A thermostable GH8 endoglucanase of Enterobacter sp. R1 is suitable for β-glucan deconstruction

Ontañon, Ornella Mailén; Ghio, Silvina; Villegas, Rubén Marrero Díaz de; Garrido, Mercedes María; Talia, Paola; Fehér, Csaba; Campos, Eleonora

doi:10.1016/j.foodchem.2019.124999

Cited by 19 publications

(17 citation statements)

References 40 publications

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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%

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%

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

Zhong

Nidetzky

2019

Biotechnology Journal

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“…All eight polysaccharide fractions contained a significant amount of α-galactose, but none of them enriched the abundance of α-galactosidase coding genes, suggesting that the α-galactosidase might not degrade the polysaccharides. Cellulase catalyzes the decomposition of cellulose and is also reported to break down seaweed polysaccharides. , The enrichment of cellulase coding genes by LjA-1 and LjA-3 is worth conducting a deep investigation. LjA-1 and LjA-3 also significantly altered the abundance of gluconeogenesis I (GLUCONEO.PWY), sucrose degradation IV (PWY.5384), and UDP-glucose-derived O-antigen building block biosynthesis pathways (PWY.7328) (Figure D–F, respectively), indicating that LjA-1 and LjA-3 could decrease the accumulation of sugars and lipopolysaccharides.…”

Section: Resultsmentioning

confidence: 99%

Composition-Activity Relationships of Polysaccharides from Saccharina japonica in Regulating Gut Microbiota in Short-Term High-Fat Diet-Fed Mice

et al. 2021

J. Agric. Food Chem.

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Saccharina japonica polysaccharide could modulate gut microbiota composition; however, the composition-activity relationship remains unclear, thus restricting its application. In the current study, we investigated the impact of eight different S. japonica polysaccharide fractions on the gut microbiota after day 2 and day 14 treatments on high-fat diet (HFD) feeding mice. The results showed that a 2 day HFD dramatically altered gut microbiota composition, and the additional 12 day HFD further strengthened the gut microbiota dysbiosis in the HFD group. LjA-1 and LjA-3 could partially alleviate the dysbiosis of gut microbiota composition and significantly alter gut microbiota function. Multiple linear regression analysis revealed that the sulfate content and the molecular weight distributions were the main factors affecting the dominant gut bacterial genera. Our findings reveal that gut microbiota homeostasis could be disordered by HFD at day 2 and provide insights into the quantitative composition-activity relationships of polysaccharides in regulating gut microbiota.

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“…GH8 are bacterial enzymes which have been characterized mainly as endoglucanases and chitosanases [ 19 ] as well as xylanases [ 31 ]. GH8 endoglucanases have been widely studied as part of Bacterial Cellulose Synthase (Bcs) complexes involved in production and export of the glucan extracellular matrix in different bacteria [ 27 , 32 ] and also as part of polysaccharide degrading systems, with CelA from the anaerobic bacterium Clostridium thermocellum as one of the most studied ones [ 33 ]. In this regard, Cel8Pa had high identity with Paenibacillus sp.…”

Section: Discussionmentioning

confidence: 99%

“…In all assays, controls of substrate without enzyme and enzyme without substrate were included. The enzymatic hydrolysis of cello-oligosaccharides (COS) (1 mg/mL final concentration), with degrees of polymerization (DP) ranging from 2 to 6 (Megazymes), was evaluated by thin layer chromatography (TLC) after 1 h incubation at optimal enzyme conditions [ 27 ]. Glucose was also included as control for trans-glycosidase activity.…”

Section: Methodsmentioning

confidence: 99%

Synergic activity of Cel8Pa β-1,4 endoglucanase and Bg1Pa β-glucosidase from Paenibacillus xylanivorans A59 in beta-glucan conversion

Ghio

Bradanini

Garrido

et al. 2020

Biotechnology Reports

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Highlights Cel8Pa is an extracellular, halotolerant, broad substrate endoglucanase. Bg1Pa is an intracellular β-glucosidase, with activity on cello oligosaccharides and high resistance to ethanol. The concerted action of Cel8Pa and Bg1Pa has a synergistic effect on saccharification of β-glucans. Cel8Pa and Bg1Pa are cold-stable and candidates for SSF ethanol 2 G processes.

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A thermostable GH8 endoglucanase of Enterobacter sp. R1 is suitable for β-glucan deconstruction

Cited by 19 publications

References 40 publications

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

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

Composition-Activity Relationships of Polysaccharides from Saccharina japonica in Regulating Gut Microbiota in Short-Term High-Fat Diet-Fed Mice

Synergic activity of Cel8Pa β-1,4 endoglucanase and Bg1Pa β-glucosidase from Paenibacillus xylanivorans A59 in beta-glucan conversion

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