Physicochemical properties of thermotolerant extracellular β-glucosidase from Talaromyces thermophilus and enzymatic synthesis of cello-oligosaccharides

Mallek-Fakhfakh, Hanen; Belghith, Hafedh

doi:10.1016/j.carres.2015.10.014

Cited by 39 publications

(24 citation statements)

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“…Reported routes for their preparation are based upon depolymerization of cellulose or bottom‐up synthesis . Chemical and enzymatic methods are known for both types of route . Control of the product DP is essential and remains a challenge .…”

Section: Introductionmentioning

confidence: 99%

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Three‐Enzyme Phosphorylase Cascade for Integrated Production of Short‐Chain Cellodextrins

Zhong

Nidetzky

2019

Biotechnology Journal

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Cellodextrins are linear β‐1,4‐gluco‐oligosaccharides that are soluble in water up to a degree of polymerization (DP) of ≈6. Soluble cellodextrins have promising applications as nutritional ingredients. A DP‐controlled, bottom‐up synthesis from expedient substrates is desired for their bulk production. Here, a three‐enzyme glycoside phosphorylase cascade is developed for the conversion of sucrose and glucose into short‐chain (soluble) cellodextrins (DP range 3–6). The cascade reaction involves iterative β‐1,4‐glucosylation of glucose from α‐glucose 1‐phosphate (αGlc1‐P) donor that is formed in situ from sucrose and phosphate. With final concentration and yield of the soluble cellodextrins set as targets for biocatalytic synthesis, three major factors of reaction efficiency are identified and partly optimized: the ratio of enzyme activity, the ratio of sucrose and glucose, and the phosphate concentration used. The efficient use of the phosphate/αGlc1‐P shuttle for cellodextrin production is demonstrated and the soluble product at 40 g L−1 is obtained under near‐complete utilization of the donor substrate offered (88 mol% from 200 mm sucrose). The productivity is 16 g (L h)−1. Through a simple two‐step route, the soluble cellodextrins are recovered from the reaction mixture in ≥95% purity and ≈92% yield. Overall, this study provides the basis for their integrated production.

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Section: Introductionmentioning

confidence: 99%

“…[15,16] Chemical and enzymatic methods are known for both types of route. [11,[17][18][19][20][21] Control of the product DP is essential and remains a challenge. [22][23][24] Robust process technology fit for the bulk production of soluble cellodextrins is currently lacking.…”

Section: Introductionmentioning

confidence: 99%

Three‐Enzyme Phosphorylase Cascade for Integrated Production of Short‐Chain Cellodextrins

Zhong

Nidetzky

2019

Biotechnology Journal

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“…Jiang et al (2011) reported that a β-glucosidase, Bgl1E, from uncultured soil microorganisms did not contain a metal ion binding site. (Mallek-Fakhfakh and Belghith 2016) found that a β-glucosidase, Bgl.tls, from Talaromyces thermophilus was not affected by the Ca 2+ , Co 2+ , Mg 2+ and Mn 2+ divalent metal ions.…”

Section: Resultsmentioning

confidence: 99%

Characterization of a beta-glucosidase from Bacillus licheniformis and its effect on bioflocculant degradation

Chen

Meng

et al. 2017

AMB Expr

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Bacillus licheniformis CGMCC 2876, an aerobic spore-forming bacterium, produces a polysaccharide bioflocculant that is biodegradable and harmless. The present study determined that β-glucosidase played a negative role in bioflocculant synthesis. The gene encoding β-glucosidase was cloned and expressed in Escherichia coli BL21. This gene consists of 1437 bp and encodes 478 amino acid residues. The recombinant β-glucosidase (Bgl.bli1) was purified and showed a molecular mass of 53.4 kDa by SDS-PAGE. The expression and reaction conditions of Bgl.bli1 were optimized; the activity of β-glucosidase reached a maximum at 45.44 U/mL. Glucose clearly inhibited the activity of β-glucosidase. The purified recombinant Bgl.bli1 hydrolysed polysaccharide bioflocculant in vitro and synergised with other cellulases. The ability of Bgl.bli1 to hydrolyse polysaccharide bioflocculant was the reason for the decrease in flocculating activity and indicated the utility of this enzyme for diverse industrial processes.

