Evaluation of the transglycosylation activities of a GH 39 β-d-xylosidase for the synthesis of xylose-based glycosides

Muzard, Murielle; Aubry, Nathalie; Plantier‐Royon, Richard; O’Donohue, Michael; Rémond, Caroline

doi:10.1016/j.molcatb.2008.10.004

Cited by 27 publications

(22 citation statements)

References 37 publications

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“…Additionally, the mutations of W217A and W315A produced a significant increase (approximately 8.3-fold) of catalytic activity for PNP-xylopyranoside, while they negatively influenced the xylanolytic activity of iXylC for birchwood xylan. Accordingly, it is expected that the evolved enzymes, W217A and W315A, with high catalytic activity may be very useful as biocatalysts for the synthesis of valuable bio-surfactants, alkyl xylopyranosides from alcohols with PNP-xylopyranoside (Muzard et al, 2009). In this study, the catalytic activity of iXylC for PNP-cellobioside could be increased only to approximately 1.2-fold and 1.9-fold by the mutations of W96A and W315A, respectively.…”

Section: Site-directed Mutagenesis Of Trp Residuesmentioning

confidence: 78%

Novel intracellular GH10 xylanase from Cohnella laeviribosi HY-21: Biocatalytic properties and alterations of substrate specificities by site-directed mutagenesis of Trp residues

Kim

Han

et al. 2010

Bioresource Technology

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Section: Site-directed Mutagenesis Of Trp Residuesmentioning

confidence: 78%

Novel intracellular GH10 xylanase from Cohnella laeviribosi HY-21: Biocatalytic properties and alterations of substrate specificities by site-directed mutagenesis of Trp residues

Kim

Han

et al. 2010

Bioresource Technology

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“…Various starting materials, including agricultural residues (such as sugarcane bagasse, corn stover, wheat bran (WB) and wheat straw (WS)) and forest residues, represent biomass substrates of interest to biorefineries [2,3]. The development of integrated biorefineries requires valorizing the entire plant, and in this context, the transformation of hemicellulosic components of plant cell walls offers new opportunities for biorefineries to produce high value molecules, such as alkyl pentosides [4,5]. …”

Section: Introductionmentioning

confidence: 99%

The hemicellulolytic enzyme arsenal of Thermobacillus xylanilyticus depends on the composition of biomass used for growth

et al. 2012

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BackgroundThermobacillus xylanilyticus is a thermophilic and highly xylanolytic bacterium. It produces robust and stable enzymes, including glycoside hydrolases and esterases, which are of special interest for the development of integrated biorefineries. To investigate the strategies used by T. xylanilyticus to fractionate plant cell walls, two agricultural by-products, wheat bran and straw (which differ in their chemical composition and tissue organization), were used in this study and compared with glucose and xylans. The ability of T. xylanilyticus to grow on these substrates was studied. When the bacteria used lignocellulosic biomass, the production of enzymes was evaluated and correlated with the initial composition of the biomass, as well as with the evolution of any residues during growth.ResultsOur results showed that T. xylanilyticus is not only able to use glucose and xylans as primary carbon sources but can also use wheat bran and straw. The chemical compositions of both lignocellulosic substrates were modified by T. xylanilyticus after growth. The bacteria were able to consume 49% and 20% of the total carbohydrates in bran and straw, respectively, after 24 h of growth. The phenolic and acetyl ester contents of these substrates were also altered. Bacterial growth on both lignocellulosic biomasses induced hemicellulolytic enzyme production, and xylanase was the primary enzyme secreted. Debranching activities were differentially produced, as esterase activities were more important to bacterial cultures grown on wheat straw; arabinofuranosidase production was significantly higher in bacterial cultures grown on wheat bran.ConclusionThis study provides insight into the ability of T. xylanilyticus to grow on abundant agricultural by-products, which are inexpensive carbon sources for enzyme production. The composition of the biomass upon which the bacteria grew influenced their growth, and differences in the biomass provided resulted in dissimilar enzyme production profiles. These results indicate the importance of using different biomass sources to encourage the production of specific enzymes.

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“…β-1,4-xylan is the second most widespread polymer present in nature, representing one-third of the available renewable biomass [10,87]. Using proper chemical, autohydrolytic, or enzymatic procedures, it is possible to produce (XOS), D-xylose and, to a lesser extent, L-arabinose from crop waste residues and forestry biomass [88][89][90].…”

Section: Production Of Xylo-oligosaccharides As High Value-added Molementioning

confidence: 99%

Parageobacillus thermantarcticus, an Antarctic Cell Factory: From Crop Residue Valorization by Green Chemistry to Astrobiology Studies

et al. 2019

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Knowledge of Antarctic habitat biodiversity, both marine and terrestrial, has increased considerably in recent years, causing considerable development in the studies of life science related to Antarctica. In the Austral summer 1986–1987, a new thermophilic bacterium, Parageobacillus thermantarcticus strain M1 was isolated from geothermal soil of the crater of Mount Melbourne (74°22′ S, 164°40′ E) during the Italian Antarctic Expedition. In addition to the biotechnological potential due to the production of exopolysaccharides and thermostable enzymes, successful studies have demonstrated its use in the green chemistry for the transformation and valorization of residual biomass and its employment as a suitable microbial model for astrobiology studies. The recent acquisition of its genome sequence opens up new opportunities for the use of this versatile bacterium in still unexplored biotechnology sectors.

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Evaluation of the transglycosylation activities of a GH 39 β-d-xylosidase for the synthesis of xylose-based glycosides

Cited by 27 publications

References 37 publications

Novel intracellular GH10 xylanase from Cohnella laeviribosi HY-21: Biocatalytic properties and alterations of substrate specificities by site-directed mutagenesis of Trp residues

Novel intracellular GH10 xylanase from Cohnella laeviribosi HY-21: Biocatalytic properties and alterations of substrate specificities by site-directed mutagenesis of Trp residues

The hemicellulolytic enzyme arsenal of Thermobacillus xylanilyticus depends on the composition of biomass used for growth

Parageobacillus thermantarcticus, an Antarctic Cell Factory: From Crop Residue Valorization by Green Chemistry to Astrobiology Studies

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