• Journal of Life Science
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• v.13 no.5
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• pp.618-625
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• 2003

Investigations were carried out to optimize the culture conditions for the production of xylanase by Paenibacillus sp. DG-22, a moderately thermophilic bacterium isolated from timber yard soil. Xylanase production showed a cell growth associated profile. Xylanase activity was found only in the culture supernatant, while $\beta-xylosidase$ activity was mainly associated with the cells. The formation of xylanase activity was induced by xylan and repressed by glucose and xylose. The production profile of xylanase was examined with various commercial xylan and maximum yield was achieved with 0.1∼ 0.5% birchwood xylan. Among various nitrogen sources tested, yeast extract was optimal for the production of xylanase. The xylanase activity was inhibited by $Co^{2+},\; Cu^{2+},\; Fe^{3+},\; Hg^{2+}\;$ and$\;Mn^{2+}$ ions while $Ca^{2+},\; Mg^{2+},\; Ni^{2+},\; Zn^{2+}$ions and DTT stimulated xylanase activity Mercury (II) ion at 5 mM concentration abolished all the xylanase activity. The predominant products of xylan-hydrolysate were xylobiose, xylotriose, and higher xylooligo-saccharides, indicating that the enzyme was an endoxylanase.

• Microbiology and Biotechnology Letters
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• v.37 no.2
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• pp.147-152
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• 2009

A xylanase was purified from the culture supernatant of Bacillus sp. A-6 by using ultrafiltration and ion exchange chromatography on the column of SP-Sepharose using 5 mM acetate buffer, pH 5.0. The xylanase was eluted from the column at the concentration less than 0.05 M NaCl. The eluted xylanase was shown to be a single protein band in SDS-PAGE. Zymogram analysis indicated that the protein band in SDS-PAGE had the enzyme activity to hydrolyze oat spelt xylan. The molecular weights of the xylanase were 15,000 based on SDS-PAGE and 14,100 based on gel filtration chromatography. Thin layer chromatography showed that the xylanase hydrolyzed oat spelt xylan into xylobiose and high-molecular-weight xylooligosaccharides. The relative activities of the heated xylanase decreased to 80% at $40^{\circ}C$ after 7 hr and less than 40% at $60^{\circ}C$ after 1 hr.

• Mycobiology
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• v.51 no.4
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• pp.239-245
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• 2023

Xylanase has been applied in various sectors, such as biomass conversion, paper, pulp, textiles, and pharmaceutical industries. This study aimed to isolate and screen potential xylanase-producing fungi from the soil of Suphan Buri Province, Thailand. Fifteen fungi were isolated, and their xylanase activities were tested by the qualitative method. The result showed that isolate SP3, SP10 and SP15 gave high xylanase activity with potency index (PI) of 2.32, 2.01 and 1.82, respectively. These fungi were selected for the xylanase quantitative test, isolate SP10 performed the highest xylanase activity with 0.535 U/mL. Through molecular methods using the 𝛽-tubulin gene, isolate SP10 was identified as Penicillium menonorum. The xylanase characteristics from P. menonorum SP10 were determined, including the xylanase isoforms and the optimum pH and temperature. The xylanase isoforms on SDS-PAGE indicated that P. menonorum SP10 produced two xylanases (45 and 54 kDa). Moreover, its xylanase worked optimally at pH 6 and 55 ℃ while reaching 61% activity at 65 ℃. These results proposed P. menonorum SP10 as a good candidate for industrial uses, especially in poultry feed and pulp industries, to improve yield and economic efficiency under slightly acidic and high-temperature conditions.

• Microbiology and Biotechnology Letters
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• v.20 no.1
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• pp.14-19
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• 1992

The xylanase producing microorganisms occurring on rotten woods were selectively isolated on the modified Czapek-Dox medium supplemented with 0.5% xylan as a sole carbon source. Among more than three-hundred isolates of xylanase producing microorganisms, only two bacterial isolates were turned out to be more potent xylanase producer than the reference strain of xylanase producer, Aureobaszdium pullulans NRRL Y-2311. The exo-xylanase producer, bacterial isolate No. 33 was identified as a strain of Pseudomonas sp. on the basis of morphological and biochemical characterizations as well as cellular fatty acid composition. Optima of pH and of temperature for enzyme reactions of xylanase were 5.5 and $50^{\circ}C$ respectively. The enzyme was stable in a range of pH 5.0~7.0 and below $45^{\circ}C$. Among the number of carbohydrate substrates, xylose was turned out to be a potent inducer of Pseudomonas sp. No.33 exo-xylanase. Among the raw materials tested, rice straw was the best material for xylanase production by Pseudomonas sp. strain No. 33.

• Microbiology and Biotechnology Letters
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• v.44 no.3
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• pp.324-332
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• 2016

A bacterial strain capable of hydrolyzing xylan was isolated from fermented soybean paste obtained from a domestic Buddhist temple, using enrichment culture with rice straw as a carbon source. The isolate, named YB-1301, was identified as Bacillus safensis on the basis of its DNA gyrase subunit B gene (gyrB) sequence. The xylanase productivity of strain YB-1301 was drastically increased when it was grown in the presence of wheat bran or various xylans. In particular, the maximum xylanase productivity reached above 340 U/ml in the culture filtrate from LB broth supplemented with only birchwood xylan at shake-flask level. The xylanase production was significantly induced by xylans at the stationary growth phase in LB medium containing xylan, whereas only a small amount of xylanase was constitutively produced from cells grown in LB medium with no addition of xylan. Furthermore, xylanase biosynthesis was induced more rapidly by the enzymatically hydrolyzed products of xylan than by the non-hydrolyzed xylan. In addition, the xylanase in the culture filtrate of B. safensis YB-1301 was found to have optimal activity at 55℃ and pH 6.5–7.0.

