• Journal of Korea Technical Association of The Pulp and Paper Industry
• /
• v.37 no.3
• /
• pp.9-16
• /
• 2005

This study was carried out to investigate the characteristics of extracellular cellulase and xylanase from 4 selected different species, such as enzyme activity and stability by pH, temperature and metal ions, for application into enzymatic deinking system. The optimal temperature and pH for enzyme activity of Bacillus pumilus I, B. subtilis I, B. pumilus II and B. subtilis II were mainly $40{\sim}60^{\circ}C$ and pH $6.0{\sim}7.0$, respectively. Certain metal ions, calcium and cobalt, elevated enzyme activity, even though there were different results of enzyme activities based on various metal ions in 4 different species. With these results we suggest that enzymatic deinking system should be proceed at $50^{\circ}C$ with neutral pH condition.

• Microbiology and Biotechnology Letters
• /
• v.44 no.3
• /
• pp.324-332
• /
• 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.

• Microbiology and Biotechnology Letters
• /
• v.37 no.2
• /
• pp.147-152
• /
• 2009

A xylanase was purified from the culture supernatant of Bacillus sp. A-6 by using ultrafiltration and ion exchange chromatography on the column of SP-Sepharose using 5 mM acetate buffer, pH 5.0. The xylanase was eluted from the column at the concentration less than 0.05 M NaCl. The eluted xylanase was shown to be a single protein band in SDS-PAGE. Zymogram analysis indicated that the protein band in SDS-PAGE had the enzyme activity to hydrolyze oat spelt xylan. The molecular weights of the xylanase were 15,000 based on SDS-PAGE and 14,100 based on gel filtration chromatography. Thin layer chromatography showed that the xylanase hydrolyzed oat spelt xylan into xylobiose and high-molecular-weight xylooligosaccharides. The relative activities of the heated xylanase decreased to 80% at $40^{\circ}C$ after 7 hr and less than 40% at $60^{\circ}C$ after 1 hr.

• Journal of Microbiology and Biotechnology
• /
• v.8 no.1
• /
• pp.49-52
• /
• 1998

A fungal strain able to produce filter paper activity (FPase) was isolated from soil by testing the ability to hydrolyze using filter paper. The isolated strain was identified as an Aspergilus sp. judging from its morphological and microscopical characteristics. The cellulase-xylanase system of Aspergillus sp. 8-17 was detected in situ after gel electrophoresis in the presence of SDS and showed that each protein pattern had a distinct polypeptide composition. ${\beta}$-1,4-Glucanase, cellobiohydrolase, and xylanase activity profiles differ from protein patterns. The Aspergillus sp. 8-17 hydrolytic enzymes responsible for the hydrolysis of ${\beta}$-glucan, MUC, and xylan have multiple active forms.

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

• Korean Journal of Microbiology
• /
• v.32 no.4
• /
• pp.306-314
• /
• 1994

The action mode of xylanase II from Trichoderma koningii ATCC 26113 on xylan and related oligosaccharides (xylotriose, xylotetraose, and arabinoxylotriose) indicated that xylanase II is an endo-enzyme and also has trans-xylosidase activity. The $^1HNMR$-NMR studies of the reaction products formed by xylanase II revealed that all the hydrolysis products of xylooligosaccharides by the enzyme have only ${\beta}$-1,4-xylosidic linkage(s). Chemical modification of the enzyme with iodoacetamide showed that two cysteine residues per molecule of the enzyme was essential for the activity. Modification of the enzyme with N-bromosuccinimide demonstrated that four of the eight tryptophan residues were involved in its active site.

• Microbiology and Biotechnology Letters
• /
• v.37 no.4
• /
• pp.383-388
• /
• 2009

A strain YB914 was isolated from soil as a producer of the extracellular xylanase, which catalyzes the hydrolysis of oat spelt xylan. The strain YB914 was identified as Streptomyces sp. on the basis of its morphological, cultural and biochemical properties. The xylanase of culture filtrate was the most active at $55^{\circ}C$ and pH 5.5, and retained 80% of its maximum activity at the range of pH 4.5~7.0. In order to optimize the culture medium for xylanase production, ingredients of G.S.S medium were replaced by several carbohydrates. The carbohydrates such as oat spelt xylan, corn cob xylan, wheat bran and lactose increased the xylanase productivity of Streptomyces sp. YB914. However, xylanase production was greatly repressed by galactose or arabinose. The maximum xylanase productivity was reached to 48 U/mL in the modified medium containing 1% oat spelt xylan and 1.5% lactose.

• Journal of Microbiology and Biotechnology
• /
• v.7 no.6
• /
• pp.386-390
• /
• 1997

A xylanase from the Bacillus sp. strain DSNC 101, isolated from soil, was purified to homogeneity by anion-exchange and hydrophobic interaction chromatography followed by gel filtration chromatography. The enzyme cleaved xylan, but not carboxymethyl cellulose, Avicel, soluble starch, and pNPX. The main product of oat spelts xylan hydrolysates was xylobiose. The xylanase had a molecular weight of 25 kDa determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Optimum temperature and pH for the xylanase activity were $50^{\circ}C$ and 6.0, respectively. $K_{m}\;and\;V_{max}$ of the enzyme for oat spelts xylan were 12.5 mg of xylan/ml and 869.5 unit/mg of protein, respectively. Xylanase was completely inhibited by Hg, Cu, and N-bromosuccinimide, but was stimulated by Ca, Co, and Mg.

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

To investigate the characteristics of active sites of the D-xylanase and $\beta$-xylosidase purified from Penicillium verruculosum, effects of various chemicals on the enzyme activity were analyzed. The D-xylanase was activated by Cua), however it was inhibited by metal ions, Hg2+ and Mna+, by chemicals, N-bromosuccinimide, iodine, diethylpyrocarbonate, and 2,3-butanedione. These results suggested that the D-xylanase from Penicillium verruculosum contained tyrosine, histidine, arginine and tryptophan at the active center. The $\beta$-xylosidase was inhibited by Hg2+, N-bromosuccinimide and sodium dodecyl sulfate, however it was not effected by Mn2+ and Cu2). It was suggested that the enzyme contained tryptophan at the active center.

• Journal of Microbiology and Biotechnology
• /
• v.23 no.6
• /
• pp.794-801
• /
• 2013

This paper reports the production and characterization of crude xylanase from the newly isolated Humicola sp. Ly01. The highest (41.8 U/ml) production of the crude xylanase was obtained under the optimized conditions (w/v): 0.5% wheat bran, 0.2% $KH_2PO_4$, and 0.5% peptone; initial pH 7.0; incubation time 72 h; $30^{\circ}C$; and 150 rpm. A considerable amount of the crude xylanase was induced using hulless barley bran or soybean meal as the carbon source, but a small amount of the enzyme was produced when supplementary urea was used as the nitrogen source to wheat bran. The crude xylanase showed apparent optimal cellulase-free xylanase activity at $60^{\circ}C$ and pH 6.0, more than 71.8% of the maximum xylanase activity in 3.0-30.0% (v/v) ethanol and more than 82.3% of the initial xylanase activity after incubation in 3.0-30.0% (v/v) ethanol at $30^{\circ}C$ for 2 h. The crude xylanase was moderately resistant to both acid and neutral protease digestion, and released 7.9 and 10.9 ${\mu}mol/ml$ reducing sugar from xylan in the simulated gastric and intestinal fluids, respectively. The xylooligosaccharides were the main products of the hydrolysis of xylan by the crude xylanase. These properties suggested the potential of the crude enzyme for being applied in the animal feed industry, xylooligosaccharides production, and high-alcohol conditions such as ethanol production and brewing.