Cloning, expression and characterization of C. crescentus xynA2 gene and application of Xylanase II in the deconstruction of plant biomass

Jacomini, Débora; Bussler, Larissa; Corrêa, Juliana Moço; Kadowaki, Marina Kimiko; Maller, Alexandre; Silva, José Luis da Conceição; Simão, Rita de Cássia Garcia

doi:10.1007/s11033-020-05507-2

Cited by 9 publications

(5 citation statements)

References 47 publications

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“…The ratio of xylobiose in the xylose-based sugars released by MxynB-8 was higher than the previously reported 19.56 and 51.6% (Azelee et al, 2016;Sepulchro et al, 2020) and lower than reported 85.99% (Xian et al, 2019). In addition, the enzymatic efficiency based on the poplar sawdust xylan in the raw material was 30.5%, which is slightly higher than or similar to other reported enzymatic hydrolysis results (Azelee et al, 2016;Jacomini et al, 2020;Sepulchro et al, 2020). These results indicate that MxynB-8 has a promising biotechnological potential to transform poplar sawdust xylan into XOS, which can contribute to valorization of underutilized agricultural and forestry wastes.…”

Section: Optimization Of Hydrolysis Conditions Of Poplar Sawdust Xylan By Mxynb-8contrasting

confidence: 54%

“…cellulose degradation function, as is the case of endo-1,4-βxylanase of Streptomyces sp. (Georis et al, 2000) and Caulobacter crescentus (Jacomini et al, 2020). Cellulose-free endo-1,4-βxylanase can remove hemicellulose compounds selectively with minimal cellulose loss, which is more profitable industrial processes, such as pulp bleaching, textile biorefining treatment, and food industry (Belfaquih et al, 2002).…”

Section: Optimization Of Endo-14-β-xylanase Mxynb-8 Hydrolysis Of Poplar Sawdust Xylanmentioning

confidence: 99%

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Co-production of Xylooligosaccharides and Xylose From Poplar Sawdust by Recombinant Endo-1,4-β-Xylanase and β-Xylosidase Mixture Hydrolysis

Jiang

Tong

et al. 2021

Front. Bioeng. Biotechnol.

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As is well-known, endo-1,4-β-xylanase and β-xylosidase are the rate-limiting enzymes in the degradation of xylan (the major hemicellulosic component), main functions of which are cleavaging xylan to release xylooligosaccharides (XOS) and xylose that these two compounds have important application value in fuel, food, and other industries. This study focuses on enzymatic hydrolysis of poplar sawdust xylan for production of XOS and xylose by a GH11 endo-1,4-β-xylanase MxynB-8 and a GH39 β-xylosidase Xln-DT. MxynB-8 showed excellent ability to hydrolyze hemicellulose of broadleaf plants, such as poplar. Under optimized conditions (50°C, pH 6.0, dosage of 500 U/g, substrate concentration of 2 mg/mL), the final XOS yield was 85.5%, and the content of XOS2−3 reached 93.9% after 18 h. The enzymatic efficiency by MxynB-8 based on the poplar sawdust xylan in the raw material was 30.5%. Xln-DT showed excellent xylose/glucose/arabinose tolerance, which is applied as a candidate to apply in degradation of hemicellulose. In addition, the process and enzymatic mode of poplar sawdust xylan with MxynB-8 and Xln-DT were investigated. The results showed that the enzymatic hydrolysis yield of poplar sawdust xylan was improved by adding Xln-DT, and a xylose-rich hydrolysate could be obtained at high purity, with the xylose yield of 89.9%. The enzymatic hydrolysis yield was higher (32.2%) by using MxynB-8 and Xln-DT together. This study provides a deep understanding of double-enzyme synergetic enzymolysis of wood polysaccharides to valuable products.

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Section: Optimization Of Hydrolysis Conditions Of Poplar Sawdust Xylan By Mxynb-8contrasting

confidence: 54%

Section: Optimization Of Endo-14-β-xylanase Mxynb-8 Hydrolysis Of Poplar Sawdust Xylanmentioning

confidence: 99%

Co-production of Xylooligosaccharides and Xylose From Poplar Sawdust by Recombinant Endo-1,4-β-Xylanase and β-Xylosidase Mixture Hydrolysis

Jiang

Tong

et al. 2021

Front. Bioeng. Biotechnol.

