A thermophilic and thermostable xylanase from Caldicoprobacter algeriensis: Recombinant expression, characterization and application in paper biobleaching

Mhiri, Sonia; Bouanane‐Darenfed, Amel; Jemli, Sonia; Neifar, Sawssan; Ameri, Rihab; Mezghani, Monia; Bouacem, Khelifa; Jaouadi, Bassem; Béjar, Samír

doi:10.1016/j.ijbiomac.2020.07.162

Cited by 48 publications

(20 citation statements)

References 52 publications

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“…The effects of various metal ions including Ag 2+ (AgNO 3 ), Ba 2+ (BaCl 2 ), Co 2+ (CoCl 2 ), Cu 2+ (CuSO 4 ), Fe 2+ (FeSO 4 ), Fe 3+ (FeCl 3 ), Hg 2+ (HgCl 2 ), Mg 2+ (MgSO 4 ), Na + (NaCl), and Zn 2+ (ZnSO 4 ) were determined at 1 mM and 10 mM concentration by adding them to the enzyme reaction mixture and incubating under standard assay conditions [ 22 ].…”

Section: Methodsmentioning

confidence: 99%

Beauveria bassiana Xylanase: Characterization and Wastepaper Deinking Potential of a Novel Glycosyl Hydrolase from an Endophytic Fungal Entomopathogen

Amobonye

Bhagwat

Singh

2021

JoF

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Beauveria bassiana is an entomopathogenic fungus widely used as a biopesticide for insect control; it has also been shown to exist as an endophyte, promoting plant growth in many instances. This study highlights an alternative potential of the fungus; in the production of an industrially important biocatalyst, xylanase. In this regard, Beauveria bassiana SAN01 xylanase was purified to homogeneity and subsequently characterized. The purified xylanase was found to have a specific activity of 324.2 Umg−1 and an estimated molecular mass of ~37 kDa. In addition, it demonstrated optimal activity at pH 6.0 and 45 °C while obeying Michaelis–Menton kinetics towards beechwood xylan with apparent Km, Vmax and kcat of 1.98 mgmL−1, 6.65 μM min−1 and 0.62 s−1 respectively. The enzyme activity was strongly inhibited by Ag2+ and Fe3+ while it was significantly enhanced by Co2+ and Mg2+. Furthermore, the xylanase was shown to effectively deink wastepaper at an optimal rate of 106.72% through its enzymatic disassociation of the fiber-ink bonds as demonstrated by scanning electron microscopy and infrared spectroscopy. This is the first study to demonstrate the biotechnological application of a homogeneously purified glycosyl hydrolase from B. bassiana.

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Section: Methodsmentioning

confidence: 99%

Beauveria bassiana Xylanase: Characterization and Wastepaper Deinking Potential of a Novel Glycosyl Hydrolase from an Endophytic Fungal Entomopathogen

Amobonye

Bhagwat

Singh

2021

JoF

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“…Xylanases are mainly used in the pulp bleaching, baking, and food industries (Walia et al 2017). Some of these technologies require xylanases to be active at higher temperatures and alkaline environments (Mhiri et al 2020). The two xylanases characterized in this study functioned at conditions of a wide range of pH and higher temperature, evidencing their potential application in the pulp bleaching and other industries.…”

Section: Discussionmentioning

confidence: 99%

“…Previously, fungal xylanases were mainly used for the degradation of xylan from plant biomass during biofuel manufacture and other industrial applications (Torres and Dela Cruz 2013;Walia et al 2017). Due to the diversity of naturally occurring efficient lignocellulose degradation systems, there is a possibility to recover novel types of xylanase from these for the efficient enzymatic degradation of xylan (Mhiri et al 2020).…”

Section: Introductionmentioning

confidence: 99%

Characterization of efficient xylanases from industrial-scale pulp and paper wastewater treatment microbiota

