pretreatmenmentioning

confidence: 99%

“…Ionic liquid (IL) pretreatment is perhaps the most promising option for combining with saccharification, due to the low temperature requirement and moderate pH range (4.8-6.5) [104,105]. Hydrophilic ILs, such as 1-butyl-3-methylimidazolium chloride and 1-allyl-3-methylimidazolium chloride, are applied to dissolve cellulose.…”

Section: Identification Of Glycosyl Hydrolases Adapted To Pretreatmenmentioning

confidence: 99%

Expression of Glycosyl Hydrolases in Lignocellulosic Feedstock: An Alternative for Affordable Cellulosic Ethanol Production

2016

View full text Add to dashboard Cite

Ethanol produced from lignocellulosic feedstock is a promising alternative to fossil fuels and corn-sourced ethanol. However, it creates unique challenges in terms of requirements for breakdown to fermentable sugars, including the need for pretreatment and enzymatic hydrolysis of structural carbohydrates. Hydrolases from microorganisms are currently utilized for biomass hydrolysis in the production of lignocellulosic ethanol; however, expressing these hydrolases in lignocellulosic feedstock is a favorable alternative, due to the large availability of biomass and the potential for the feedstock to play a dual role as both biomass substrate and enzyme provider. This review summarizes recent achievements in hydrolytic enzyme expression in a variety of model plants and potential feedstocks, including strategies to improve enzyme yield and to prevent deleterious effects on plants hosts. We propose possible scenarios for utilizing enzyme-expressing transgenic feedstock and illustrate the potential benefits of using these crops for ethanol production. Furthermore, challenges are highlighted and potential solutions proposed to move the field forward to cost-comparable lignocellulosic ethanol.

show abstract

Point by point analysis: how ionic liquid affects the enzymatic hydrolysis of native and modified cellulose

Cited by 124 publications

References 61 publications

Identification and characterization of a multidomain hyperthermophilic cellulase from an archaeal enrichment

Identification and characterization of a multidomain hyperthermophilic cellulase from an archaeal enrichment

In Situ Saccharification of Cellulose using a Cellulase Mixture and Supplemental β-glucosidase in Aqueous-Ionic Liquid Media

Expression of Glycosyl Hydrolases in Lignocellulosic Feedstock: An Alternative for Affordable Cellulosic Ethanol Production

Contact Info

Product

Resources

About