• Journal of Microbiology and Biotechnology
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• 제6권3호
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• pp.173-178
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• 1996

Synergic effects among endo-xylanase, $\beta$-xylosidase, and acetyl xylan esterase of Bacillus stearothermophilus in the hydrolysis of xylan were studied by using birchwood, oat spelt, and acetylated xylan as substrates. Synergism between endo-xylanase and $\beta$-xylosidase was observed on all three substrates tested, indicating that $\beta$-xylosidase enhanced the production of xylose by relieving the end-product inhibition upon endo-xylanase conferred by xylooligomers. Endo-xylanase and $\beta$-xylosidase also showed synergism with acetyl xylan esterase in the hydrolysis of birchwood and acetylated xylan, while no synergic effect was detected in oat spelt xylan hydrolysis. Thus, the hydrolysis of xylan containing acetic acid side chains required the action of acetyl xylan esterase, which eliminated the steric hindrance of the side chains, leading to the better hydrolysis by endo-xylanase and $\beta$-xylosidase , and the acetyl xylan esterase activity was also enhanced by endo-xylanase and $\beta$-xylosidase for the latter enzymes provided acetyl xylan esterase with shorter xylan oligomers, the better substrate for the enzyme.

• 펄프종이기술
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• 제43권3호
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• pp.52-58
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• 2011

Proton-NMR spectroscopic method was applied to kinetic study of concentrated sulfuric acid hydrolysis reaction, especially focused on 2nd step of acid hydrolysis with deferent reaction time and temperature as main variables. Commercial xylan extracted from beech wood was used as model compound. In concentrated acid hydrolysis, xylan was converted to xylose, which is unstable in 2nd hydrolysis condition, which decomposed to furfural or other reaction products. Without neutralization steps, proton-NMR spectroscopic analysis method was valid for analysis of not only monosaccharide (xylose) but also other reaction products (furfural and formic acid) in acid hydrolyzates from concentrated acid hydrolysis of xylan, which was the main advantages of this analytical method. Higher temperature and longer reaction time at 2nd step acid hydrolysis led to less xylose concentration in xylan acid hydrolyzate, especially at $120^{\circ}C$ and 120 min, which meant hydrolyzed xylose was converted to furfural or other reaction products. Loss of xylose was not match with furfural formation, which meant part of furfural was degraded to other undetected compounds. Formation of formic acid was unexpected from acidic dehydration of pentose, which might come from the glucuronic acid at the side chain of xylan.

• Journal of Microbiology and Biotechnology
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• 제6권3호
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• pp.179-183
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• 1996

Synergism among endo-xylanase, $\beta$-xylosidase, and $\alpha$-L-arabinofuranosidase from Bacillus stearothermophilus upon xylan hydrolysis was investigated by using birchwood, oat spelt, and arabinoxylan as substrates. Endo-xylanase and $\beta$-xylosidase showed the cooperative action on all three substrates tested, revealing the fact that $\beta$-xylosidase assists endo-xylanase action in xylan hydrolysis by relieving the endproduct inhibition upon endo-xylanase conferred by xylooligomers. $\alpha$-L-Arabinofuranosidase also exhibited synergic effects with endo-xylanase and $\beta$-xylosidase on oat spelt and arabinoxylan, which contained significant amounts of arabinose side chains, whereas no synergism was detected on birchwood xylan which had only trace amounts of the side chain. Thus, the hydrolysis of xylan containing arabinose side chains required $\alpha$-L-arabinofuranosidase as well as endo-xylanase and $\beta$-xylosidase for the better hydrolysis of the substrates, and these enzymes work cooperatively in order to maximize the extent and rate of xylan hydrolysis.

• Journal of the Korean Wood Science and Technology
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• 제52권2호
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• pp.101-117
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• 2024

The conversion characteristics of the major components of Liriodendron tulipifera were investigated during acid-catalyzed organosolv pretreatment. Glucan in L. tulipifera was slowly hydrolyzed, whereas xylan was rapidly hydrolyzed. Simultaneous hydrolysis and degradation of xylan and lignin occurred; however, after complete hydrolysis of xylan at higher temperatures, lignin remained and was not completely degraded or solubilized. These conversion characteristics influence the structural properties of glucan in L. tulipifera. Critical hydrolysis of the crystalline regions in glucan occurred along with rapid hydrolysis of the amorphous regions in xylan and lignin. Breakdown of internal lignin and xylan bonds, along with solubilization of lignin, causes destruction of the lignin-carbohydrate complex. Over a temperature of 160℃, the lignin that remained was coalesced, migrated, and re-deposited on the surface of pretreated solid residue, resulting in a drastic increase in the number and content of lignin droplets. From the results, the characteristic conversions of each constituent and the changes in the structural properties in L. tulipifera effectively improved enzymatic hydrolysis in the range of 140℃-150℃. Therefore, it can be concluded that significant changes in the biomass recalcitrance of L. tulipifera occurred during organosolv pretreatment.

