• 제목/요약/키워드: Beta-xylosidase

검색결과 79건 처리시간 0.032초

Production and Location of Xylanolytic Enzymes in Alkaliphilic Bacillus sp. K-1

  • Lee Yun-Sik;Ratanakhanokchai Khanok;Piyatheerawong Weela;Kyu Khin-Lay;Rho Min-Suk;Kim Yong-Seok;Om Aeson;Lee Joo-Won;Jhee Ok-Hwa;Chon Gil-Hyung;Park Hyun;Kang Ju-Seop
    • Journal of Microbiology and Biotechnology
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    • 제16권6호
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    • pp.921-926
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    • 2006
  • The production and location of xylanolytic enzymes in alkaliphilic Bacillus sp. K-1, isolated from the wastewater treatment plant of the pulp and paper industry, was studied. When grown in alkaline xylan medium, the bacteria produced xylanolytic enzymes such as xylanase, $\beta$-xylosidase, arabinofuranosidase, and acetyl esterase. Two types of xylanases (23 and 45 kDa) were found to be extracellular, but another type of xylanase (35 and/or 40 kDa) was detected as pellet-bound that was eluted with 2% triethylamine from the residual xylan of the culture. The xylanases were different in their molecular weight and xylan-binding ability. Arabinofuranosidase and $\beta$-xylosidase were found to be intracellular and extracellular, respectively, and acetyl esterase was found to be extracellular. The extracellular xylanolytic enzymes effectively hydrolyzed insoluble xylan, lignocellulosic materials, and xylans in kraft pulps.

Paenibacillus sp. DG-22로부터 xylanase 생산의 최적화 (Optimization of Xylanase Production from Paenibacillus sp. DG-22)

  • Lee, Yong-Eok
    • 생명과학회지
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    • 제13권5호
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    • pp.618-625
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    • 2003
  • 목재 저장소의 토양에서 분리된 호열성 세균인 Paenibacillus sp. DG-22로부터 xylanase를 생산하기 위한 배양조건을 최적화시키기 위해 연구를 수행하였다. Xylanase생산은 세포의 생장과 연관된 양상을 나타내었다. Xylanase 활성은 배양상청액에서만 발견된 반면 $\beta-xylosidase$활성은 주로 세포와 결합되어 있었다. Xylanase활성의 형성은 자일란에 의해 유도되었고 포도당과 자일로스에 의해서 억제되었다. 여러 상업적 자일란을 이용하여 xylanase의 생산양상을 조사한 결과 0.1-0.5%의 birchwood xylan에서 가장 높은 생산율을 나타내었다. 조사된 여러 질소 원들 중 효모추출물이 xylanase생산을 위하여 최적이었다. xylanase의 활성은 $Co^{2+},\; Cu^{2+},\; Fe^{3+},\; Hg^{2+}\;$$\; Mn^{2+}$ 이온들에 의하여 억제된 반면 $Ca^{2+},\; Mg^{2+},\; Ni^{2+},\; Zn^{2+}$ 이온들과 DTT에 의해서는 촉진되었다. 수은은 5 mM의 농도에서 xylanase 활성을 완전히 파괴하였다. 자일란 가수분해의 주된 산물은 자일로바이오스, 자일로트라이오스 그리고 자일로 올리고당이었고 이것은 이 효소가 endoxylanase라는 것을 나타낸다.

Trichoderma viride 균체외 효소로 부터 Xylanase의 정제 및 Xylan의 분해 (Purification of an Xylanase from the Extracellular Xylanolytic Systems of Trichoderma viride and Hydrolysis of Xylan)

  • 엄태진
    • Journal of the Korean Wood Science and Technology
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    • 제19권2호
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    • pp.22-29
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    • 1991
  • The endo-1,4-${\beta}$-xylanase was extracted and purified from the extracellular xylanolytic systems of Trichoderma viride. The crude enzyme was chromatographed with ion-exchange reins of DEAE Sepharose CL-6B, Sepharose, S-Sepharose CL-6B and the resulting xylanase was turned out to be a single protein as 20KD hy SDS-polyacrylamide gel electrophoresis. The xylooligomers were obtained from xylan by incubation with the purified xylanase up to 50%. The ${\beta}$-xylosidase lost its activity completely by incubation of crude enzyme for 24hr with buffer solution of pH 2.8 at $27^{\circ}C$. And also, the xylooligomers were obtained from xylan as a main product by incubation with the crude enzyme treated with acidic buffer.

