Laccase-mediated delignification and detoxification of lignocellulosic biomass: removing obstacles in energy generation

Malhotra, Manisha; Suman, Sunil Kumar

doi:10.1007/s11356-021-13283-0

Cited by 66 publications

(21 citation statements)

References 134 publications

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“…Several studies have shown the efficient lignin removal, and increase in the reducing sugar content after saccharification in LCB pretreated with fungal laccases [11][12][13][14]. However, there are some challenges to using laccase for LCB delignification, such as high costs for enzymatic production, stability, and low-efficiency process, which makes the area of research still at an early stage in terms of commercial application [15]. Hence, more research is required to overcome the existing limitations in using these biocatalysts on an industrial scale.…”

Section: Introductionmentioning

confidence: 99%

Enzymatic Pretreatment with Laccases from Lentinus sajor-caju Induces Structural Modification in Lignin and Enhances the Digestibility of Tropical Forage Grass (Panicum maximum) Grown under Future Climate Conditions

Freitas

Alnoch

Contato

et al. 2021

IJMS

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Since laccase acts specifically in lignin, the major contributor to biomass recalcitrance, this biocatalyst represents an important alternative to the pretreatment of lignocellulosic biomass. Therefore, this study investigates the laccase pretreatment and climate change effects on the hydrolytic performance of Panicum maximum. Through a Trop-T-FACE system, P. maximum grew under current (Control (C)) and future climate conditions: elevated temperature (2 °C more than the ambient canopy temperature) combined with elevated atmospheric CO2 concentration(600 μmol mol−1), name as eT+eC. Pretreatment using a laccase-rich crude extract from Lentinus sajor caju was optimized through statistical strategies, resulting in an increase in the sugar yield of P. maximum biomass (up to 57%) comparing to non-treated biomass and enabling hydrolysis at higher solid loading, achieving up to 26 g L−1. These increments are related to lignin removal (up to 46%) and lignin hydrophilization catalyzed by laccase. Results from SEM, CLSM, FTIR, and GC-MS supported the laccase-catalyzed lignin removal. Moreover, laccase mitigates climate effects, and no significant differences in hydrolytic potential were found between C and eT+eC groups. This study shows that crude laccase pretreatment is a potential and sustainable method for biorefinery solutions and helped establish P. maximum as a promising energy crop.

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Section: Introductionmentioning

confidence: 99%

Enzymatic Pretreatment with Laccases from Lentinus sajor-caju Induces Structural Modification in Lignin and Enhances the Digestibility of Tropical Forage Grass (Panicum maximum) Grown under Future Climate Conditions

Freitas

Alnoch

Contato

et al. 2021

IJMS

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“…Figure 2B shows the active site structure of laccase, where the laccase-catalyzed reaction is carried out. The laccase active site mainly involves three copper-binding sites (Type 1 (T1), Type 2 (T2), and Type 3 (T3)) [27][28][29]. The T1 active site center exhibits an intense spectrophotometric absorption at wavelengths of 600-610 nm.…”

Section: Laccase Information and Reactionmentioning

confidence: 99%

Recent Advances in the Development of Laccase-Based Biosensors via Nano-Immobilization Techniques

et al. 2022

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Monitoring phenolic compounds is critical in the environmental, food, and medical sectors. Among many recent advanced detection platforms, laccase-based biosensing platforms gave very rapid, effective, online, and in situ sensing of phenolic compounds. In laccase-based biosensors, laccase immobilization techniques have a vital role. However, a detailing of the advancements in laccase immobilization techniques employed in laccase-based biosensors is lacking in the literature. Thus, in this review, we assessed how the nano-immobilization techniques shaped the laccase biosensing platforms. We discussed novel developments in laccase immobilization techniques such as entrapment, adsorption, cross-linking, and covalent over new nanocomposites in laccase biosensors. We made a comprehensive assessment based on the current literature for future perspectives of nano-immobilized laccase biosensors. We found the important key areas toward which future laccase biosensor research seems to be heading. These include 1. A focus on the development of multi-layer laccase over electrode surface, 2. The need to utilize more covalent immobilization routes, as they change the laccase specificity toward phenolic compounds, 3. The advancement in polymeric matrices with electroconductive properties, and 4. novel entrapment techniques like biomineralization using laccase molecules. Thus, in this review, we provided a detailed account of immobilization in laccase biosensors and their feasibility in the future for the development of highly specific laccase biosensors in industrial, medicinal, food, and environmental applications.

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“…Due to their synthetic origin and complex aromatic structures, they are recalcitrant to the conventional microbial degradation or decolorization. LC is able to degrade them but often in combination with the synthetic mediators hydroxybenzotriazole (HBT), ABTS and violuric acid (VA) [8,12,79].…”

Section: Laccase Industrial Applicationmentioning

confidence: 99%

“…Owing to the enzymatic treatment, the shift from energy intensive processes, such as steam or chemical-based ones, to mild and environmentally friendly processes is feasible [8], while valorizing the plant material and applying circularity in food systems. In this regard, plant material deriving from food wastes still represents a poorly exploited resource which may enter new production paths.…”

Section: Introductionmentioning

confidence: 99%

Fungal Laccases: The Forefront of Enzymes for Sustainability

Loi

Glazunova

Федорова

et al. 2021

JoF

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Enzymatic catalysis is one of the main pillars of sustainability for industrial production. Enzyme application allows minimization of the use of toxic solvents and to valorize the agro-industrial residues through reuse. In addition, they are safe and energy efficient. Nonetheless, their use in biotechnological processes is still hindered by the cost, stability, and low rate of recycling and reuse. Among the many industrial enzymes, fungal laccases (LCs) are perfect candidates to serve as a biotechnological tool as they are outstanding, versatile catalytic oxidants, only requiring molecular oxygen to function. LCs are able to degrade phenolic components of lignin, allowing them to efficiently reuse the lignocellulosic biomass for the production of enzymes, bioactive compounds, or clean energy, while minimizing the use of chemicals. Therefore, this review aims to give an overview of fungal LC, a promising green and sustainable enzyme, its mechanism of action, advantages, disadvantages, and solutions for its use as a tool to reduce the environmental and economic impact of industrial processes with a particular insight on the reuse of agro-wastes.

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Laccase-mediated delignification and detoxification of lignocellulosic biomass: removing obstacles in energy generation

Cited by 66 publications

References 134 publications

Enzymatic Pretreatment with Laccases from Lentinus sajor-caju Induces Structural Modification in Lignin and Enhances the Digestibility of Tropical Forage Grass (Panicum maximum) Grown under Future Climate Conditions

Enzymatic Pretreatment with Laccases from Lentinus sajor-caju Induces Structural Modification in Lignin and Enhances the Digestibility of Tropical Forage Grass (Panicum maximum) Grown under Future Climate Conditions

Recent Advances in the Development of Laccase-Based Biosensors via Nano-Immobilization Techniques

Fungal Laccases: The Forefront of Enzymes for Sustainability

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