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“…Xyl10B presented higher specific activity values (255 IU/mg) than other GH10 xylanases identified from metagenomics analyses, such as: Pm25, derived from the (Jacomini et al 2020;Hero et al 2021;Vacilotto et al 2021). On the other hand, it showed an activity range similar to that of rXylR from Duganella sp.…”

Section: Discussionmentioning

confidence: 80%

“…As compared with xylanases derived from bacteria, Xyl10B showed higher specific activity than some of them, such as JdXyn10A, derived from Jonesia denitrificans (~ 65 IU/mg), CoXyn10A, derived from Cohnella sp. (~ 71.16 IU/mg), and XynA2, derived from Caulobacter crescentus (~ 1.02 IU/mg) (Jacomini et al 2020 ; Hero et al 2021 ; Vacilotto et al 2021 ). On the other hand, it showed an activity range similar to that of rXylR from Duganella sp.…”

Section: Discussionmentioning

confidence: 99%

Characterization of a novel GH10 alkali-thermostable xylanase from a termite microbiome

Mon

Villegas

Campos

et al. 2022

Bioresour. Bioprocess.

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The aim of the present study was to assess the biochemical and molecular structural characteristics of a novel alkali-thermostable GH10 xylanase (Xyl10B) identified in a termite gut microbiome by a shotgun metagenomic approach. This endoxylanase candidate was amplified, cloned, heterologously expressed in Escherichia coli and purified. The recombinant enzyme was active at a broad range of temperatures (37–60 ºC) and pH values (4–10), with optimal activity at 50 ºC and pH 9. Moreover, its activity remained at more than 80% of its maximum at 50 °C for 8 h. In addition, Xyl10B was found to be stable in the presence of salt and several ions and chemical reagents frequently used in the industry. These characteristics make this enzyme an interesting candidate for pulp and paper bleaching industries, since this process requires enzymes without cellulase activity and resistant to high temperatures and alkaline pH (thermo-alkaliphilic enzymes). The products of xylan hydrolysis by Xyl10B (short xylooligosaccharides, xylose and xylobiose) could be suitable for application as prebiotics and in the production of bioethanol. Graphical Abstract

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“…It was shown that ApXyn11A did not possess degradation of cellulose and cellobiose, which was similar to the hydrolytic properties of xylanases from Streptomyces sp (Georis et al, 2000). and Caulobacter crescentus(Jacomini et al, 2020). Xylanase without cellulose degradation capacity can selectively remove hemicellulose compounds and reduce cellulose loss, and thus ApXyn11A can be better used in paper, textile, and food industries(Belfaquih et al, 2002).…”

mentioning

confidence: 77%

Cloning, heterologus expression and characterization of a thermophilic and salt tolerant GH11 xylanase from Allostreptomyces psammosilenae YIM DR4008 T

Zhu

et al. 2023

Preprint

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Xylanases are used in a wide range of applications such as food, feed, and bioenergy production. Many industrial applications need to be carried out at high temperatures, so it is important to discover new thermophilic xylanases. In this study, a xylanase gene (576 bp), denominated apxyn11a, was obtained from Allostreptomyces psammosilenae YIM DR4008T and was cloned and heterologously expressed in Escherichia coli BL21(DE3). The recombinant xylanase (ApXyn11A) was isolated and purified by Ni2+-affinity chromatography. The molecular weight of recombinant ApXyn11A was 22.7 kDa. Its optimum reaction temperature and pH were 65°C and 5.6, respectively. It maintained above 95% relative activity after incubation at 55°C for 120 min and more than 80% residual activity after incubation in pH 4.0–6.0 for 24 h. What more, ApXyn11A exhibited more than 60% relative activity in presence of 3.5 M NaCl. The kinetic parameters Km (0.2 mg/mL), Vmax (2000 µmol/min/mg) and Kcat (755.09 S− 1) were determined using corn cob xylan as the substrate. These indicate that ApXyn11A has the properties of small molecular weight, thermophilic, salt and acid tolerance, which predicts the potential use of ApXyn11A in food, feed, paper and bioenergy fields.

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Cloning, expression and characterization of C. crescentus xynA2 gene and application of Xylanase II in the deconstruction of plant biomass

Cited by 9 publications

References 47 publications

Co-production of Xylooligosaccharides and Xylose From Poplar Sawdust by Recombinant Endo-1,4-β-Xylanase and β-Xylosidase Mixture Hydrolysis

Co-production of Xylooligosaccharides and Xylose From Poplar Sawdust by Recombinant Endo-1,4-β-Xylanase and β-Xylosidase Mixture Hydrolysis

Characterization of a novel GH10 alkali-thermostable xylanase from a termite microbiome

Cloning, heterologus expression and characterization of a thermophilic and salt tolerant GH11 xylanase from Allostreptomyces psammosilenae YIM DR4008 T

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