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Characterization of cell wall hydrolases induced by sugar starvation

  • Lee, Eun-Jeong;Koizumi, Nozomu
    • 한국식물생명공학회:학술대회논문집
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    • 한국식물생명공학회 2005년도 추계학술대회 및 한일 식물생명공학 심포지엄
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    • pp.371-374
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    • 2005
  • In our previous work in transcriptional regulation of sugar, expression of genes encoding putative glycosyl hydrolases in Arabidopsis was induced by sugar starvation. They were annotated as b-galactosidase (At5g56870), ${\beta}-xylosidase$ (At5g49360) and ${\beta}-glucosidase$ (At3g60140), which belong to glycosyl hydrolase family that has a catalytic domain of polysaccharides. From the primary structure of deduced amino acid sequence, they were predicted to localize to cell wall. Further investigation of these cell wall hydrolases implicated that cell wall polysaccharides provide metabolizable sugars to nutrient allocation under sugar starvation.

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국내산 침엽수 목분의 진탕배양에서 나타난 Fomitopsis palustris의 효소 활성 및 셀룰로오스 분해 (Enzyme Activities and Cellulose Degradation of Domestic Softwoods in Shaking Culture of Fomitopsis palustris)

  • 최두열;이영민;김영균;윤정준;김영숙
    • Journal of the Korean Wood Science and Technology
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    • 제35권6호
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    • pp.91-99
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    • 2007
  • 소나무, 낙엽송, 리기다소나무, 잣나무 등 국내산 침엽수 목분을 기질로 진탕배양했을 때 갈색부후균인 Fomitopsis palustris로부터 분비된 당 분해성 균체 외 효소는 Endoglucanase (EG), $\beta$-glucosidase (BGL) 및 $\beta$-1,4-xylosidase (BXL)와 함께 결정형 셀룰로오스를 분해하는 Cellobiohydrolase (CBH)도 활성을 갖은 것으로 나타났다. 4주간 배양에서 변재는 심재에 비해 큰 효소활성을 나타냈으나, 배양기간을 증가시킴으로써 효소활성이 커지는 것으로 밝혀져 효소에 의한 목질바이오매스 분해의 경우 심변재 혼합처리도 가능할 수 있음이 시사되었다. 그리고, 균체 의 단백질을 SDS-PAGE로 분석한 결과, 대부분의 수종에서 나타나는 효소의 단백질 패턴은 거의 유사한 것으로 나타나 효소를 이용한 목질계 바이오매스 분해의 경구 수종별 혼합처리도 가능함이 시사되었다. F. palustris에 의해 분해된 목분(60 mesh 통과) 셀룰로오스의 결정화도 감소율은 4주 배양에서 약 4.2~20.4%, 8주 배양에서 약 12.9~28.9% 수준으로 나타났다.

북구 이탄습지의 생지화학적 반응에 있어서 체외효소의 중요성-미량기체 발생량 및 용존유기탄소 동태와의 연관성에 대하여 (Importance of Extracellular Enzyme Activities in Northern Peatland Biogeochemistry-Possible Coupling with Trace Gas Emission and DOC Dynamics)

  • ;박석순;강호정
    • 생태와환경
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    • 제39권4호통권118호
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    • pp.435-444
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    • 2006
  • 세 종류의 이탄습지 (bog, fen, swamp)에서 탄수유기물 분해에 관여하는 일군의 체외 효소 활성도. 미량 기체 ($CO_2$$N_2O$), DOC 변화 등을 12개월에 걸쳐 측정하였다 ${\beta}-glucosidase$, cellobiohydrolase, ${\beta}-xylosidase$, N-acetylglucosaminidase 등이 각각 $0.008-0.066\;{\mu}mole\;g^{-1}\;min^{-1}$, $0.003-0.021\;{\mu}mole\;g^{-1}\;min^{-1}$, $0.003-0.016\;{\mu}mole\;g^{-1}\;min^{-1}$, $0.004-0.047\;{\mu}mole\;g^{-1}\;min^{-1}$ 범위의 활성도를 보였다. 전반적으로 swamp에서의 활성도가 가장 높았고, fen과 bog의 순서로 나타났다. 세 종류 습지의 자료를 모두 합쳤을 때, 효소의 활성도는 미량 기체의 발생량이나 가용한 탄소의 양과 유의한 양의 상관관계를 보였다. 또한, 4가지 효소 활성도의 평균값은 미량기체와 가용한 탄소량의 변화에 있어서 20-40% 정도의 변이를 설명할 수 있었다. 이 결과로 비추어, 유기탄소 무기화에 관여하는 효소는 북구 이탄습지에서 미량기체 발생과 DOC 동태에 중요한 역할을 하는 것으로 사료된다.

