• Journal of the Korean Wood Science and Technology
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• v.25 no.2
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• pp.100-109
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• 1997

The objectives of this study was to decrease pollutions of bleaching effluent and was to enhanced brightness of non-chlorine bleached pulps by xylanase treatments. Xylanase cloned Esherichacoli(E. coli) capable of each of endo, exo-xylanase and acetyl-esterase were obtained from Bacillus stearothermophillus. These xylanase was maintained high activity in alkali and high temperature. Especially endo-xylanase would be more active in $60^{\circ}C$ and pH 11. Xylanase pretreatment(X) of unbleached pulp increased brightness, and decreased the degree of delignification. The degree of increase in brightness of pulp due to xylanase pretreatment was similar to non-enzyme treated pulp, regardless of the amount of enzyme added. Therefore, the addition of xylanase of 2 unit was recommended when considering costs of enzyme. The pulp bleached XO sequence had higher brightness and lower Kappa no, than O bleached pulp, while pulp bleached XP sequence had similar brightness and Kappa no. with P bleached pulp. In XOC/D, XOZ and XOP bleaching sequences, brightness and degree of delignification were improved. The C/D and Z stage bleached pulp was good effect on rate of raise in brightness and Kappa no., but P stage bleached pulp had similar level in non-enzyme treated bleaching sequence.

• Korean Journal of Microbiology
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• v.14 no.3
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• pp.99-99
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• 1976

Some properties of xylanase produced by Pleurotus ostreatus during its gorwth in a rice straw medium were investigated. The results are summarized as follows : 1) The optimum pH of xylanase was 5.0 and the stable pH ranged from 4.5 to 6.0. 2) The optimum temperature for the xylanse was around $50^{\circ}C$ and the xylanse activity was completely lost in 10 minutes at $70^{\circ}C$ 3) The activity of xylanse was inhibited by managanous ion, but was increased by other metalic ions. Especially K, Mg and Ca ions considerably increased the activity.

• Korean Journal of Microbiology
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• v.14 no.3
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• pp.93-104
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• 1976

Some properties of xylanase produced by Pleurotus ostreatus during its gorwth in a rice straw medium were investigated. The results are summarized as follows : 1) The optimum pH of xylanase was 5.0 and the stable pH ranged from 4.5 to 6.0. 2) The optimum temperature for the xylanse was around $50^{\circ}C$ and the xylanse activity was completely lost in 10 minutes at $70^{\circ}C$ 3) The activity of xylanse was inhibited by managanous ion, but was increased by other metalic ions. Especially K, Mg and Ca ions considerably increased the activity.

• Journal of Microbiology and Biotechnology
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• v.12 no.1
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• pp.153-156
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• 2002

The characterization of a partially purified, cellulase-free, thermostable alkaline xylanase from thermoalkalophilic Bacillus sp. JB-99 was investigated. The xylanase production was the highest when birchwood xylan was added to a medium containing finely powdered rice bran, showing 4,826 IU$ml^-1$ of activity for 15 h of incubation. The partially purified xylanase exhibited an optimum temperature and pH at $70^C{\circ}$ and 10, respectively. The enzyme was stable at pH 5-11 at $50^C{\circ}$. The xylanase activity was strongly inhibited by $Hg^2+$, while dithiothreitol, cysteine, and ${\beta}$-mercaptoethanol enhanced the activity.

• Microbiology and Biotechnology Letters
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• v.27 no.5
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• pp.370-377
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• 1999

Thermo-tolerant bacterium producing the xylanase was isolated from soil and identified as Bacillus pumilus. This strain, named Bacillus pumilus TX703, was able to grow ad produce xylanase at the culture temperature of 5$0^{\circ}C$. The maximum xylanase production was obtained when 1%(w/v) birchwood xylan and 1% (w/v) soytone were used as carbon source and nitrogen source, respectively. The biosynthesis of xylanase was under the catabolite repression induced by glucose in the culture medium, and it was completely inhibited in the presence of 0.2% (w/v) glucose. The maximum activity of xylanase was observed from pH8.0 to 9.0 and from 50 to 6$0^{\circ}C$ and the enzyme was highly heat-stable, whose activity remained was over 50% at 8$0^{\circ}C$, and was quite stable from pH5.0 to 10.0.

