• Journal of Microbiology and Biotechnology
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• v.17 no.11
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• pp.1811-1817
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• 2007

Extracellular enzymes from Lentinus edodes M290 on normal woods (Quercus mongolica) and waste logs from oak mushroom production were comparatively investigated. Endoglucanase, cellobiohydrolase, ${\beta}$-glucosidase, and xylanase activities were higher on waste mushroom logs than on normal woods after 1. edodes M290 inoculation. Xylanase activity was especially different, with a three times higher activity on waste mushroom logs. When the waste mushroom logs were used as a carbon source, a new 35 kDa protein appeared. After the purification, the optimal pH and temperature for xylanase activity were determined to be 4.0 and $50^{\circ}C$, respectively. More than 50% of the optimal xylanase activity was retained when the temperature was increased from 20 to $60^{\circ}C$, after a 240 min reaction. At $40^{\circ}C$, the xylanase maintained 93% of the optimal activity, after a 240 min reaction. The purified xylanase showed a very high homology to the xylanase family 10 from Aspergillus terreus by LC/MS-MS analysis. The highest Xcorr (1.737) was obtained from the peptide KWI SQGIPIDGIG SQTHLGSGGS WTVK originated from Aspergillus terreus, indicating that the 35 kDa protein was xylanase. This protein showed low homology to a previously reported L. edodes xylanase sequence.

• Proceedings of the Korea Technical Association of the Pulp and Paper Industry Conference
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• 1999.11a
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• pp.194-204
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• 1999

The use of genetically cloned xylanase acquired from Bacillus strearthermophillus improves bleachability for oak kraft pulps. Combination of xylanase(X). oxygen(O), ozone(Z). peroxide(P), alkaline extraction(Eo. Eop), and chlorination(C/D, D) have been tested in a variety of bleaching sequences. The effectiveness of xylanase pre-treatment(XO) and post-treatment(OX) in oxygen bleaching is mainly compared. With xylanase treatment the brightness increase by 1.5-2.1% ISO in OZEP, OZEoP, OZEopP and OPZP sequences. There is only numerically difference of brightness gains between OX and XO sequences. With xylanase treatment chemical requirements for bleaching decrease by 42.6-48.6% in OC/DEoD sequence and 47.9-54.7% as active chlorine in OC/DEopD sequence at the same brightness. the reduction of bleaching chemicals is higher in XO sequence than those in OX sequence. Following xylanase treatment the viscosity increases from 11.7-12.0 mPa·s to 12.4-13.5 mPa·s and the brightness stability is considerably improved however the difference of effectiveness between XO and OX sequence is not present. Compared to tensile index vs tear index, the physical properties are similar for TCF bleaching sequences with and without xylanase treatments. However in OC/DEoD and OC/DEopD sequences the physical properties decrease with xylanase treatment. There is no difference in the physical properties between XO and OX sequences. COD, BOD and color of bleaching effluents increase slightly with xylanase treatment, however the discharge of COD end-load into environmental impact decrease.

• Asian-Australasian Journal of Animal Sciences
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• v.31 no.9
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• pp.1491-1499
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• 2018

Objective: This study was designed to investigate the effects of an Aspergillus sulphureus xylanase expressed in Pichia pastoris on the growth performance, nutrient digestibility and gut microbes in weanling pigs. Methods: A total of 180 weanling pigs (initial body weights were $8.47{\pm}1.40kg$) were assigned randomly to 5 dietary treatments. Each treatment had 6 replicates with 6 pigs per replicate. The experimental diets were wheat based with supplementation of 0, 500, 1,000, 2,000, and 4,000 U xylanase/kg. The experiment lasted 28 days (early phase, d 0 to 14; late phase, d 15 to 28). Results: In the early phase, compared to the control, average daily gain (ADG) was higher for pigs fed diets supplemented with xylanase and there was a quadratic response in ADG (p<0.05). In the entire phase, ADG was higher for the pigs fed 1,000 or 2,000 U/kg xylanase compared to the control (p<0.05). The gain to feed ratio was higher for pigs fed diets supplemented with 1,000 or 2,000 U/kg xylanase compared to the control (p<0.05). Increasing the amount of xylanase improved the apparent total tract digestibility of dry matter, crude protein, neutral detergent fiber, calcium, and phosphorus during both periods (p<0.05). Xylanase supplementation (2,000 U/kg) decreased the proportion of Lachnospiraceae (by 50%) in Firmicutes, but increased Prevotellaceae (by 175%) in Bacteroidetes and almost diminished Enterobacteriaceae (Escherichia-Shigella) in Proteobacteria. Conclusion: Xylanase supplementation increased growth performance and nutrient digestibility up to 2,000 U/kg. Supplementation of xylanase (2,000 U/kg) decreased the richness of gut bacteria but diminished the growth of harmful pathogenic bacteria, such as Escherichia-Shigella, in the colon.