다양한 버섯 수확 후 배지로부터 목질섬유소 분해효소의 최적 추출 및 특성 (Optimal Extraction and Characteristics of Lignocellulytic Enzymes from Various Spent Mushroom Composts)

  • 임선화;이윤혜;강희완
    • 한국균학회지
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    • 제41권3호
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    • pp.160-166
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    • 2013
  • 느타리버섯(Pleurotus ostreatus), 큰느타리버섯(Pleurotus eryngii), 팽이버섯(Flammulina velvtipes)과 노루궁뎅이버섯(Hericium erinaceum), 느티만가닥버섯(Lyophyllum ulmarium), 노랑느타리버섯(Pleurotus cornucopiae), 잣버섯(Lentinus lepideus), 버들송이버섯(Agrocybe cylindracea)의 수확 후 배지 (spent mushroom compost, SMC)로부터 ${\alpha}$-amylase (EC 3.2.1.1), lignin peroxidase (EC 1.11.1.14), laccase (EC 1.10.3.2), xylanase (EC 3.2.1.8), ${\beta}$-xylosidase (EC 3.2.1.37), ${\beta}$-glucosidase (EC 3.2.1.21) 및 cellulase (EC 3.2.1.4)의 활성을 추출 buffer별로 조사하였다. 물과 0.25% Triton X-100가 효소 회수율이 높았으며 xylanase는 팽이버섯 SMC에서 153 U/g으로 가장 많이 생산되었으며 laccase는 큰느타리버섯 SMC에서 8.0 U/g로 가장 높았다. ${\alpha}$-amylase (3.6 U/g)와 cellulase (3.2 U/g)는 버들송이 SMC에서 가장 많이 생산되었다. 큰느타리버섯 SMC 추출물의 laccase와 cellulase 활성은 상용 효소와 필적하는 효소활성을 보여 산업적 이용 가능성을 시사하였다.

Cellulase Production in the Digestive Organs of Reticulitermes speratus, a Native Termite from Milyang, Korea

  • Lee, Young-Min;Kim, Yoon-Hee;Cho, Moon-Jung;Shin, Keum;Kim, Yeong-Suk
    • Journal of the Korean Wood Science and Technology
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    • 제38권5호
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    • pp.421-428
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    • 2010
  • This study investigated on enzyme production in the digestive organs of the native termite (Reticulitermes speratus) in Milyang, Korea. Four types of major cellulases [EG (endo-1,4-${\beta}$-glucanase), BGL (${\beta}$-glucosidase), CBH (cellobiohydrolase) and BXL (${\beta}$-1,4-xylosidase)] were present in the digestive organs of the termite. The strong enzyme activity for BGL was found from the native termite, and also shown that the enzyme was distributed in the salivary gland, foregut, and hindgut. BXL, which breaks down hemicellulose near the amorphous region, was detected mainly from salivary gland, foregut, and midgut. However, CBH was distributed mainly in the hindgut. Meanwhile, EG which degrades cellulose, was found mainly in the hindgut and salivary glands. These facts indicate that celluases production patterns are differ from different sites compare to the same species found in Japan, suggesting that enzyme production in the digestive organs of termites is changed according to their habitats.

Characterization of Two Algal Lytic Bacteria Associated with Management of the Cyanobacterium Anabaena flos-aquae

