• The Korean Journal of Mycology
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• v.39 no.3
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• pp.198-204
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• 2011

This study was carried out to investigate occurence of microbiales density and characteristics of xylanase produced by those in Janggyeong Panjeon. Cladosporium cladosporioides H1, Penicillium citreonigrum H3, Penicillilum toxicarium H4, Aspergillus versicolor H6, Acremonium alternarium H7 isolated from Janggyeong Panjeon produced xylanase, which had different production rates and specialized activities in an acidic condition. Cladosporium cladosporioides H1, Aspergillus versicolor H6, and Acremonium alternatum H7 produced xylanase at a faster rate than other fungi. A xylanase of Cladosporium cladosporioides H1 and Penicillilum toxicarium H4 showed a high thermostability in an acidic condition. As results, this study may lead to the development of a strategy for preservation of organic cultural heritages.

• 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℃.

• Microbiology and Biotechnology Letters
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• v.21 no.6
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• pp.588-593
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• 1993

Xylanase(1, 4-beta-D-xylan xylanohydrolase` EC 3.2.1.8) II was purified from Penicillium verruculosum by using the techniques of two anion exchange chromatographies, and gel filtration. The molecular weight of this enzyme was about 22, 000 as determined by SDS-electrophoresis. The enzyme showed hydropytic activity toward xylan but did not catalyze hydrolysis of Rho-nitrophenyl-beta-D-xylopyranoside, Rho-nitrophenyl-beta-D-glucopyranoside, Rho-nitrophenyl-beta-D-cellobiopyranoside, and celluloses such as Avicel, cotton, filter paper, carboxymethylcellulose.

• 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.

• 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 $Hg^{++}$.

• The Korean Journal of Mycology
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• v.25 no.2 s.81
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• pp.91-100
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• 1997

Production of alkaline carboxymethyl cellulase (CMCase) and xylanase by batch and fed-batch cultures of alkalophilic Cephalosporium sp. RYM-202 was investigated. Of carbon sources tested, wheat bran gave the highest production of those enzymes. The high levels of CMCase on carboxymethyl cellulose and xylanase on birchwood xylan suggest that the biosynthesis of CMCase and xylanase in Cephalosporium sp. RYM-202 is regulated separately at the level of enzyme induction. The temperature and pH for maximal production of those enzymes was $20^{\circ}C$ and 9.0, respectively. High concentration of wheat bran in batch fermentation resulted in the lower and delayed production of the enzymes by catabolite repression. In fed-batch fermentation with controlled feeding of 5% final wheat bran concentration, the highest activities of CMCase and xylanase were 0.39 and 9.2 units/ml, respectively, and 1.22 and 1.36 times higher respectively than those in batch fermentation on 5% wheat bran.

• Asian-Australasian Journal of Animal Sciences
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• v.20 no.11
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• pp.1721-1728
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• 2007

An in vitro and a feeding trial were conducted to investigate the effect of xylanase supplementation on the feeding value of growing pig diets containing high proportions of Chinese double-low rapeseed meals (DLRM). Seven diets were formulated to meet NRC (1998) nutrient requirements. Diet 1 based on corn-soybean meal was used as positive control 1, and diet 2, a practical diet which incorporated a conventional level of Chinese DLRM (60 g/kg diet), as positive control 2. Diet 3 contained a higher level of DLRM (100 g/kg diet) as the negative control. Diet 3 plus xylanase at 0.10, 0.25, 0.50 and 0.70 g/kg diet created diets 4, 5, 6 and 7, respectively. The seven diets were incubated in triplicate with the in vitro two-stage enzyme incubation method to predict responses of diets to xylanase in terms of digestibility of dry matter (DM), crude protein (CP) and neutral detergent fibre (NDF). In vitro, the negative control had the lowest CP and NDF digestibility. Both DM and CP digestibility were increased (p<0.05) owing to xylanase supplementation either at 0.50 or 0.70 g/kg diet, and NDF digestibility was improved following xylanase addition at all of the test levels. There was a high linear correlation ($r^2>90$, p<0.05) between the activity concentration of the enzyme when transformed into its logarithmic value and in vitro digestibility coefficients of DM, CP or NDF. In the feeding trial, 112 crossbred pigs were randomly assigned to seven dietary treatments with 16 replicate pens of one pig each. An obvious dose effect on growth rate was observed ($r^2=0.79$, p<0.05) within the inclusion levels of xylanase. Compared with the negative control, xylanase addition at 0.70 g/kg diet resulted in significantly increased ADG (878 g/d vs. 828 g/d, p<0.05), and a tendency towards improved growth rate (868 g/d vs. 828 g/d, p = 0.10) was also observed following the inclusion of xylanase at 0.50 g/kg diet. It would appear that the nutrient utilization of corn and Chinese DLRM diets by pigs could be enhanced by an appropriate amount of xylanase addition. The in vitro and in vivo results suggested that the in vitro incubation method is feasible for predicting responses of pigs to exogenous enzymes and identifying those preparations that possess potential for improvement of the nutritive values of feedstuffs.

