The isolation, characterization and effect of lignin isolated from steam pretreated Douglas-fir on the enzymatic hydrolysis of cellulose

Nakagame, Seiji; Chandra, Richard P.; Kadla, John F.; Saddler, Jack N.

doi:10.1016/j.biortech.2010.12.082

Cited by 212 publications

(178 citation statements)

References 30 publications

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“…This implied that the hydrophobicity was the main factor that influenced the adsorption of cellulase onto the lignin samples. The same conclusion was reached in previous studies (Gessner et al 2000;Nakagame et al 2010Nakagame et al , 2011aRahikainen et al 2013). The surface charges of the Eusxs, Bsxs, EuA, and BA were -0.78 mmol/g, -1.47 mmol/g, -1.0 mmol/g, and -0.85 mmol/g, respectively.…”

Section: Surface Charge and Hydrophobicity Of The Ligninsupporting

confidence: 72%

“…It is well known that hydrophobic interactions play a greater role in the adsorption of cellulases and related enzymes onto lignocellulose (Palonen et al 2004;Berlin et al 2005a,b). Hydrogen bonding or electrostatic interaction are also responsible for enzyme adsorption onto lignin (Brash and Horbett 1995;Nakagame et al 2011aNakagame et al , 2011bRahikainen et al 2013). Kellock et al (2017) indicated that lignins isolated from steam pretreated spruce (SPS) is more inhibitory to xylanase, β-glucosidase, and individual components of cellulase such as CBH and endoglucanases (EG) than wheat straw (SPWS) lignin.…”

Section: Introductionmentioning

confidence: 99%

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Study of the Difference between Enzyme Adsorption onto Hydrotropic and Alkali Lignin Separated from Eucalyptus and Bamboo

Mou¹,

Wu²,

He³

et al. 2018

BioResources

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Enzymatic hydrolysis of lignocellulosic biomass is the key step for controlling the cost of bioethanol production. However, the non-productive adsorption of cellulase onto lignin in biomass severely hampers the enzyme activity and hydrolysis efficiency. Thus, understanding the adsorption mechanism of cellulase onto lignin is critical for the development of enzyme mixtures and enzymatic hydrolysis. In this investigation, cellulase, β-glucosidase (BG), and xylanase adsorption onto lignin from eucalyptus and bamboo, extracted by alkali and hydrotropic techniques, were compared. The physico-chemical properties of the four types of isolated lignin were detected. Langmuir isotherms were used to interpret the cellulase adsorption kinetics of the lignin. The hydrophobicity was found to be the major factor that affected the cellulase adsorption affinity of lignin. The surface charge was important for the adsorption of BG and xylanase onto the lignin. A comparison was made between hydrotropic and alkali lignin, and the hydrotropic lignin from eucalyptus had the highest cellulase adsorption capacity and lowest BG and xylanase adsorption capacities.

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Section: Surface Charge and Hydrophobicity Of The Ligninsupporting

confidence: 72%

Section: Introductionmentioning

confidence: 99%

Study of the Difference between Enzyme Adsorption onto Hydrotropic and Alkali Lignin Separated from Eucalyptus and Bamboo

Mou¹,

Wu²,

He³

et al. 2018

BioResources

View full text Add to dashboard Cite

show abstract

“…For example, recent studies have shown that softwood chips that had been steam-pretreated at higher severities displayed higher enzymatic digestibility despite the relative increase in the lignin content in the water-insoluble pretreated material (Ewanick et al 2007;Nakagame et al 2011b), suggesting that the lignin content itself is not the major factor limiting efficient enzymatic hydrolysis at low enzyme dosage. Further studies to elucidate the exact mechanisms (chemical bonds being cleaved, change in lignin hydrophobicity, formation of new bonds, lignin redistribution) underlying the capability of brown-rot fungi to overcome the lignin barrier without removing it and the impact of specific modifications on enzyme access to the polysaccharides can provide new insights on how to improve biomass pretreatment technologies.…”

Section: Lignin Rearrangement During Brown-rot Decaymentioning

confidence: 97%

Peculiarities of brown-rot fungi and biochemical Fenton reaction with regard to their potential as a model for bioprocessing biomass

Arantes

Jellison

Goodell

2012

Appl Microbiol Biotechnol

287

214

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This work reviews the brown-rot fungal biochemical mechanism involved in the biodegradation of lignified plant cell walls. This mechanism has been acquired as an apparent alternative to the energetically expensive apparatus of lignocellulose breakdown employed by white-rot fungi. The mechanism relies, at least in the incipient stage of decay, on the oxidative cleavage of glycosidic bonds in cellulose and hemicellulose and the oxidative modification and arrangement of lignin upon attack by highly destructive oxygen reactive species such as the hydroxyl radical generated non-enzymatically via Fenton chemistry [Formula: see text]. Modifications in the lignocellulose macrocomponents associated with this non-enzymatic attack are believed to aid in the selective, near-complete removal of polysaccharides by an incomplete cellulase suite and without causing substantial lignin removal. Utilization of this process could provide the key to making the production of biofuel and renewable chemicals from lignocellulose biomass more cost-effective and energy efficient. This review highlights the unique features of the brown-rot fungal non-enzymatic, mediated Fenton reaction mechanism, the modifications to the major plant cell wall macrocomponents, and the implications and opportunities for biomass processing for biofuels and chemicals.

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“…The role of electrostatic interactions was investigated by comparing enzyme adsorption and protein pI values, but the results are inconclusive because both positively and negatively charged proteins were found to adsorb to lignin (4). The role of the carbohydrate-binding module (CBM), 3 found in many cellulase enzymes and important for targeting enzyme to substrate, was shown to enhance enzyme adsorption to lignin (5).…”

mentioning

confidence: 99%

Predicting Enzyme Adsorption to Lignin Films by Calculating Enzyme Surface Hydrophobicity

Sammond

Yarbrough

Mansfield

et al. 2014

Journal of Biological Chemistry

127

115

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Background:Lignin is a plant cell wall polymer that inhibits enzymatic saccharification of polysaccharides for the production of biofuel. Results: The adsorption of enzymes to lignin surfaces correlates to solvent-exposed hydrophobic clusters. Conclusion: Hydrophobicity, not surface charge, identifies proteins that preferentially adsorb to lignin. Significance: The method could be used to design improved cellulase cocktails to lower the cost of biofuel production.

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The isolation, characterization and effect of lignin isolated from steam pretreated Douglas-fir on the enzymatic hydrolysis of cellulose

Cited by 212 publications

References 30 publications

Study of the Difference between Enzyme Adsorption onto Hydrotropic and Alkali Lignin Separated from Eucalyptus and Bamboo

Study of the Difference between Enzyme Adsorption onto Hydrotropic and Alkali Lignin Separated from Eucalyptus and Bamboo

Peculiarities of brown-rot fungi and biochemical Fenton reaction with regard to their potential as a model for bioprocessing biomass

Predicting Enzyme Adsorption to Lignin Films by Calculating Enzyme Surface Hydrophobicity

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