• Microbiology and Biotechnology Letters
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• v.20 no.5
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• pp.527-533
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• 1992

The optimal conditions for cellulase and xylanase production by Trichoderma reesei 28217 were studied for enzymatic deinking of old newspaper. The amounts of cellulase and xylanase from the strain was varied by initial medium pH, Tween 80, inoculum size of spore suspension, and carbon and nitrogen sources. The optimal conditions for cellulase production were pH 5.0-6.5, 0.02% of Tween 80, 0.5-1.0% of inoculum size of spore suspension ($1{\times}10^{7}$/ml). cottonseed meal as nitrogen source, and corn flour as carbon source. On the other hand, the optimal conditions for xylanase production were pH 6.5, 0.01% of Tween 80, corn steep liquor as nitrogen source, and disintegrated old newspaper as carbon source. The inoculum size for xylanase production was the same as for cellulase production. The concomitant production of cellulase and xylanase in shake flask culture was efficiently induced in the medium containing 0.5% cottonseed meal as nitrogen source and 1.0% old newspaper and 2.0% corn flour as carbon sources. In this case the activities of cellulase and xylanase produced were 6.11-7.22 IU/mJ and 97.7 IU/ml. respectively. However, the cellulase production in $5{\ell}$ fermentor scale was slightly decreased compared with that in flask scale. Moreover, xylanase production was severely reduced in a fermentor scale. The study for the reason of decreased enzyme production in fermentor is further needed.

• 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.

• Journal of Life Science
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• v.22 no.7
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• pp.912-919
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• 2012

A Bacillus sp. strain producing celluase and xylanase was isolated from environmental soil with LB agar plate containing carboxymethylcellulose (CM-cellulose) and beechwood xylan stained with trypan blue as substrates, respectively. Based on the 16S rRNA gene sequence and API 50 CHL test, the strain was identified as B. subtilis and named B. subtilis NC1. The cellulase and xylanase from B. subtilis NC1 exhibited the highest activities for CM-cellulose and beechwood xylan as substrate, respectively, and both enzymes showed the maximum activity at pH 5.0 and $50^{\circ}C$. We cloned and sequenced the genes for cellulase and xylanase from genomic DNA of the B. subtilis NC1 by the shot-gun cloning method. The cloned cellulase and xylanase genes consisted of a 1,500 bp open reading frame (ORF) encoding a 499 amino acid protein with a calculated molecular mass of 55,251 Da and a 1,269 bp ORF encoding a 422 amino acid protein with a calculated molecular mass of 47,423 Da, respectively. The deduced amino acid sequences from the genes of cellulase and xylanase showed high identity with glycosyl hydrolases family (GH) 5 and 30, respectively.

• Asian-Australasian Journal of Animal Sciences
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• v.26 no.7
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• pp.945-951
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• 2013

In vitro studies were undertaken to develop an appropriate fibrolytic enzymes cocktail comprising of cellulase, xylanase and ${\beta}$-D-glucanase for maize stover with an aim to increase its nutrient utilization in sheep. Cellulase and xylanase added individually to ground maize stover at an increasing dose rates (0, 100, 200, 400, 800, 1,600, 3,200, 6,400, 12,800, 25,600, 32,000, 38,400, and 44,800 IU/g DM), increased (p<0.01) the in vitro dry matter digestibility and in vitro sugar release. The doses selected for studying the combination effect of enzymes were 6,400 to 32,000 IU/g of cellulase and 12,800 to 44,800 IU/g of xylanase. At cellulase concentration of 6,400 IU/g, IVDMD % was higher (p<0.01) at higher xylanase doses (25,600 to 44,800 IU/g). While at cellulase doses (12,800 to 32,000 IU/g), IVDMD % was higher at lower xylanase doses (12,800 and 25,600 IU/g) compared to higher xylanase doses (32,000 to 44,800 IU/g). At cellulase concentration of the 6,400 to 32,000 IU/g, the amount of sugar released increased (p<0.01) with increasing levels of xylanase concentrations except for the concentration of 44,800 IU/g. No effect of ${\beta}$-D-glucanase (100 to 300 IU/g) was observed at lower cellulase-xylanase dose (cellulase-xylanase 12,800 to 12,800 IU/g). Based on the IVDMD, the enzyme combination cellulase-xylanase 12,800 to 12,800 IU/g was selected to study its effect on feed intake and rumen fermentation pattern, conducted on 12 rams (6 to 8 months; $20.34{\pm}2.369$ kg body weight) fed 50% maize stover based TMR. The total volatile fatty acids (p<0.01) and ammonia-N concentration was higher in enzyme supplemented group, while no effect was observed on dry matter intake, ruminal pH and total nitrogen concentration.