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“…Hydrolysis of residual cellulose can be achieved using endo-and exoglucanases with a reduce activity of β-glucosidases [19] or modified carbon catalysts [20]. Enzyme-driven lytic oxidation is performed with polysaccharide monooxygenases (LPMOs) [21], enzymes that are present nowadays Fermentation 2020, 6, 31 3 of 27in most up-to-date cellulolytic enzyme industrial preparations. β-glucosidases not only hydrolyze cellobiose but they can catalyzed the reverse reaction (transglycosilation) to render C2, C3, C4 and C5 COS (cellobiose, cellotriose and higher molecular weight oligosaccharides) in the presence of relatively low concentrations of water [22].The hemicellulose fraction in lignocellulosic biomass is a rich source of xylooligosaccharides and mannooligosaccharides.…”

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Production of Oligosaccharides from Agrofood Wastes

et al. 2020

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The development of biorefinery processes to platform chemicals for most lignocellulosic substrates, results in side processes to intermediates such as oligosaccharides. Agrofood wastes are most amenable to produce such intermediates, in particular, cellooligo-saccharides (COS), pectooligosaccharides (POS), xylooligosaccharides (XOS) and other less abundant oligomers containing mannose, arabinose, galactose and several sugar acids. These compounds show a remarkable bioactivity as prebiotics, elicitors in plants, food complements, healthy coadyuvants in certain therapies and more. They are medium to high added-value compounds with an increasing impact in the pharmaceutical, nutraceutical, cosmetic and food industries. This review is focused on the main production processes: autohydrolysis, acid and basic catalysis and enzymatic saccharification. Autohydrolysis of food residues at 160-190 • C leads to oligomer yields in the 0.06-0.3 g/g dry solid range, while acid hydrolysis of pectin (80-120 • C) or cellulose (45-180 • C) yields up to 0.7 g/g dry polymer. Enzymatic hydrolysis at 40-50 • C of pure polysaccharides results in 0.06-0.35 g/g dry solid (DS), with values in the range 0.08-0.2 g/g DS for original food residues.Fermentation 2020, 6, 31 2 of 27 forestall engineering approaches, to name a few. Lignocellulosic biomass, of any origin is, therefore, a most promising raw material for biorefineries, considering such facilities as integrated refineries turning biomass into fuels, platform chemicals, food, feed and materials using integrated processes with an optimized used of resources [4]. This vision can be extended to resources of aquatic origin (seaweed, seagrass and microalgae) as well as residues from livestock [5,6]. In general, apart from forestall and energy crops biomass, most of it depends on the production of biomass and, in particular, food wastes [7,8]. While more than 100,000 M tons of biomass wastes are yearly produced [7], wastes strictly considered as food wastes (foods not consumed from any part of the food supply chain or any part of the food that is non edible and, therefore, becomes a residue) account for more than 1300 M tons each year [8]. The valorization of biomass wastes into a plethora of useful energy vectors, chemical compounds and ingredients receives a notable amount of interest from all stakeholders, including researchers and entrepreneurs. They are a source to several value-added products, such as monosaccharides (glucose, xylose, mannose, fructose, arabinose and more), oligosaccharides (fructoor FOS, xylo-or XOS, galacto-or GOS, galacturonic-or GALOS, lactosucrose, etc.), biofuels (ethanol, butanol, dimethylether -DME-, biodiesel, hydrogen), bioactive compounds (flavonoids, phenolic acids, terpenes, terpenoids, carotenoids), nanocellulose (bacterial, wood-related), lignin and its derivatives (a source of aromatics from biomass and prospective substitute of the aromatic or BTEX fraction produced in oil refineries) [8]. Oligomers from cellulose, hemicellulose, lignin, pectin and oth...

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Physicochemical properties of thermotolerant extracellular β-glucosidase from Talaromyces thermophilus and enzymatic synthesis of cello-oligosaccharides

Cited by 39 publications

References 39 publications

Three‐Enzyme Phosphorylase Cascade for Integrated Production of Short‐Chain Cellodextrins

Three‐Enzyme Phosphorylase Cascade for Integrated Production of Short‐Chain Cellodextrins

Characterization of a beta-glucosidase from Bacillus licheniformis and its effect on bioflocculant degradation

Production of Oligosaccharides from Agrofood Wastes

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