Construction and screening of metagenomic library derived from soil for β-1, 4-endoglucanase gene

Pandey, Sangeeta; Gulati, Sneha; Goyal, Etika; Singh, Surender; Kumar, Kanika; Nain, Lata; Saxena, Anil Kumar

doi:10.1016/j.bcab.2016.01.008

Cited by 9 publications

(4 citation statements)

References 43 publications

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“…The use of function-based metagenomic approaches to search for novel lignocellulosic enzymes have led to the discovery of novel b-galactosidases/a-arabinopyranosidases (Beloqui et al 2010), cellulases Kim et al 2008;Lopes et al 2015;Pandey et al 2016), xylanases (Hu et al 2008;Kanokratana et al 2015), xylose isomerases (Parachin and Gorwa-Grauslund 2011), b-xylosidase/a-arabinofuranosidase (Matsuzawa et al 2015) and b-glucosidases (Del Pozo et al 2012;Biver et al 2014), supporting this strategy as a powerful activity-based screening tool to identify entirely new classes of gene sequences encoding new or known functions (Handelsman 2004;Parachin and Gorwa-Grauslund 2011). Several sources of potential cellullose-and hemicellulosedepleting microbial communities are being used for metagenomic analysis.…”

Section: Discussionmentioning

confidence: 99%

Applying functional metagenomics to search for novel lignocellulosic enzymes in a microbial consortium derived from a thermophilic composting phase of sugarcane bagasse and cow manure

Colombo

Oliveira

Carneiro

et al. 2016

Antonie van Leeuwenhoek

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Environments where lignocellulosic biomass is naturally decomposed are sources for discovery of new hydrolytic enzymes that can reduce the high cost of enzymatic cocktails for second-generation ethanol production. Metagenomic analysis was applied to discover genes coding carbohydrate-depleting enzymes from a microbial laboratory subculture using a mix of sugarcane bagasse and cow manure in the thermophilic composting phase. From a fosmid library, 182 clones had the ability to hydrolyse carbohydrate. Sequencing of 30 fosmids resulted in 12 contigs encoding 34 putative carbohydrate-active enzymes belonging to 17 glycosyl hydrolase (GH) families. One third of the putative proteins belong to the GH3 family, which includes β-glucosidase enzymes known to be important in the cellulose-deconstruction process but present with low activity in commercial enzyme preparations. Phylogenetic analysis of the amino acid sequences of seven selected proteins, including three β-glucosidases, showed low relatedness with protein sequences deposited in databases. These findings highlight microbial consortia obtained from a mixture of decomposing biomass residues, such as sugar cane bagasse and cow manure, as a rich resource of novel enzymes potentially useful in biotechnology for saccharification of lignocellulosic substrate.

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Section: Discussionmentioning

confidence: 99%

Applying functional metagenomics to search for novel lignocellulosic enzymes in a microbial consortium derived from a thermophilic composting phase of sugarcane bagasse and cow manure

Colombo

Oliveira

Carneiro

et al. 2016

Antonie van Leeuwenhoek

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“…Cellulases have a wide range of applications in various industries such as textile, laundry, pulp and paper, food and feed products, as well as in bioethanol production (Bhat, 2000;Dave et al, 2013;Silva et al, 2013). Cellulases have great potential in the saccharification of lignocellulosics into fermentable sugars which can be used for the production of bioethanol (Boggione et al, 2016;Maki et al, 2009;Pandey et al, 2016). It is critical to consider the conditions that contribute to enzyme stability for the design and development of a biotechnological process where the function of the enzyme is relevant.…”

Section: Introductionmentioning

confidence: 99%

Single method of purification for endoglucanase from Aspergillus niger by polyelectrolyte precipitation

Boggione

Becher

Farruggia

2016

Biocatalysis and Agricultural Biotechnology

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The precipitation of endoglucanase from Aspergillus niger with synthetic and natural electrically charged polymers-poly vinyl sulfonate (PVS) and chitosan (CHS)-was characterized and applied to a simple method of purification of an enzymatic extract obtained from fungal culture under solid-state fermentation (SSF). The kinetics of complex formation was determined. The results of the kinetic profile obtained for CHS and PVS indicated an exothermic mechanism for the formation of the non-soluble complex. CHS exhibited a marked stabilizing effect on endoglucanase. The enzyme precipitated successfully with both polymers. The precipitation method applied to commercial endoglucanase and the fungal extract showed similar patterns with high purification factors. The recovery of the activity in the re-dissolved precipitate from the fungal extract was close to 40% at pH 5.3 using PVS (1% w/w) as precipitating agent and the purification factor was near 9. The purification factor of endoglucanase in the precipitate of the enzymatic extract from SSF with CHS (0.05% w/v) was around 7. These parameters make this precipitation method appropriate to be included in the last stages of a downstream process, with advantages such as simplicity, scalability and ability to concentrate and stabilize the enzyme.

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“…Metagenomics allows retrieval of genes encoding biocatalysts from culturable as well as non-cultural microbes. Many cellulase genes have been identified from environmental metagenomes ( Garg et al, 2016 ; Matsuzawa and Yaoi, 2016 ; Pandey et al, 2016 ; Zhou et al, 2016 ), hindgut contents of termites ( Duan et al, 2017 ; Tsegaye et al, 2018 ), rumen ( Ko et al, 2015 ; Song et al, 2016 ; Do et al, 2018 ), compost ( Lemos et al, 2017 ; Lee et al, 2018 ), oil reservoirs ( Lewin et al, 2017 ), and sludge from a biogas reactor ( Wei et al, 2015 ). Very few of them have, however, been characterized adequately ( Garg et al, 2016 ; Song et al, 2016 ; Lee et al, 2018 ).…”

Section: Cellulases Retrieved From Metagenomesmentioning

confidence: 99%

Progress in Ameliorating Beneficial Characteristics of Microbial Cellulases by Genetic Engineering Approaches for Cellulose Saccharification

2020

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Lignocellulosic biomass is a renewable and sustainable energy source. Cellulases are the enzymes that cleave β-1, 4-glycosidic linkages in cellulose to liberate sugars that can be fermented to ethanol, butanol, and other products. Low enzyme activity and yield, and thermostability are, however, some of the limitations posing hurdles in saccharification of lignocellulosic residues. Recent advancements in synthetic and systems biology have generated immense interest in metabolic and genetic engineering that has led to the development of sustainable technology for saccharification of lignocellulosics in the last couple of decades. There have been several attempts in applying genetic engineering in the production of a repertoire of cellulases at a low cost with a high biomass saccharification. A diverse range of cellulases are produced by different microbes, some of which are being engineered to evolve robust cellulases. This review summarizes various successful genetic engineering strategies employed for improving cellulase kinetics and cellulolytic efficiency.

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Construction and screening of metagenomic library derived from soil for β-1, 4-endoglucanase gene

Cited by 9 publications

References 43 publications

Applying functional metagenomics to search for novel lignocellulosic enzymes in a microbial consortium derived from a thermophilic composting phase of sugarcane bagasse and cow manure

Applying functional metagenomics to search for novel lignocellulosic enzymes in a microbial consortium derived from a thermophilic composting phase of sugarcane bagasse and cow manure

Single method of purification for endoglucanase from Aspergillus niger by polyelectrolyte precipitation

Progress in Ameliorating Beneficial Characteristics of Microbial Cellulases by Genetic Engineering Approaches for Cellulose Saccharification

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