Carbohydrate-Binding Modules of Potential Resources: Occurrence in Nature, Function, and Application in Fiber Recognition and Treatment

Liu, Yena; Wang, Peipei; Tian, Jing; Seidi, Farzad; Guo, Jiaqi; Zhu, Wenshuai; Xiao, Huining; Song, Junlong

doi:10.3390/polym14091806

Cited by 14 publications

(8 citation statements)

References 139 publications

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“…CEs catalyze the de-O or de-N-acylation of substituted saccharides to remove esters from substituted saccharides [ 54 ]. CBMs are noncatalytic modules promoting the association of all other CAZymes with the substrates [ 55 ]. Taken together, these CAZymes in strain DH15 are likely to contribute to polysaccharide degradation and resource utilization within Microcystis colonies for its own growth and survival.…”

Section: Resultsmentioning

confidence: 99%

Genomic Insights into Paucibacter aquatile DH15, a Cyanobactericidal Bacterium, and Comparative Genomics of the Genus Paucibacter

Le,

Ko,

et al. 2023

J. Microbiol. Biotechnol.

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Microcystisblooms threaten ecosystem function and cause substantial economic losses. Microorganismbased methods, mainly using cyanobactericidal bacteria, are considered one of the most ecologically sound methods to control Microcystis blooms. This study focused on gaining genomic insights into Paucibacter aquatile DH15 that exhibited excellent cyanobactericidal effects against Microcystis. Additionally, a pan-genome analysis of the genus Paucibacter was conducted to enhance our understanding of the ecophysiological significance of this genus. Based on phylogenomic analyses, strain DH15 was classified as a member of the species Paucibacter aquatile. The genome analysis supported that strain DH15 can effectively destroy Microcystis, possibly due to the specific genes involved in the flagellar synthesis, cell wall degradation, and the production of cyanobactericidal compounds. The pan-genome analysis revealed the diversity and adaptability of the genus Paucibacter, highlighting its potential to absorb external genetic elements. Paucibacter species were anticipated to play a vital role in the ecosystem by potentially providing essential nutrients, such as vitamins B 7 , B 12 , and heme, to auxotrophic microbial groups. Overall, our findings contribute to understanding the molecular mechanisms underlying the action of cyanobactericidal bacteria against Microcystis and shed light on the ecological significance of the genus Paucibacter.

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Section: Resultsmentioning

confidence: 99%

Genomic Insights into Paucibacter aquatile DH15, a Cyanobactericidal Bacterium, and Comparative Genomics of the Genus Paucibacter

Le,

Ko,

et al. 2023

J. Microbiol. Biotechnol.

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“…Laccases are multicopper oxidases capable of oxidizing a variety of phenolic and non-phenolic substrates. At the same time, CBMs are non-catalytic domains that can specifically bind to carbohydrates, facilitating the enzyme’s attachment to the complex structure of lignocellulosic biomass or synthetic polymers [ 32 , 33 , 34 , 35 ]. The potential benefit of fussing a CBM onto a laccase was also emphasized in this study, with wildtype Fom_lac catalyzed oxidation of lignin through long-distance electron transfer through an aqueous solution from lignin to mediator ( Figure 7 A).…”

Section: Discussionmentioning

confidence: 99%

An Engineered Laccase from Fomitiporia mediterranea Accelerates Lignocellulose Degradation

Pham,

Deng,

Choudhary

et al. 2024

Biomolecules

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Laccases from white-rot fungi catalyze lignin depolymerization, a critical first step to upgrading lignin to valuable biodiesel fuels and chemicals. In this study, a wildtype laccase from the basidiomycete Fomitiporia mediterranea (Fom_lac) and a variant engineered to have a carbohydrate-binding module (Fom_CBM) were studied for their ability to catalyze cleavage of β-O-4′ ether and C–C bonds in phenolic and non-phenolic lignin dimers using a nanostructure-initiator mass spectrometry-based assay. Fom_lac and Fom_CBM catalyze β-O-4′ ether and C–C bond breaking, with higher activity under acidic conditions (pH < 6). The potential of Fom_lac and Fom_CBM to enhance saccharification yields from untreated and ionic liquid pretreated pine was also investigated. Adding Fom_CBM to mixtures of cellulases and hemicellulases improved sugar yields by 140% on untreated pine and 32% on cholinium lysinate pretreated pine when compared to the inclusion of Fom_lac to the same mixtures. Adding either Fom_lac or Fom_CBM to mixtures of cellulases and hemicellulases effectively accelerates enzymatic hydrolysis, demonstrating its potential applications for lignocellulose valorization. We postulate that additional increases in sugar yields for the Fom_CBM enzyme mixtures were due to Fom_CBM being brought more proximal to lignin through binding to either cellulose or lignin itself.

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“…Based on the topology of the ligand-binding site, CBMs can be classified into types A, B ( endo -type), or C ( exo -type) ( Gilbert, Knox, and Boraston, 2013 ). Type A CBMs display a high binding capacity to crystalline polysaccharides (e.g., cellulose and chitin) through hydrophobic interactions regulated by conserved aromatic triplets and are therefore considered potential candidates for PET-binding peptides ( Zhang et al, 2013 ; Y. Liu, Wang, et al, 2022b ).…”

Section: Strategy For Improved Pet-biodegradationmentioning

confidence: 99%

Current advances in the structural biology and molecular engineering of PETase

Liu,

Wang,

Yang

et al. 2023

Front. Bioeng. Biotechnol.

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Poly(ethylene terephthalate) (PET) is a highly useful synthetic polyester plastic that is widely used in daily life. However, the increase in postconsumer PET as plastic waste that is recalcitrant to biodegradation in landfills and the natural environment has raised worldwide concern. Currently, traditional PET recycling processes with thermomechanical or chemical methods also result in the deterioration of the mechanical properties of PET. Therefore, it is urgent to develop more efficient and green strategies to address this problem. Recently, a novel mesophilic PET-degrading enzyme (IsPETase) from Ideonella sakaiensis was found to streamline PET biodegradation at 30°C, albeit with a lower PET-degrading activity than chitinase or chitinase-like PET-degrading enzymes. Consequently, the molecular engineering of more efficient PETases is still required for further industrial applications. This review details current knowledge on IsPETase, MHETase, and IsPETase-like hydrolases, including the structures, ligand‒protein interactions, and rational protein engineering for improved PET-degrading performance. In particular, applications of the engineered catalysts are highlighted, including metabolic engineering of the cell factories, enzyme immobilization or cell surface display. The information is expected to provide novel insights for the biodegradation of complex polymers.

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Carbohydrate-Binding Modules of Potential Resources: Occurrence in Nature, Function, and Application in Fiber Recognition and Treatment

Cited by 14 publications

References 139 publications

Genomic Insights into Paucibacter aquatile DH15, a Cyanobactericidal Bacterium, and Comparative Genomics of the Genus Paucibacter

Genomic Insights into Paucibacter aquatile DH15, a Cyanobactericidal Bacterium, and Comparative Genomics of the Genus Paucibacter

An Engineered Laccase from Fomitiporia mediterranea Accelerates Lignocellulose Degradation

Current advances in the structural biology and molecular engineering of PETase

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