Lignin-derived inhibition of monocomponent cellulases and a xylanase in the hydrolysis of lignocellulosics

Kellock, Miriam; Rahikainen, Jenni; Marjamaa, Kaisa; Kruus, Kristiina

doi:10.1016/j.biortech.2017.01.072

Cited by 79 publications

(51 citation statements)

References 43 publications

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“…At a pH of 4.8, the adsorption capacity of cellulase onto the EuA and Bsxs lignin was higher than for the BG and xylanase. This result was different from the effects of organosolv-softwood lignin on enzymes reported by Berlin et al (2006) and Kellock et al (2017). Haven and Jørgensen (2013) found that the BG (Novozyme 188) did not adsorb onto the lignin from steampretreated wheat straw.…”

Section: Adsorption Capacity Of Different Enzymes Onto the Lignincontrasting

confidence: 54%

“…Subsequently, the adsorption of cellulase onto lignins has slightly reduction. This probably because the adsorption of cellulase onto lignin effected by the different adsorption behavior of monocomponent of cellulase onto lignin, which needs further investigation (Li et al 2017;Kellock et al 2017 ). From the results shown in Fig.…”

Section: Table 3 Langmuir Adsorption Isotherm Parameters Of Enzyme Amentioning

confidence: 99%

“…The pH value and temperature could influence the adsorption and desorption behaviors of cellulase on lignin by changing the protein properties (Lu et al 2017). It was shown that enzyme properties, surface charge, and surface hydrophobicity could not alone explain the adsorption behaviour of enzyme onto lignins (Kellock et al 2017). The binding mechanism of enzyme onto lignin is complicated.…”

Section: Introductionmentioning

confidence: 99%

“…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. The pH value and temperature could influence the adsorption and desorption behaviors of cellulase on lignin by changing the protein properties (Lu et al 2017).…”

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: Adsorption Capacity Of Different Enzymes Onto the Lignincontrasting

confidence: 54%

Section: Table 3 Langmuir Adsorption Isotherm Parameters Of Enzyme Amentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

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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“…Nonproductive adsorption of cellulases onto lignin is considered an important mechanism behind retardation of enzymatic cellulose degradation in lignocellulose‐based processes (Liu, Sun, Leu, & Chen, ; Saini, Patel, Adsul, & Singhania, ; Sipponen et al, ). Studies have reported adsorption of cellulases onto lignin isolated from various biomass feedstocks and have correlated such adsorption with the observed retardation of enzymatic degradation of pure model cellulose in the presence of the isolated lignin (Kellock, Rahikainen, Marjamaa, & Kruus, ; Rahikainen et al, ; Tu, Pan, & Saddler, ). Hydrophobic interaction (Sammond et al, ; Tu et al, ), electrostatic interaction (Lan, Lou, & Zhu, ; Yarbrough et al, ), and hydrogen bonding (Sewalt, Glasser, & Beauchemin, ; Yu et al, ) have been regarded as the cause of the nonproductive binding of cellulases to lignin.…”

Section: Introductionmentioning

confidence: 99%

Cellulases adsorb reversibly on biomass lignin

Djajadi

Pihlajaniemi

Rahikainen

et al. 2018

Biotech & Bioengineering

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Adsorption of cellulases onto lignin is considered a major factor in retarding enzymatic cellulose degradation of lignocellulosic biomass. However, the adsorption mechanisms and kinetics are not well understood for individual types of cellulases. This study examines the binding affinity, kinetics of adsorption, and competition of four monocomponent cellulases of Trichoderma reesei during adsorption onto lignin. TrCel7A, TrCel6A, TrCel7B, and TrCel5A were radiolabeled for adsorption experiments on lignin‐rich residues (LRRs) isolated from hydrothermally pretreated spruce (L‐HPS) and wheat straw (L‐HPWS), respectively. On the basis of adsorption isotherms fitted to the Langmuir model, the ranking of binding affinities was TrCel5A > TrCel6A > TrCel7B > TrCel7A on both types of LRRs. The enzymes had a higher affinity to the L‐HPS than to the L‐HPWS. Adsorption experiments with dilution after 1 and 24 hr and kinetic modeling were performed to quantify any irreversible binding over time. Models with reversible binding parameters fitted well and can explain the results obtained. The adsorption constants obtained from the reversible models agreed with the fitted Langmuir isotherms and suggested that reversible adsorption–desorption existed at equilibrium. Competitive binding experiments showed that individual types of cellulases competed for binding sites on the lignin and the adsorption data fitted the Langmuir adsorption model. Overall, the data strongly indicate that the adsorption of cellulases onto lignin is reversible and the findings have implications for the development of more efficient cellulose degrading enzymes.

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