  • Kim, Jeong-Dong;Lee, Choul-Gyun
    • Biotechnology and Bioprocess Engineering:BBE
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    • 제11권5호
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    • pp.382-390
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    • 2006
  • Various microorganisms were isolated from the surface waters and sediments of eutrophic lakes and reservoirs in Korea to enable an investigation of bacteria having algal lytic activities against Anabaena flos-aquae when water blooming occurs and to study enzyme profiles of algal lytic bacteria. Two bacterial strains, AFK-07 and AFK-13, were cultured, characterized and identified as Acinetobacter johnsonii and Sinorhizobium sp., respectively. The A. johnsonii AFK-07 exhibited a high level of degradatory activities against A. flos-aquae, and produced alginase, caseinase, lipase, fucodian hydrolase, and laminarinase. Moreover, many kinds of glycosidase, such as ${\beta}-galactosidase,\;{\beta}-glucosidase,\;{\beta}-glucosaminidase,\;and\; {\beta}-xylosidase$, which hydrolyzed ${\beta}-O-glycosidic$ bonds, were found in cell-free extracts of A. johnsonii AFK-07. Other glycosidases such as ${\alpha}-galactosidase,\;{\alpha}-N-Ac-galactosidase,\;{\alpha}-mannosidase,\; and\;{\alpha}-L-fucosidase$, which cleave ${\alpha}-O-glycosidic$ bonds, were not identified in AFK-07. In the Sinorhizobium sp. AFK-13, the enzymes alginase, amylase, proteinase (caseinase and gelatinase), carboxymethyl-cellulase (CMCase), laminarinase, and lipase were notable. No glycosidase was produced in the AFK-13 strain. Therefore, the enzyme system of A. johnsonii AFK-07 had a more complex mechanism in place to degrade the cyanobacteria cell walls than did the enzyme system of Sinorhizobium sp. AFK-13. The polysaccharides or the peptidoglycans of A. flos-aquae may be hydrolyzed and metabolized to a range of easily utilized monosaccharides or other low molecular weight organic substances by strain AFK-07 of. A. johnsonii, while the products of polysaccharide degradation or peptidoglycans were more likely to be utilized by Sinorhizobium sp. AFK-13. These bacterial interactions may offer an alternative effective approach to controlling the water choking effects of summer blooms affecting our lakes and reservoirs.

Hydrolysis of Arabinoxylo-oligosaccharides by α-ʟ-Arabinofuranosidases and β-ᴅ-Xylosidase from Bifidobacterium dentium

  • Lee, Min-Jae;Kang, Yewon;Son, Byung Sam;Kim, Min-Jeong;Park, Tae Hyeon;Park, Damee;Kim, Tae-Jip
    • Journal of Microbiology and Biotechnology
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    • 제32권2호
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    • pp.187-194
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    • 2022
  • Two α-ʟ-arabinofuranosidases (BfdABF1 and BfdABF3) and a β-ᴅ-xylosidase (BfdXYL2) genes were cloned from Bifidobacterium dentium ATCC 27679, and functionally expressed in E. coli BL21(DE3). BfdABF1 showed the highest activity in 50 mM sodium acetate buffer at pH 5.0 and 25℃. This exo-enzyme could hydrolyze p-nitrophenyl arabinofuranoside, arabino-oligosaccharides (AOS), arabinoxylo-oligosaccharides (AXOS) such as 32-α-ʟ-arabinofuranosyl-xylobiose (A3X), and 23-α-ʟ-arabinofuranosyl-xylotriose (A2XX), whereas hardly hydrolyzed polymeric substrates such as debranched arabinan and arabinoxylans. BfdABF1 is a typical exo-ABF with the higher specific activity on the oligomeric substrates than the polymers. It prefers to α-(1,2)-ʟ-arabinofuranosidic linkages compared to α-(1,3)-linkages. Especially, BfdABF1 could slowly hydrolyze 23,33-di-α-ʟ-arabinofuranosyl-xylotriose (A2+3XX). Meanwhile, BfdABF3 showed the highest activity in sodium acetate at pH 6.0 and 50℃, and it has the exclusively high activities on AXOS such as A3X and A2XX. BfdABF3 mainly catalyzes the removal of ʟ-arabinose side chains from various AXOS. BfdXYL2 exhibited the highest activity in sodium citrate at pH 5.0 and 55℃, and it specifically hydrolyzed p-nitrophenyl xylopyranoside and xylo-oligosaccharides (XOS). Also, BfdXYL2 could slowly hydrolyze AOS and AXOS such as A3X. Based on the detailed hydrolytic modes of action of three exo-hydrolases (BfdABF1, BfdABF3, and BfdXYL2) from Bf. dentium, their probable roles in the hemiceullose-utilization system of Bf. dentium are proposed in the present study. These intracellular exo-hydrolases can synergistically produce ʟ-arabinose and ᴅ-xylose from various AOS, XOS, and AXOS.