• The Korean Journal of Food And Nutrition
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• v.7 no.1
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• pp.16-22
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• 1994

Xylanase from Bacillus sp. GS was purified through acetone precipitation, DEAE-Sephadex A-50 ion exchange chromatography and Sephadex G-100 gel filtration. The optimum reaction temperature of purified xylanase was 50t . Its optimum pH was between pH 6.0 and pH 6.5. This enzyme was stable below 5$0^{\circ}C$ for several hours and stable at between pH 5.5 and pH 8.0. The enzyme activity of xylanase was remarkably increased by Co++ and Cu++ ions. According to the study of hydrolysis mode of this enzyme, it was turned out to be ends type xylanase that can produce xylooligosaccharides, known as bifidogenic factor, from xylan.

• 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.

• Proceedings of the Korean Society for Applied Microbiology Conference
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• 1986.12a
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• pp.519.2-519
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• 1986

고온 호알카리성 Bacillus K-17의 xylanase유전자의 구조해명과 대량 생산 균주를 개발하기 위채 Bacillus K-17의 염색체를 pER 322를 사용하여 E. coli에 형질전환시켜 xylanase 활성을 나타내는 형질전환체를 얻었다. 이 형질전환체에서 hybrid plasmid를 분리하여 제한효소로 mapping하였고 이 유전자가 Bacillus K-17유래인가를 hybridization에 의해 확인하였다. Recombinant plasmid pAX 1113은 5.1kb HindIII 절편을 가졌으며 BgIII site가 두곳, ECoRI과 pst site가 한곳이었으며 효소를 정제한 결과 Bacillus K-17이 생산하는 두 가지 xylanase중에서 xylanase I과 동일하였다.

• Journal of Microbiology and Biotechnology
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• v.9 no.2
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• pp.157-162
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• 1999

Bacillus pumilus PJ19 isolated from Pinus leaves showed optimum xylanase production when grown in yeast tryptone broth at $37^{\circ}C$, pH 7.2, and shaken at 200 rpm after 48 h of incubation. Xylanase production was induced by xylan and xylose but repressed in the presence of glucose. Xylanase production by B. pumilus PJ19 was not growth-associated and the maximum enzyme production was found after 36 h of incubation.

• 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.

• Korean Journal of Microbiology
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• v.47 no.1
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• pp.81-86
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• 2011

Xylanase is a class of enzymes that hydrolyze the linear polysaccharide ${\beta}$-1,4-xylan into xylose. This enzyme is applied in the process of paper making and may be used for the process of biofuel production in the future. The Paenibacillus donghaensis JH8, isolated from Donghae deepsea sediment and reported as a novel bacterium, was known to degrade xylan and its xylanase was characterized in this study. The enzyme was maximally induced in the presence of 0.1% xylan. The production of xylanase was started at early logarithmic phase and reached about 55 miliunit at stationary phase of growth. The optimal temperature and pH of extracellular xylanase were found to be $40^{\circ}C$ and pH 6.0, respectively. The activity of xylanase was inhibited by the presence of $Ca^{2+}$, $Mn^{2+}$, $Fe^{2+}$, $Cu^{2+}$, $Al^{3+}$ or EDTA, and activated by $K^+$, $Ag^+$ or DTT. This xylanase was stable at $40^{\circ}C$ for 120 min, but lost almost their activity in 30 min at $60^{\circ}C$. Zymography analysis of concentrated culture supernatant revealed one major band at 42 kDa and two faint bands at 68 and 120 kDa.

• The Korean Journal of Mycology
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• v.25 no.4 s.83
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• pp.297-304
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• 1997

Effects of cultural conditions on the production of xylanase by Tremella fuciformis, symbiotic fungi and mixed fungi were investigated. The optimum carbon source for high production of xylanase by T. fuciformis, symbiotic fungi and mixed fungi was xylose. The optimum nitrogen source for both T. fuciformis and symbiotic fungi was $KNO_3$, whereas mixed fungi was $(NH_4)_2SO_4$. The optimum culture period for high production of xylanase was 5 days for both T. fuciformis and mixed fungi, and 6 days for symbiotic fungi, respectively. The optimum temperature for T. fuciformis and symbiotic fungi was $40^{\circ}C$, and the corresponding value for mixed fungi was $45^{\circ}C$. Xylanase activity was high at pH 6 for T. fuciformis and symbiotic fungi, and pH 7 for mixed fungi. Except $Hg^{2+}$ and $Pb^{2+}$, metal ions in T. fuciformis inhibited the activity of xylanase, and, thermal stability of xylanase in T. fuciformis, symbiotic fungi and mixed fungi maintained 80% of activity until $50^{\circ}C$. The Michaelis constant (Km) of xylan was $6.25{\times}10^{-5}\;M$ in T. fuciformis, $5.6{\times}10^{-2}\;M$ in symbiotic fungi, $5.2{\times}10^{-2}\;M$ in mixed fungi.