Incorporating Lignin into Polyethylene Glycol Enhanced Its Performance for Promoting Enzymatic Hydrolysis of Hardwood

Lai, Chenhuan; Jia, Yuan; Yang, Chundong; Chen, Liwei; Shi, Hao; Yong, Qiang

doi:10.1021/acssuschemeng.9b05724

Cited by 47 publications

(14 citation statements)

References 31 publications

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“…This provides some evidences that PEG can be adsorbed on the surface of residual lignin in substrate, albeit this adsorption is not strong. The authors in other studies have similar ndings [39].…”

Section: Interaction Between Peg and Cellulasesupporting

confidence: 69%

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Comparison of the Interaction Modes Between Cellulase and Bovine Serum Albumin /Lignosulfonate /Polyethylene Glycol in Promoting Lignocellulose Saccharification

Wang

Lan

Guo

et al. 2021

Preprint

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Background: Bovine serum albumin (BSA), polyethylene glycol (PEG) and lignosulfonate (LS) have been extensively employed as synergistic agents in lignocellulose saccharification, albeit it has not been fully understood how they interact with enzymes from the perspectives of molecular interactions. Herein, we attempted to unveil the promotion mechanisms of BSA, PEG and LS for lignocellulose saccharification from the perspective of their respective interaction with cellulase using Quartz Crystal Microbalance with Dissipation monitoring (QCM-D), Surface Plasmon Resonance (SPR), and Small Angle X-ray Scattering (SAXS) to investigate their respective interaction and the complex formation. In the meanwhile, we compared the effects of adding these additives into the enzymatic hydrolysis of pure cellulose (Avicel) and green liquor-pretreated lignocellulose (GL).Results: The results showed that BSA and LS could bind to cellulase to form complexes, whereas PEG did not. However, PEG had a high affinity to lignin or lignin derivatives. In term for Avicel and GL substrates, the results showed that BSA and PEG promoted the enzymatic hydrolysis of both substrates, while LS had a promoting effect for GL only and inhibited some extent for Avicel. Conclusions: This study showed that synergistic agents of LS, BSA, and PEG have different interaction modes with cellulase. BSA and LS form complexes with cellulase and the formed complexes prevent from nonproductive binding by residue lignin; whereas PEG prevents from nonproductive binding by forming a thin layer on residue lignin which actually serve as steric hindrance. This investigation will help us to understand the sophisticated interactions among the components in the complicated enzymatic system, especially the interactions between enzymes and synergistic agents. It will be helpful in the design and utilization of synergistic additives in the lignocellulose biorefinery process as well.

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Section: Interaction Between Peg and Cellulasesupporting

confidence: 69%

“…On the other hand, PEG can adsorb on substrate lignin, preventing cellulase from adsorbing on substrate lignin nonproductively. This hypothesis was brought up by Lei et al [39]. that PEG forms a physical barrier to reduce the adsorption of cellulase onto substrate lignin.…”

Section: Proposed Interaction Mechanismsmentioning

confidence: 99%

Comparison of the Interaction Modes Between Cellulase and Bovine Serum Albumin /Lignosulfonate /Polyethylene Glycol in Promoting Lignocellulose Saccharification

Wang

Lan

Guo

et al. 2021

Preprint

View full text Add to dashboard Cite

show abstract

Section: Interaction Between Peg and Cellulasesupporting

confidence: 69%

“…On the other hand, PEG can adsorb on substrate lignin, preventing cellulase from adsorbing on substrate lignin nonproductively. This hypothesis was brought up by Lei et al [38]. that PEG forms a physical barrier to reduce the adsorption of cellulase onto substrate lignin.…”

Section: Proposed Interaction Modesmentioning

confidence: 99%

Exploring the Promoting Mechanisms of Bovine Serum Albumin, Lignosulfonate, Polyethylene Glycol for Lignocellulose Saccharification from Perspective of Molecular Interactions with Cellulase