• Journal of Animal Science and Technology
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• v.50 no.3
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• pp.429-436
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• 2008

A bacterium producing cold-active cellulase and xylanase was isolated from pig feces. The isolate, DK42 strain, was found to be the Gram-positive, non-motile, catalase-positive, and spore-forming stain. Under an electron microscope, the cells were observed to be rod-shaped. The isolate was identified as Bacillus licheniformis DK42 on the basis of morphological and biochemical properties as well as 16S rRNA gene sequences. The characterization of crude cellulase and xylanase from B. licheniformis DK42 was investigated. Cellulase exhibited an optimum temperature and pH at 45℃ and 6.0, whereas xylanase exhibited an optimum temperature and pH at 55℃ and 6.0. Especially cellulase maintained approx. 50% of its maximum activity even at 10℃, indicating that it is cold-active. Both cellulase and xylanase were stable after 2hr at 35℃, whereas they lost their activities after 30min at 65℃.

• Korean Journal of Soil Science and Fertilizer
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• v.44 no.5
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• pp.836-840
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• 2011

In order to isolate thermophilic compost-promoting bacteria with high activity of cellulase and xylanase, spent mushroom substrates with sawdust were collected from mushroom cultivation farm, Jinju, Gyeongnam in Korea. Among of the isolates, one strain, designated SJ21 was selected by agar diffusion method. The strain SJ21 was identified as members of the Bacillus lincheniformis by biochemical characteristics using Bacillus ID kit and VITEK 2 system. Comparative 16S rDNA gene sequence analysis showed that strain SJ21 formed a distinct phylogenetic tree within the genus Bacillus and was most closely related to Bacillus subtilis with 16S rDNA gene sequence similarity of 99%. On the basis of its physiological properties, biochemical characteristics and phylogenetic distinctiveness, strain SJ21 was classified within the genus Bacillus, for which the name Bacillus sp. SJ21 is proposed. The cellulase and xylanase activity of Bacillus sp. SJ21 was slightly increased according to bacterial population from exponential phase to stationary phase in growth curve for Bacillus sp. SJ21.

• Journal of Life Science
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• v.22 no.1
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• pp.74-79
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• 2012

This study was conducted to investigate the production of water-soluble carbohydrates (WSCs) by treatment of different amounts of rice straw with cellulase, hemicellulase, and xylanase. Treatment of high amounts of rice straw (100 g/l) with cellulase and hemicellulase resulted in similar production of WSCs. Reducing the amount of rice straw to 50 g/l decreased the production of WSCs by hemicellulase but had no effect on WSC production by cellulase. The interaction among rice straw amounts, and hemicellulase and xylanase activities was investigated using a Box Behnken design and a response surface model. An interaction was found only between hemicellulase and xylanase. An enzyme mixture consisting of 0.55 mg/ml of hemicellulase and 0.65 mg/ml of xylanase generated the highest amounts of WSCs, regardless of the amount of rice straw provided. Therefore, the activity of cellulase was higher than that of either hemicellulose or xylanase for WSC production from rice straw. The interaction observed for hemicellulase and xylanase indicates that a combined enzyme treatment could improve the production of WSCs from rice straw.