• Journal of the Korean Wood Science and Technology
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• 제40권6호
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• pp.389-396
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• 2012

본 연구는 산 촉매에 의한 자이란 분해속도를 분석하는 것으로 $120^{\circ}C$에서 60분 동안 가수분해를 수행하여 자이란 분해속도를 조사하였다. 산 촉매로는 황산, 옥살산, 말레산을 사용하였다. 자이란 분해에 관여하는 분해속도상수($k_1$)는 산 농도에 비례하여 증가하였으며 이것은 산 농도가 증가할수록 자이란 가수분해가 빠르게 진행된다는 것을 의미한다. 황산, 옥살산, 말레산 중에서 자이란에서 자이로스로 분해되는 속도는 황산을 촉매로 사용하였을 때 가장 높았다. 하지만 수소농도인 pH를 기준으로 하였을 때, 즉 같은 pH 조건에서 가수분해를 수행하였을 때 자이란에서 자이로스로 분해되는 속도는 옥살산, 말레산과 같은 dicarboxylic acid 촉매에서 황산을 사용하였을 때 보다 높은 분해속도상수를 나타냈다.

• 펄프종이기술
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• 제40권4호
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• pp.43-50
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• 2008

Adsorption of xylans extracted from birchwood and oat spelt on Hw-BKP were analyzed using HPLC. The effect of xylan adsorption on paper properties such as tensile, tear index and brightness was also investigated. The constituents of xylan was analyzed with HPLC after hydrolysis with dilute sulfuric acid. It was shown that xylose was the major constituent and small amounts of glucose and galactose were contained in the xylan samples. Adsorption of xylan on hardwood fibers was evaluated using acid hydrolysis and HPLC techniques. Results showed that the adsorption of negatively charged xylan on the fiber surface was negligible probably because electrostatic repulsion between these two materials. Pretreatment of the fiber with alum increased xylan adsorption. The amount of adsorption increased up to 30 mg/g. With the increase of xylan adsorption both tensile and tear strength of the handsheet increased suggesting xylan can be a very effective strength agents for papermaking. Brightness of the handsheets decreased, however, with the use of xylan.

• Journal of Microbiology and Biotechnology
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• 제25권9호
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• pp.1476-1484
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• 2015

Three endoxylanase-encoding genes from the moderately themophilic chemoorganotrophic bacterium Melioribacter roseus were cloned and expressed in Escherichia coli. Genes xyl2091 (Mros_2091) and xyl2495 (Mros_2495) encode GH10 family hydrolases, whereas xyl2090 (Mros_2090) represents the GH30 family. In addition to catalytic domains, Xyl2090 and Xyl2091 contain carbohydrate-binding modules that could facilitate their binding to xylans and Por sorting domains associated with the sorting of proteins from the periplasm to the outer membrane, where they are covalently attached. Recombinant endoxylanase Xyl2495 exhibited a high specific activity of 1,920 U/mg on birchwood xylan at 40℃. It is active at low temperatures, exhibiting more than 30% of the maximal activity even at 0℃. Endoxylanases Xyl2090 and Xyl2091 have lower specific activities but higher temperature optima at 80℃ and 65℃, respectively. Analysis of xylan hydrolysis products revealed that Xyl2090 generates xylo-oligosaccharides longer than xylopentaose. Xylose and xylobiose are the major products of xylan hydrolysis by the recombinant Xyl2091 and Xyl2495. No activity against cellulose was observed for all enzymes. The presence of three xylanases ensures efficient xylan hydrolysis by M. roseus. The highly processive "free" endoxylanase Xyl2495 could hydrolyze xylan under moderate temperatures. Xylan hydrolysis at elevated temperatures could be accomplished by concerted action of two cell-bound xylanases; Xyl2090 that probably degrades xylans to long xylo-oligosaccharides, and Xyl2091 hydrolyzing them to xylose and xylobiose. The new endoxylanases could be useful for saccharification of lignocellulosic biomass in biofuels production, bleaching of paper pulp, and obtaining low molecular weight xylooligosaccharides.

