Microbial cellulases – An update towards its surface chemistry, genetic engineering and recovery for its biotechnological potential

Paul, Manish; Mohapatra, Sushanta Kumar; Mohapatra, Pradeep Kumar Das; Thatoi, Hrudayanath

doi:10.1016/j.biortech.2021.125710

Cited by 26 publications

(12 citation statements)

References 140 publications

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“…2 Prediction of signal peptides based on SignalP analysis. 3 We only considered proteins identified by at least two unique peptides. 4 Secretome analysis based on spectral counting.…”

Section: Figuresmentioning

confidence: 99%

“…Cellulases have several industrial applications (e.g., in the paper, food, pharmaceutical, and chemical industries) representing 10% of the enzymes market valued at USD 10.7 billion in 2020, and this market is expected to grow to USD 17.88 billion by 2027 [2]. However, the most significant application lies in commercial enzymatic cocktails used in lignocellulose-based biorefineries [3][4][5].…”

Section: Introductionmentioning

confidence: 99%

“…Fungi are well-known for their capacity to secrete a broad range of cellulases with distinct proprieties and high titers – which are desired for the large application and demand for biotechnological purposes [3][4] [6]. Trichoderma reesei is the main filamentous fungi (hereafter called fungi) widely used to produce cellulases in industry owing to the high capacity of secretion – reaching up 100 g/l of cellulase [7][6] [5].…”

Section: Introductionmentioning

confidence: 99%

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An insight into cellulolytic capacity of the Trichoderma harzianum P49P11 revealed by omics approaches

Codima

Tomazetto

Persinoti

et al. 2022

Preprint

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Cellulases are a group of enzymes with several applications in biofuel production, and the paper, food, pharmaceutical, and chemical industries. Trichoderma harzianum P49P11 secrete all cellulases with high efficiency, representing an alternative to the current filamentous fungi in biotechnological industries. In this study, the cellulolytic mechanisms employed by the strain P49P11 to degrade crystalline cellulose in batch fermentation culture mode were elucidated by combining genome and secretome analysis. The strain P49P11 encodes nineteen cellulase genes from five different CAZyme families (GH5, GH6, GH7, GH12, and GH45), followed by several enzyme families for hemicellulose, pectin, and alpha- and beta-glucans degradation. The diverse CAZymes were also observed in the secretome, including cellulases, hemicellulases, and glucanases. In addition, beta-glucosidases and xylanase activities detected during the fermentation process validated our secretome analysis. Taken together, our results revealed all enzymatic machinery used by the T. harzianum P49P11 to degrade cellulose in batch fermentation mode.

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“…2 Prediction of signal peptides based on SignalP analysis. 3 We only considered proteins identified by at least two unique peptides. 4 Secretome analysis based on spectral counting.…”

Section: Figuresmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

An insight into cellulolytic capacity of the Trichoderma harzianum P49P11 revealed by omics approaches

Codima

Tomazetto

Persinoti

et al. 2022

Preprint

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“…The presence of lignin often inhibits the cellulose hydrolysis so special efforts are undertaken to overcome this problem. Besides stabilization and the possibility of catalyst reuse, the cellulase immobilization on nanostructured supports may reduce the cellulase surface charge, thus diminishing its non-specific binding to lignin and increasing the interactions with cellulose [ 21 ]. Often biomass waste first requires delignification with another enzymatic catalyst before cellulase can efficiently hydrolyze cellulose [ 22 ] or co-immobilization of several enzymes on the same support is implemented, which is a more prominent trend [ 23 , 24 , 25 , 26 , 27 , 28 ].…”

Section: Introductionmentioning

confidence: 99%

Cellulase Immobilization on Nanostructured Supports for Biomass Waste Processing

2022

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Nanobiocatalysts, i.e., enzymes immobilized on nanostructured supports, received considerable attention because they are potential remedies to overcome shortcomings of traditional biocatalysts, such as low efficiency of mass transfer, instability during catalytic reactions, and possible deactivation. In this short review, we will analyze major aspects of immobilization of cellulase—an enzyme for cellulosic biomass waste processing—on nanostructured supports. Such supports provide high surface areas, increased enzyme loading, and a beneficial environment to enhance cellulase performance and its stability, leading to nanobiocatalysts for obtaining biofuels and value-added chemicals. Here, we will discuss such nanostructured supports as carbon nanotubes, polymer nanoparticles (NPs), nanohydrogels, nanofibers, silica NPs, hierarchical porous materials, magnetic NPs and their nanohybrids, based on publications of the last five years. The use of magnetic NPs is especially favorable due to easy separation and the nanobiocatalyst recovery for a repeated use. This review will discuss methods for cellulase immobilization, morphology of nanostructured supports, multienzyme systems as well as factors influencing the enzyme activity to achieve the highest conversion of cellulosic biowaste into fermentable sugars. We believe this review will allow for an enhanced understanding of such nanobiocatalysts and processes, allowing for the best solutions to major problems of sustainable biorefinery.

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“…Fungi, as the primary producers of cellulose-degrading enzymes, have received most of the attention regarding biotechnological applications. However, as previously reported, the lack of endogenous β-glucosidase is always the fatal defect of current industrial microorganisms used for the enzymatic degradation of cellulose, such as Trichoderma reesei [ 5 , 6 ]. This is because the end-product inhibition of CBHs by cellobiose, which is the natural substrate of β-glucosidase, can seriously reduce the overall conversion rate of cellulose into glucose [ 7 , 8 ].…”

Section: Introductionmentioning

confidence: 99%

Improving the Substrate Affinity and Catalytic Efficiency of β-Glucosidase Bgl3A from Talaromyces leycettanus JCM12802 by Rational Design

2021

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Improving the substrate affinity and catalytic efficiency of β-glucosidase is necessary for better performance in the enzymatic saccharification of cellulosic biomass because of its ability to prevent cellobiose inhibition on cellulases. Bgl3A from Talaromyces leycettanus JCM12802, identified in our previous work, was considered a suitable candidate enzyme for efficient cellulose saccharification with higher catalytic efficiency on the natural substrate cellobiose compared with other β-glucosidase but showed insufficient substrate affinity. In this work, hydrophobic stacking interaction and hydrogen-bonding networks in the active center of Bgl3A were analyzed and rationally designed to strengthen substrate binding. Three vital residues, Met36, Phe66, and Glu168, which were supposed to influence substrate binding by stabilizing adjacent binding site, were chosen for mutagenesis. The results indicated that strengthening the hydrophobic interaction between stacking aromatic residue and the substrate, and stabilizing the hydrogen-bonding networks in the binding pocket could contribute to the stabilized substrate combination. Four dominant mutants, M36E, M36N, F66Y, and E168Q with significantly lower Km values and 1.4–2.3-fold catalytic efficiencies, were obtained. These findings may provide a valuable reference for the design of other β-glucosidases and even glycoside hydrolases.

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Microbial cellulases – An update towards its surface chemistry, genetic engineering and recovery for its biotechnological potential

Cited by 26 publications

References 140 publications

An insight into cellulolytic capacity of the Trichoderma harzianum P49P11 revealed by omics approaches

An insight into cellulolytic capacity of the Trichoderma harzianum P49P11 revealed by omics approaches

Cellulase Immobilization on Nanostructured Supports for Biomass Waste Processing

Improving the Substrate Affinity and Catalytic Efficiency of β-Glucosidase Bgl3A from Talaromyces leycettanus JCM12802 by Rational Design

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