Production and partial characterization of xylanase produced by Jonesia denitrificans isolated in Algerian soil

Boucherba, Nawel; Benallaoua, Saı̈d; Copinet, Estelle; Hebal, Hakim; Duchiron, Francis

doi:10.1016/j.procbio.2010.10.003

Cited by 32 publications

(17 citation statements)

References 40 publications

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“…Jonesia species, Streptomyces species, Penicillium speices) for natural xylanase production (Table 1). The result from strain J3-8 is consistent with previous studies1516, showing that initial pH and initial concentration of xylan are important factors for improving extracellular xylanase production. Fontes et al also reported that more xylanases, especially extracellular ones, can be produced by using xylan rather than glucose as a substrate6.…”

Section: Resultssupporting

confidence: 91%

Characterization of a xylanase-producing Cellvibrio mixtus strain J3-8 and its genome analysis

2015

Sci Rep

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Cellvibrio mixtus strain J3-8 is a gram-negative, xylanase-producing aerobic soil bacterium isolated from giant snails in Singapore. It is able to produce up to 10.1 U ml−1 of xylanase, which is comparable to xylanase production from known bacterial and fungal strains. Genome sequence analysis of strain J3-8 reveals that the assembled draft genome contains 5,171,890 bp with a G + C content of 46.66%, while open reading frame (ORF) annotations indicate a high density of genes encoding glycoside hydrolase (GH) families involved in (hemi)cellulose hydrolysis. On the basis of 15 identified putative xylanolytic genes, one metabolic pathway in strain J3-8 is constructed for utilization of xylan. In addition, a 1,083 bp xylanase gene from strain J3-8 represents a new member of GH11 family. This gene is verified to be novel via phylogenetic analysis. To utilize this novel gene for hydrolysis of xylan to xylose, it is expressed in recombinant E. coli and characterized for its hydrolytic activity. This study shows that strain J3-8 is a potential candidate for hydrolysis of lignocellulosic materials.

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Section: Resultssupporting

confidence: 91%

Characterization of a xylanase-producing Cellvibrio mixtus strain J3-8 and its genome analysis

2015

Sci Rep

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“…Previous reports about the effectiveness of WB as strong inducers of xylanase activity are available in literature [22,23]. This would be expected, also, for SCB and BSG, since these three substrates are composed mainly by cellulose, hemicellulose, and lignin.…”

Section: Resultsmentioning

confidence: 70%

Production of Thermophilic Endo-β-1,4-xylanases by Aspergillus fumigatus FBSPE-05 Using Agro-industrial By-products

Souza

Bispo

Bon

et al. 2012

Appl Biochem Biotechnol

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In the present paper, endo-β-1,4-xylanase production by Aspergillus fumigatus was evaluated in solid-state fermentation using low-cost substrates such as sugarcane bagasse (SCB), brewer's spent grain (BSG), and wheat bran (WB). The partial characterization of the crude enzyme was also performed. In the experimental conditions, the highest levels of endo-β-1,4-xylanase production by A. fumigatus FBSPE-05 occurred within 8 days incubation when using SCB/liquid medium at 1:2 ratio (219.5 U g(-1)) and 4 days incubation when using WB/liquid medium at 1:1 ratio (215.6 U g(-1)). Crude enzyme from this last condition was used to enzyme characterization, showing best enzyme activity at 60 °C and pH 6.0, which suggests a thermophilic endoxylanase. The crude enzyme retained 73% of its activity after 1 h at 60 °C, and zymogram has shown three bands of endo-β-1,4-xylanase activity, with different molecular masses. A. fumigatus FBSPE-05 was able to grow and produce good levels of endo-β-1,4-xylanase using agro-industrial by-products, making this strain worthy for further investigation. To our knowledge, this is the first study reporting the use of SCB and/or BSG as sole substrates for endoxylanase production by solid-state fermentation using A. fumigatus.

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“…Among the various metal ions tested, Mg 2+ increased the activity significantly, whereas K + , Ca 2+ brought slight fall in the xylanase activity. The metal ions exert their effect by interacting with some amino acid residues involved in the active site, which causes a change in conformation leading to higher activity . All other ions such as Na + , Hg 2+ , Cu 2+ , Zn 2+ , Mn 2+ , Fe 3+ , and Co 2+ were found to be the potent inhibitors of isoenzymes activity.…”

Section: Resultsmentioning

confidence: 99%

Fast flow rate processes for purification of alkaline xylanase isoforms from Bacillus pumilus AJK and their biochemical characterization for industrial application purposes

Singh

Sharma

Varghese

et al. 2019

Biotechnology Progress

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This study shows the presence of five isozymic forms of alkaline xylanase from Bacillus pumilus using fast flow rate microfiltration, ultrafiltration, Q-sepharose, and phenyl sepharose chromatographic techniques. Polyacrylamide gel electrophoresis, highperformance liquid chromatography, and zymographic studies also revealed the purity of five isoforms of alkaline xylanases. Isoforms-X-I, X-III, and X-V exhibited optimum activity at pH 8.5, whereas X-II, X-IV showed maximum activity at pH 9. All isoforms were optimally active at temperature 55 C. Isoforms were found to be stable at pH 7-11, showed 92-100% residual activity after 3 hr, treatment time for most industrial applications. The isoforms retained nearly 80-86% residual activity after incubating at 45 C for 3 hr. Molecular weights of xylanase I-V, were 13.1, 15.3, 18.4, 20.1, and 21.0 kDa, respectively. Mg 2+ ions were found to be potent activator for all isozymic forms. The Km and Vmax values of X-I, X-II, X-III, X-IV, and X-V were 6.71, 6.66, 7.14, 5.88, 6.25 mg/ml and 2,000, 1,695, 1,666.66, 1,428.57, and 1,408.45 IU/mg protein, respectively. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis revealed the monomeric nature of all isoforms. The lowmolecular masses, significantly enhanced activity in the presence of industrially suitable-low cost activator, better stability of all isoforms at pH 7-11 and at higher temperature, also presence of multiple forms of alkaline xylanase, makes this enzyme suitable for textile-paper industries. This is also the first report mentioning the purification of five isozymic forms of alkaline xylanase using fast flow rate techniques.

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Production and partial characterization of xylanase produced by Jonesia denitrificans isolated in Algerian soil

Cited by 32 publications

References 40 publications

Characterization of a xylanase-producing Cellvibrio mixtus strain J3-8 and its genome analysis

Characterization of a xylanase-producing Cellvibrio mixtus strain J3-8 and its genome analysis

Production of Thermophilic Endo-β-1,4-xylanases by Aspergillus fumigatus FBSPE-05 Using Agro-industrial By-products

Fast flow rate processes for purification of alkaline xylanase isoforms from Bacillus pumilus AJK and their biochemical characterization for industrial application purposes

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