Wang

Liu

et al. 2021

Preprint

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Background: Bovine serum albumin (BSA), polyethylene glycol (PEG) and lignosulfonate (LS) have been extensively employed as synergistic agents in lignocellulose saccharification. Nevertheless, the promoting mechanisms have not been fully understood and there are a number of controversial opinions existed. All attention has been paid to the interactions between respective additive and substrate. However, rarely attention has been paid to the interactions between additives and cellulase. The interaction between respective additive and cellulase is actually more important since cellulase interacts with the additives before it contacts with substrate.Results: This investigation showed that BSA and LS could bind to cellulase to form complexes, whereas PEG did not. However, PEG had a high affinity to lignin or lignin derivatives. The complexes of Cell-BSA consisted of one BSA and four cellulase molecules; while the complexes of Cell-LS were composed of one cellulase and four LS molecules in the testing conditions. Regarding to the enzymatic hydrolytic efficiency for Avicel and lignocellulose substrates, the results showed that BSA and PEG promoted the enzymatic hydrolysis for both substrates, while LS had a promoting effect for lignocellulose only and inhibited some extent for Avicel. Conclusions: This study showed that synergistic agents of LS, BSA, and PEG have different interaction modes with cellulase. BSA and LS can form complexes with cellulase and the formed complexes prevent them from nonproductive binding by residue lignin; what’s more, the cellulase-BSA complexes improve the hydrolytic capability of pristine enzyme whereas cellulase-LS complexes reduce. The promoting mechanism of PEG has to be attributed to two aspects: one is to prevent cellulase from nonproductive binding to residue lignin by forming a thin layer that actually serves as steric hindrance on residue lignin; the other is the structure change of substrate induced by PEG addition. This investigation will help us to understand the sophisticated interactions among the components in the complicated enzymatic system, especially the interactions between enzymes and synergistic agents. It will be helpful in the design and utilization of synergistic additives in the lignocellulose biorefinery process as well.

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“…Some surfactants were generally used to enhance the enzymatic hydrolysis of lignocellulose, as these surfactants can prevent the thermal inactivation of enzymes and reduce the nonproductive adsorption. ,− Tween 80 has been reported as one of the most widely used surfactants to improve the hydrolysis efficiency and can reduce the cellulases adsorption on lignin . Hence, it was selected to investigate the effect of nonionic surfactants on the Bs EXLX1 adsorption.…”

Section: Resultsmentioning

confidence: 99%

Real-Time QCM-D Monitoring of the Adsorption–Desorption of Expansin on Lignin

Cui

Duan

et al. 2020

Langmuir

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Expansin has nonhydrolytic disruptive activity and synergistically acts with cellulases to enhance the hydrolysis of cellulose. The adsorption–desorption of expansin on noncellulosic lignin can greatly affect the action of expansin on lignocellulose. In this study, three lignins with different sources (kraft lignin (KL), sodium lignin sulfonate (SLS), and enzymatic hydrolysis lignin (EHL)) were selected as the substrates. The real-time adsorption–desorption of Bacillus subtilis expansin (BsEXLX1) on lignins was monitored using quartz crystal microgravimetry with dissipation (QCM-D). The effects of temperature and Tween 80 on the adsorption–desorption behaviors were also investigated. The results show that BsEXLX1 exhibited high binding ability on lignin and achieved maximum adsorption of 283.2, 273.8, and 266.9 ng cm–2 at 25 °C on KL, SLS, and EHL, respectively. The maximum adsorption decreased to 148.2–192.8 ng cm–2 when the temperature increased from 25 to 45 °C. Moreover, Tween 80 competitively bound to lignin and significantly prevented expansin adsorption. After irreversible adsorption of Tween 80, the maximum adsorption of BsEXLX1 greatly decreased to 33.3, 37.2, and 10.3 ng cm–2 at 25 °C on KL, SLS, and EHL, respectively. Finally, a kinetic model was developed to analyze the adsorption–desorption process of BsEXLX1. BsEXLX1 has a higher adsorption rate constant (k A) and a lower desorption rate constant (k D) on KL than on SLS and EHL. The findings of this study provide useful insights into the adsorption–desorption of expansin on lignin.

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Incorporating Lignin into Polyethylene Glycol Enhanced Its Performance for Promoting Enzymatic Hydrolysis of Hardwood

Cited by 47 publications

References 31 publications

Comparison of the Interaction Modes Between Cellulase and Bovine Serum Albumin /Lignosulfonate /Polyethylene Glycol in Promoting Lignocellulose Saccharification

Comparison of the Interaction Modes Between Cellulase and Bovine Serum Albumin /Lignosulfonate /Polyethylene Glycol in Promoting Lignocellulose Saccharification

Exploring the Promoting Mechanisms of Bovine Serum Albumin, Lignosulfonate, Polyethylene Glycol for Lignocellulose Saccharification from Perspective of Molecular Interactions with Cellulase

Real-Time QCM-D Monitoring of the Adsorption–Desorption of Expansin on Lignin

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