• Journal of Microbiology and Biotechnology
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• v.16 no.12
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• pp.1856-1861
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• 2006

A Bacillus sp. A-6 strain that produced xylanase was isolated from rice bran. The optimal temperature and pH for xylanase activity of the culture supernatant of Bacillus sp. A-6 were 40$^{\circ}C$ and pH 7, respectively. The optimal temperature and pH for xylanase production in the xylan medium were 30$^{\circ}C$ and pH 9, respectively. The optimal concentrations of oat spelt xylan and peptone for xylanase production were 0.5% and 1.5%, respectively. The best nitrogen sources for xylanase production was beef extract, but xylanase production was also supported comparably by tryptone and peptone. The bacterial growth in the optimal xylan medium reached stationary growth phase after 12 h of incubation. The xylanase production in the culture supernatant increased dramatically during the initial 12 h exponential growth phase and then remained constant at 23.8-24.5 unit/ml during the stationary growth phase. The pH of the culture medium decreased from 8.8 to 6.7 during the exponential growth phase and subsequently increased to 8.1 during the stationary growth phase. Rice bran, sorghum bran, and wheat bran as well as oat spelt xylan induced xylanase production. The xylanase production was repressed when glucose was added to the xylan-containing medium.

• Microbiology and Biotechnology Letters
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• v.2 no.3
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• pp.133-140
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• 1974

1) Two xylanase (designed as A and B) of Myriococcus albomyces were purified from an extract of wheat koji culture. Puriscation steps included first ammonium sulfate fractionation followed successively by SE-Sephadex column chromatgraphy. DEAE-Sephadex column chromatography and gel filtration on Sephadex G-100 repectively. 2) The optimum pH and pH stability for crude xylanse were found to be pH 5.0 and pH 4.0-7.0 respectively. 3) The optimium temperature was found to he 5$0^{\circ}C$ and for the thermal statbility of xylanase, the enryme incubated at $65^{\circ}C$ for 60min did not affect their stability. 4) The purised xylanase A and B were considered as liquefying xylanase and saccharogenic xylauase repectively. 5) The Bylanase A was most active at pH 4.0 and range of pH 3.0-8.0 at 3$0^{\circ}C$ for six hrs. The B was most active at pH 5.0 showing stability range of pH 4.0 to 8.5 at 3$0^{\circ}C$ for 6 hrs. incubation respectively. The Optimum temperature of xylanase A and B were found to be 7$0^{\circ}C$ and $65^{\circ}C$ for 60min repectively.

• Korean Journal of Microbiology
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• v.48 no.2
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• pp.141-146
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• 2012

A gene encoding the xylanase (XynA) predicted from partial genomic sequence of Paenibacillus woosongensis was cloned into Escherichia coli by PCR. This xynA gene consisted of 633 nucleotides, encoding a polypeptide of 211 amino acid residues. The deduced amino acid sequence exhibited 85-89% identity with those of several Paenibacillus xylanases, belonging to the glycosyl hydrolase family 11. As a results of expression of the structural gene by T7 promoter of a pET23a(+) expression vector, xylanase activity was higher in cell-free extract than culture filtrate of a recombinant Escherichia coli BL21(DE3) CodonPlus. However, the expression level of xylanase was not sufficient be detected by SDS-PAGE. The cell-free extract showed maximal xylanase activity at $60^{\circ}C$ and pH 5.5. The predominant products resulting from xylan and xylooligosaccharide hydrolysis were xylose and xylotriose. The enzyme could hydrolyze xylooligosaccharides larger than xylbiose.

• Journal of Life Science
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• v.15 no.5 s.72
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• pp.734-738
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• 2005

A gene coding for xylanase from alkali-tolerant Bacillus alcalophilus AX2000 was cloned into Escherichia coli $DH5\alpha$ using pUC19. Among 2,000 transformants, one transformant showed clear zone on the detection agar plate containing oat-spells xylan. Its recombinant plasmid, named pXTY99, was found to carry 7.0 kb insert DNA fragment. When the nucleotide sequence of the cloned xylanase gene (xynT) was determined, xynT gene was found to consist of 1,020 base-pair open reading frame coding for a poly-peptide of 340 amino acids with a deduced molecular weight of 40 kDa. The coding sequence was preceded by a putative ribosome binding site, and the transcription initiation signals. The deduced amino acid sequence of xylanase is similar to those of the xylanases from Bacillus sp. Nl37 and B. stearothermophilus 21 with $61\%$ and $59\%$ identical residues, respectively.

• Biotechnology and Bioprocess Engineering:BBE
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• v.2 no.2
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• pp.94-96
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• 1997

A xylanase was purified from a commercial crude xylanase, Pulpzyme HC, and used for the bleaching of kraft pulp in the absence or in the presence of nonionic surfactants, Tween 20, Tween 80, and Igepal C930. The purified xylanase has a molecular weight of 23,500 as determined by a reducing SDS-PAGE. Tween 20 was most effective to enhance the efficiency of the enzymatic bleaching of kraft pulp by xylanase.