• KSBB Journal
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• v.29 no.5
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• pp.316-322
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• 2014

Xylanase have been used to convert the polymetric xylan into fermentable sugars from the production of ethanol and xylitol from plant biomass. The aim of this study was to isolate and identify xylanolytic bacterium from herbivore feces and was to used the xylanase for enzymatic hydrolysis of biomass. Xylanolytic strains were isolated from 59 different feces of herbivores from Seoul Grand Park located in Gwacheon Gyeonggi-do. The xylanolytic strains were selected by congo red staining and DNS method. Total 67 strains isolated from the herbivores feces were tested for xylanase activity. Among the strains, H10-1, which has the highest xylanase activity, was isolated from feces of Ceratotherium simum. The H10-1 strain was identified as Bacillus pumilus based on its morphological/biochemical characteristics and partial 16S rDNA gene sequences. Culture conditions of B. pumilus H10-1 such as initial medium pH, incubation temperature and incubation time were optimized for maximum xylanase production. And also xylanase produced by B. pumilus H10-1 was applied for the saccharification of Miscanthus sacchariflorus cv. 'Geodae 1', which was pretreated with 1.5M NaOH. The optimized culture conditions of B. pumilus H10-1 were pH 9, $30^{\circ}C$ incubation temperature, and 7 day incubation time, respectively. This xylanase activity under the optimized conditions was $20.4{\pm}3.3IU$. The crude xylanase produced by B. pumilus H10-1 was used for the saccharification of xylan derived from pretreated 'Geodae 1'. The saccharification conditions were $50^{\circ}C$, 200 rpm, and 5 days. Saccharification efficiency of pretreated 'Geodae 1' by B. pumilus H10-1 was 8.2%.

• Applied Biological Chemistry
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• v.18 no.3
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• pp.109-116
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• 1975

In order to utilize the agricultural waste products for animal feeds, two high xylanase producing mold strains were selected from various sources of samples. The optimum conditions of xylanase production and the characteristics of the mold enzyme were investigated,and summarized as follows. 1. Two Aspergillus niger strains (experimental No. 1701 and 430) showed the high xylanase activity. 2. The highest xylanase production was obtained at pH 5.0-6.0 in two days. 3. Xylanase production in strain 1701 was increase with the addition of carboxy methyl cellulose, $NH_4H_2PO_4$ and corn steep liquor as carbon sources and natural nutrients, as respectively, while the other carbon, nitrogen, phosphate sources, natural nutrients and minerals gave no remarkable effect. In the strain 430, the enzyme procuction was not effected with the above substrate sources. 4. Maximum xylan hydrolysis reaction with the crude enzyme extract (33.3% v/v) was obtained in the 2% substrate concentration at pH 5.0 and $60^{\circ}C$ in three hours in both strains. 5. Maximum xylan hydrolysis rate was 95% at the optimum conditions for xylanase activity.