• 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.

• 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.

• 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.23 no.3
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• pp.304-310
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• 1995

A thermophilic bacterium producing the extracellular cellulase-free xylanase was isolated from soil and has been identified as Bacillus sp. The optimal growth temperature was 50$\circ$C and the optimal pH, 7.0. Under the optimal growth condition, maximal xylanase production was 2.2 units/ml in the flask culture. The enzyme production was induced by xylan and xylose, but was repressed by sucrose or trehalose. The partially purified xylanase was most active at 70$\circ$C. It was found that the enzyme was stable at 65$\circ$C for 10 hours with over 75% of the activity. The enzyme was most active at pH 7.0 and retained 90% of its maximum activity between pH 5.0 and pH 9.0 though Bacillus sp. was not grown on alkaline conditions (>pH 8.0). In addition, the activity of xylanase was over 60% at pH 10.0. At the ambient temperature, the enzyme was stable over a pH range of 5.0 to 9.0 for 10 h, indicating that the enzyme is thermostable and alkalotolerant. The activity of xylanase was completely inhibited by metal ions including Hg$^{2+}$ and Fe$^{2+}$, while EDTA, phenylmethylsulfonyl fluoride (PMSF), $\beta$-mercaptoethanol and SDS didn't affect its activity. The enzyme was also identified to exert no activity on carboxymethylcellulose, laminarin, galactomannan, and soluble starch.

• Journal of Life Science
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• v.12 no.2
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• pp.188-199
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• 2002

A gene coding for xylanase from thermo-tolerant Bacillus pumilus TX703 was cloned into Escherichia coli DH5 $\alpha$ using pUC19. Among 7,400 transformants, four transformants showed clear zones on the detection agar plates containing oat-spells xylan. One of them which showed highest xylanase activity was selected and its recombinant plasmid, named pXES106, was found to carry 2.24 kb insert DNA fragment. When the nucleotide sequence of the cloned xylanase gene (xynK) was determined, xynK gene was found to consist of 1,227 base-pair open reading frame coding for a polypeptide of 409 amino acids with a deduced molecular weight of 48 kDa. The coding sequence was preceded by a putative ribosome binding site, the transcription initiation signals, and cia-acting catabolite responsive element. The deduced amino acids sequence of xylanase is similar to those of the xylanases from Hordeum vulgare (barley) and Clostridium thermocellum, with 39 and 31% identical residues, respectively. The amino acids sequence of this xylanase was quite different from those of the xylanases from other Bacillus species.

• 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.

• Asian-Australasian Journal of Animal Sciences
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• v.18 no.1
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• pp.66-74
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• 2005

Three experiments were conducted to study the property of xylanase and the effects of xylanase in wheat-based diets on growth performance of broilers, respectively. Experiment 1 was performed in vitro to evaluate the effect of different pH and temperature on xylanase activity, and to evaluate the enzymic stability under different conditions. The results indicated that the optimum temperature and pH for xylanase activity were $50^{\circ}C$ and 4.5, respectively. The activity of enzyme solution was reduced rapidly after the treatment of water bath above $60^{\circ}C$ for 10 min. The enzyme was relatively stable at pH 3.5 to 8.0 and deteriorated when incubated at pH below 3.5. In Experiment 2, a total of 378 d-old male Arbor Acres broilers were randomly distributed to 7 different treatments with 6 replicates (9 birds) in each treatment. The treatments were as follows: (1) corn based diet (CS), (2) wheat based diet (WS), (3) WS+ 0.05% xylanase, (4) WS+0.15% xylanase, (5) WS+0.25% xylanase, (6) WS+0.35% xylanase, (7) WS+0.45% xylanase. The results showed that the body weight and feed/gain ratio of the broilers fed wheat-based diets have been significantly improved (p<0.05) compared to that fed corn-based diet in the first 3 wk. With regard to the wheat-based diets, the xylanase supplementation had a tendency to improve the growth performance in first 3 wk. After 3 wk, no significant difference (p>0.05) was found among all these different treatments. The supplementation of xylanase and the type of diets did not affect the feed intake but increased the concentration of triglyceride in serum. In Experiment 3, a total of 360 d-old male Arbor Acres broilers were assigned to 30 groups with 12 birds in each group randomly. These groups were then randomly distributed to 5 different treatments with 6 replicates within each treatment. The broilers of each treatment were fed one of the diets as follows: (1) Corn based diet, (2) White wheat based diet (WW) (3) White wheat based diet+0.25% xylanase, (4) Red wheat based diet, (5) Red wheat based diet+0.25% xylanase. The results showed that the body weight and feed/gain ratio had been significantly improved (p<0.05) by xylanase supplementation in the first 2 or 3 wk. The effect of xylanase in red wheat diet is a little higher than that used in white wheat diet. From the results of the present experiments, it can be concluded that the supplementation of Aspergillar xylanase can improve the performance of the broilers fed the wheat-based diet.

• Journal of Microbiology and Biotechnology
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• v.25 no.12
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• pp.2016-2023
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• 2015

Xylanase plays important roles in a broad range of industrial production as a biocatalyst, and its applications commonly require immobilization on supports to enhance its stability. Aluminum hydroxide, a carrier material with high surface area, has the advantages of simple and low-cost preparation and resistance to biodegradation, and can be potentially used as a proper support for xylanase immobilization. In this work, xylanase from Thermomyces lanuginosus was immobilized on two types of aluminum hydroxide particles (gibbsite and amorphous Al(OH)₃) through adsorption, and the properties of the adsorbed enzymes were studied. Both particles had considerable adsorptive capacity and affinity for xylanase. Xylanase retained 75% and 64% of the original catalytic activities after adsorption to gibbsite and amorphous Al(OH)₃. Both the adsorptions improved pH and thermal stability, lowered activation energy, and extended lifespan of the immobilized enzyme, as compared with the free enzyme. Xylanase adsorbed on gibbsite and amorphous Al(OH)₃ retained 71% and 64% of its initial activity, respectively, after being recycled five times. These results indicated that aluminum hydroxides served as good supports for xylanase immobilization. Therefore, the adsorption of xylanase on aluminum hydroxide particles has promising potential for practical production.

• 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.

• Korean journal of food and cookery science
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• v.31 no.1
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• pp.18-25
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• 2015

This study investigated the baking properties of sorghum with the addition of xylanase or Pentopan, which is a baking additive containing xylanase. The control bread was made with a 30% substitution for wheat flour and the optimum level of enzyme addition was 0.75 mg/g flour for Pentopan and 5 mg/g flour for xylanase. The water binding capacity of wheat flour increased with the addition of sorghum, but decreased with the addition of either xylanase or Pentopan. The resistance of dough increased while extensibility decreased with the addition of sorghum; however, resistance decreased while extensibility increased with the addition of the enzyme. Specific volume of bread decreased significantly with the addition of sorghum. However, the specific volume was significantly recovered with the addition of enzyme. Crumb firmness was higher in the sorghum-added sample, but crumb firmness of the bread decreased with the addition of the enzyme. The crumb firmness of bread with added xylanase decreased significantly in 24 hours. These results demonstrated that adding sorghum with either xylanase or Pentopan that included xylanase increased specific volume and decreased crumb firmness whereas sorghum decreased the quality of fermented bread when added to wheat flour. The firmness rate of fermented bread particularly decreased with the addition of pure xylanase.