• Korean Chemical Engineering Research
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• 제52권2호
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• pp.226-232
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• 2014

본 연구에서는 $120{\sim}150^{\circ}C$에서 다양한 산 촉매에 의한 자이란 가수분해 거동을 조사하였다. 또한 자이란에서 자이로스 생성과 자이로스로부터 푸르푸랄 분해에 대한 kinetic 인자를 분석하였다. 높은 반응온도와 산 촉매 농도는 자이란 가수분해와 자이로스 분해를 촉진하였다. 최대 반응속도상수($k_1$)에 대한 가수분해 조건은 산 촉매에 따라 다르게 나타났다. 황산, 옥살산, 말레산 중에서 자이란 반응속도상수($k_1$)는 황산 100 mM로 $120^{\circ}C$에서 반응하였을 때 $0.0241min^{-1}$로 가장 높게 나타났다. 하지만 황산은 옥살산, 말레산과 비교하여 자이로스 분해를 더욱 유도하여 상대적으로 높은 푸르푸랄을 생성하였다. 자이란 분해에 관여하는 활성화 에너지는 황산에서 가장 높게 나타났다.

• 한국미생물·생명공학회지
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• 제11권1호
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• pp.23-32
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• 1983

본 연구에서는 Aspergillus niger KG79에서 두종류의 D-xylanase를 분리.정제하여 그 특성을 규명하였다. 이 두 종류의 D-xylanase의 물리화학적 및 동력학적 특성은 큰 차이가 없었다. 이들 Xylanase는 D-Xylan으로부터 Xylose, Xylobiose와 Xylotriose를 분해 생성하였다. 그러나 보리짚 Xylan을 기질로 사용했을 경우에는 Xylanase I 은 II보다 측쇄 arabinose를 상당히 빨리 분해하였다. 이들 효소에 의한 Xylan의 분해도는 기질의 종류에 따라 차이가 나서 보리짚 Xylan과 larchwood Xylan의 분해도는 각각 10%와 25%(환원당량) 정도로 나타났다. 순수정제된 Xylanase와 $\beta$-Xylosidase를 사용하여 재조합한 Xylanase계의 기질분해력을 비교한 결과 최적조건에서 보리짚과 larchwood Xylan은 각각 28%와 54%씩 분해 전환되었다. 이러한 결과는 Xylan의 효소분해도의 제한요소는 기질의 물리적 특성의 차이에 기인함을 추정할 수 있었다.

• Journal of Microbiology and Biotechnology
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• 제16권8호
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• pp.1255-1261
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• 2006

An alkaliphilic bacterium, Bacillus sp. strain BK, was found to produce extracellular cellulase-free xylanolytic enzymes with xylan-binding activity. Since the pellet-bound xylanase is eluted with 2% TEA from the pellet of the culture, they contain a xylan-binding region that is stronger than the xylan-binding xylanase of the extracellular enzyme. The xylanases had a different molecular weight and xylan-binding ability. The enzyme activity of xylanase in the extracellular fraction was 6 times higher than in the pellet-bound enzyme. Among the enzymes, xylanase had the highest enzyme activity. When Bacillus sp. strain BK was grown in pH 10.5 alkaline medium containing xylan as the sole carbon source, the bacterium produced xylanase, arabinofuranosidase, acetyl esterase, and $\beta$-xylosidase with specific activities of 1.23, 0.11, 0.06, and 0.04 unit per mg of protein, respectively. However, there was no cellulase activity detected in the crude enzyme preparation. The hydrolysis of agricultural residues and kraft pulps by the xylanolytic enzymes was examined at 50$^{\circ}C$ and pH 7.0. The rate of xylan hydrolysis in com hull was higher than those of sugarcane bagasse, rice straw, com cop, rice husk, and rice bran. In contrast, the rate of xylan hydrolysis in sugarcane pulp was 2.01 and 3.52 times higher than those of eucalyptus and pine pulp, respectively. In conclusion, this enzyme can be used to hydrolyze xylan in agricultural residues and kraft pulps to breach and regenerate paper from recycled environmental resources.