• The Korean Journal of Mycology
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• v.18 no.4
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• pp.209-217
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• 1990

The influence of cellulosic and hemicellulosic substrates on the production of cellulase and xylanase complexes in Aspergillus niger was investigated. The culture conditions with different substrates exhibited profound effects on the level of endoglucanase (CMCase), ${\beta}-glucosidase$, endoxylanase and ${\beta}-xylosidase$, and on their isozyme patterns. However, intracellular and extracellular isozyme patterns of cellulase and xylanase complexes were qualitatively identical and appeared to be simultaneous in the early growth phase. Prolonged incubation led to the increase in the concentrations of isozymes with a little changes in the relative proportions of those isozymes. These results suggest that the biosynthesis of cellulase and xylanase complexes in A. niger is coordinately regulated at the level of induction. Moreover, multiple forms of extracellular cellulase and xylanase complexes seem to be the outcome of specific gene expression and should not be considered solely as the consequence of post-secretional modification of synthesized enzymes.

• Applied Biological Chemistry
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• v.24 no.4
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• pp.260-266
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• 1981

Some properties of cellulase and xylanase produced from Pleurotus ostreatus 301 and Lentinus edodes 3-1 during its growth in rice straw medium were investigated. The cellulase activities of P. ostreatus 301 and L. edodes 3-1 were increased in proportion to substrate concentration within 0.6% and 0.8%, respectively, and xylanase activities of two strains were increased within 1%. The reducing sugar production of cellulase and xylanase in two strains were proportionaly increased until 30 min. and 60 min. respectively. The opium pH for cellulase activities of P. ostreatus 301 and L. edodes 3-1 were pH 4.0 and pH 4.5, respectively, and xylanase activities of two strains were pH 5.0. The stable pH range for cellulase activities of P. ostreatus 301 was within 4.0 to 6.0 and L. edodes 3-1 was within 3.0 to 5.0, Xylanase activities of P. ostreatus 301 was within 4.5 to 6.0 and L. edodes 3-1 was within 3.5 to 6.0. The optium temperature for cellulase activities of P. ostraeatus 301 and L. edodes 3-1 were $40^{\circ}C$ and $50^{\circ}C$, respectively, but xylanase activities of P. ostreatus 301 and L. edodes 3-1 were $50^{\circ}C$ and $45^{\circ}C$, respectively. Thermal stability of enzymes were below of optimum temperature and these were mostly inactivate at $70^{\circ}C$ for 10 min of the metalic ions tested, cellulase activities of L. edodes 3-1 was increased by $Co^{++},\; Mg^{++}$ at the concentration of $10^{-2}M$, but were greatly inhibited by $Hg^{++},\;Cu^{++}$ in two strains. Xylanase activities were increased by $Ca^{++},\;Co^{++},\;Mg^{++}$ and $Cd^{++}$ but was greatly inhibited by $Hg^{++}$.

• Proceedings of the Korean Society for Applied Microbiology Conference
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• 1978.04a
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• pp.97.2-97
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• 1978

숙성한 퇴비에서 16종의 사상균을 분리하고 이들의 xylanase 및 cellulase의 활성을 측정하였다. 이 결과 효소활성이 강한 6 균주를 선별하고 이들의 형태학적 특성을 속까지 동정하고 선별된 균주가 생산하는 xylanase와 cellulase의 성질을 비교 검토하였다. 선별된 균주의 배양기질에 따른 효소생산량 산량을 비교하기 위해 cellulose와 xylan으로 배양한 후 이들을 분해하는 효소활성의 비 즉 xylanase/cellulase 비를 계산하고 이들 효소의 일반 성질을 검토하였다. 차후 연구에서 이들 효소를 분리, 정제하기 위해 acetone에 의한 침전성을 아울러 실험하였다.