• Microbiology and Biotechnology Letters
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• v.16 no.6
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• pp.499-504
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• 1988

Among the new yeast strains which were isolated from soils by incubating in the xylan containing minimal medium at 3$0^{\circ}C$, one strain(XB-33) was finally selected by the results of extracellular xylanase production test. The characteristics of XB-33 was almost consistent with those of the Cryptococcus ater. The formation of xylanase activity was induced by xylan and repressed by xylose or glucose. The xylanase was partially purified from the culture supernatant with DEAE-Sephadex A5O chromatography. The enzyme had a pH optimum for activity at 5.0 and its stability range was pH 5-7. The temperature optimum was at 5$0^{\circ}C$, but the enzyme activity was greatly lost by heating at 7$0^{\circ}C$ for 60 minutes. The hydrolysis products from xylan by crude enzyme detected by TLC, were xylose and n series of higher oligosaccharides. The Km value of xylanase was 20 (mg/ml).

• Mycobiology
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• v.35 no.3
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• pp.166-169
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• 2007

A total of 106 Penicillium species were tested to examine their ability of degrading cellobiose, pectin and xylan. The activity of ${\beta}$-glucosidase was generally strong in all the Penicillium species tested. P. citrinum, P. charlesii, P. manginii and P. aurantiacum showed the higher ability of producing ${\beta}$-glucosidase than other tested species. Pectinase activity was detected in 24 Penicillium species. P. paracanescens, P. sizovae, P. sartoryi, P. chrysogenum, and P. claviforme showed strong pectinase activity. In xylanase assay, 84 Penicillium species showed activity. Strong xylanase activity was detected from P. megasporum, P. sartoryi, P. chrysogenum, P. glandicola, P. discolor, and P. coprophilum. Overall, most of the Penicillium species tested showed strong ${\beta}$-glucosidase activity. The degree of pectinase and xylanase activity varied depending on Penicillium species.

• Microbiology and Biotechnology Letters
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• v.43 no.4
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• pp.330-335
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• 2015

The optimum conditions for the production of xylanase from Bacillus agaradhaerens DK-2386 have been previously investigated. In this study xylanase was purified by ammonium sulfate precipitation and CM-sepharose ion exchange chromatography. The molecular mass of the xylanase as determined by SDS-PAGE was 23 kDa in a form of monomeric enzyme. The optimum pH and temperature for xylanase activity was 6.0 and $60^{\circ}C$, respectively. Xylanase activity was increased by the addition of EDTA and then stabilized at $40^{\circ}C$ for 24 h. The maximum xylanase activity was obtained when Birchwood xylan was used as a substrate and the $V_{max}$ and $K_m$ were $49,724{\mu}mol/min$ and 6.08 mg/ml, respectively.

• Journal of Industrial Technology
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• v.29 no.A
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• pp.161-167
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• 2009

The bifunctional Xylanase-Cellulase hybrid protein was constructed by gene fusion. Two genes corresponding to endoxylanase gene (xylS) and endocellulase gene (celA) were amplified by PCR from Bacillus licleniformis NBL420. It was then linked through splicing by overlap extension (SOE) by PCR method. The two resulting fused hybrids, xyl/cel and cel/xyl, which differ by its orientation, were confirmed by its nucleotide sequencings. One of two fusion genes, xyl/cel was successfully expressed into pET22b(+) vector (pxyl/cel) with bifunctional xylanase-cellulase activity. On the contrary, the other cel/xyl fusion protein showed only cellulase activity with much decreased xylanase activity. Enzymatic properties of Xyl/Cel fusion protein were investigated regarding optimum pH, optimum temp, thermostability, and pH stability. It was revealed that Xyl/Cel fusion protein retained the bifunctional xylanase-cellulase activities eventhough two enzymes were connected with each other directly. These informations could be useful for construction of other hybrid proteins as well as increased range of substrate utilization.

• KSBB Journal
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• v.26 no.5
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• pp.465-470
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• 2011

Twenty six microorganisms were isolated from soil and horse manure samples from in Iowa, U.S. Microorganisms were cultivated and screened by using plate count agar (PCA) at $35^{\circ}C$ containing 1% (w/v) oat spelt xylan instead of glucose. The xylanase activities of bacterial strains were analyzed by measuring the concentration of reducing sugar by DNS method. All isolated strains were characterized as the rod form and gram positive strains. Among the isolated strains, the HM6 strains gave the highest xylanase activity. This strain was identified as Bacillus pumilus HM6 by 16S rDNA sequence, morphological and biochemical analysis. Optimal culture temperature and initial medium pH for B. pumilus HM6 were $30-35^{\circ}C$ and pH 6-7, respectively. The maximum xylanase activity of 6879 IU/mL was obtained after growth of HM6 with 1% (w/v) oat spelt xylan at $35^{\circ}C$ for 6 days. Studies on enzymatic properties showed that the optimum conditions for the highest xylanase activity were $60^{\circ}C$ and pH 8.0. In addition, xylanase activity was stable over 2 hours at $50^{\circ}C$, whereas activity decreased after 30 min at $70^{\circ}C$.