Wang

Liang

et al. 2021

AMB Expr

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Xylanases are widely used enzymes in the food, textile, and paper industries. Most efficient xylanases have been identified from lignocellulose-degrading microbiota, such as the microbiota of the cow rumen and the termite hindgut. Xylanase genes from efficient pulp and paper wastewater treatment (PPWT) microbiota have been previously recovered by metagenomics, assigning most of the xylanase genes to the GH10 family. In this study, a total of 40 GH10 family xylanase genes derived from a certain PPWT microbiota were cloned and expressed in Escherichia coli BL21 (DE3). Among these xylanase genes, 14 showed xylanase activity on beechwood substrate. Two of these, PW-xyl9 and PW-xyl37, showed high activities, and were purified to evaluate their xylanase properties. Values of optimal pH and temperature for PW-xyl9 were pH 7 and 60 ℃, respectively, while those for PW-xyl37 were pH 7 and 55 ℃, respectively; their specific xylanase activities under optimal conditions were 470.1 U/mg protein and 113.7 U/mg protein, respectively. Furthermore, the Km values of PW-xyl9 and PW-xyl37 were determined as 8.02 and 18.8 g/L, respectively. The characterization of these two xylanases paves the way for potential application in future pulp and paper production and other industries, indicating that PPWT microbiota has been an undiscovered reservoir of efficient lignocellulase genes. This study demonstrates that a metagenomic approach has the potential to screen efficient xylanases of uncultured microorganisms from lignocellulose-degrading microbiota. In a similar way, other efficient lignocellulase genes might be identified from PPWT treatment microbiota in the future.

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“…Thermophilic and hyperthermophilic bacteria such as Bacillus licheniformis ( Raj et al, 2018 ) Rhodothermus marinus ( Karlsson et al, 2004 ), Caldicoprobacter algeriensis ( Mhiri et al, 2020 ), Thermococcus zilligii , Sulfolobus solfataricus, and Pyrodictium abyssi have been extensively studied to produce highly thermostable xylanase. The majority of the xylanase produced from these thermophiles were identified to be members of families 10 and 11 of glycoside hydrolases (GH) ( Ghosh et al, 2020 ).…”

Section: Cellulase and Xylanase Of Thermophilesmentioning

confidence: 99%

“…The purified thermostable xylanase was optimally active at pH 6.5 and 80°C. It exhibited excellent thermostability with a half-life of 20 min at 80°C ( Mhiri et al, 2020 ). A xylanase from B. licheniformis had optimum relative activity at pH 9.0 and 60°C and maintained 80% of its relative activity when incubated for 1 h at a 60°C ( Raj et al, 2018 ).…”

Section: Cellulase and Xylanase Of Thermophilesmentioning

confidence: 99%

Thermostable Cellulases / Xylanases From Thermophilic and Hyperthermophilic Microorganisms: Current Perspective

Ajeje¹,

Hu²,

Song³

et al. 2021

Front. Bioeng. Biotechnol.

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The bioconversion of lignocellulose into monosaccharides is critical for ensuring the continual manufacturing of biofuels and value-added bioproducts. Enzymatic degradation, which has a high yield, low energy consumption, and enhanced selectivity, could be the most efficient and environmentally friendly technique for converting complex lignocellulose polymers to fermentable monosaccharides, and it is expected to make cellulases and xylanases the most demanded industrial enzymes. The widespread nature of thermophilic microorganisms allows them to proliferate on a variety of substrates and release substantial quantities of cellulases and xylanases, which makes them a great source of thermostable enzymes. The most significant breakthrough of lignocellulolytic enzymes lies in lignocellulose-deconstruction by enzymatic depolymerization of holocellulose into simple monosaccharides. However, commercially valuable thermostable cellulases and xylanases are challenging to produce in high enough quantities. Thus, the present review aims at giving an overview of the most recent thermostable cellulases and xylanases isolated from thermophilic and hyperthermophilic microbes. The emphasis is on recent advancements in manufacturing these enzymes in other mesophilic host and enhancement of catalytic activity as well as thermostability of thermophilic cellulases and xylanases, using genetic engineering as a promising and efficient technology for its economic production. Additionally, the biotechnological applications of thermostable cellulases and xylanases of thermophiles were also discussed.

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A thermophilic and thermostable xylanase from Caldicoprobacter algeriensis: Recombinant expression, characterization and application in paper biobleaching

Cited by 48 publications

References 52 publications

Beauveria bassiana Xylanase: Characterization and Wastepaper Deinking Potential of a Novel Glycosyl Hydrolase from an Endophytic Fungal Entomopathogen

Beauveria bassiana Xylanase: Characterization and Wastepaper Deinking Potential of a Novel Glycosyl Hydrolase from an Endophytic Fungal Entomopathogen

Characterization of efficient xylanases from industrial-scale pulp and paper wastewater treatment microbiota

Thermostable Cellulases / Xylanases From Thermophilic and Hyperthermophilic Microorganisms: Current Perspective

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