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Volumn 36, Issue 5, 2013, Pages 555-565

Highly thermo-halo-alkali-stable β-1,4-endoxylanase from a novel polyextremophilic strain of Bacillus halodurans

Author keywords

Endoxylanase; Polyextremophilic; Response surface methodology; Saccharification; Thermo halo alkali stable

Indexed keywords

BACILLUS HALODURANS; ENDOXYLANASE; PLACKETT-BURMAN DESIGNS; POLYEXTREMOPHILIC; RESPONSE SURFACE METHODOLOGY; SUBMERGED FERMENTATION; THERMO-HALO-ALKALI-STABLE; XYLANASE PRODUCTIONS;

EID: 84877920158     PISSN: 16157591     EISSN: 16157605     Source Type: Journal    
DOI: 10.1007/s00449-012-0811-4     Document Type: Article
Times cited : (22)

References (49)
  • 1
    • 55849106319 scopus 로고    scopus 로고
    • Pretreatment: The key to unlocking low-cost cellulosic ethanol
    • 10.1002/bbb.49 1:CAS:528:DC%2BD1cXisVarurw%3D
    • Yang B, Wyman CE (2008) Pretreatment: the key to unlocking low-cost cellulosic ethanol. Biofuels Bioprod Bioref 2(1):26-40
    • (2008) Biofuels Bioprod Bioref , vol.2 , Issue.1 , pp. 26-40
    • Yang, B.1    Wyman, C.E.2
  • 2
    • 34548754522 scopus 로고    scopus 로고
    • Progress and challenges in enzyme development for biomass utilization
    • 1:STN:280:DC%2BD2srjtVeksA%3D%3D
    • Merino Sandra T, Cherry J (2007) Progress and challenges in enzyme development for biomass utilization. Adv Biochem Eng Biotechnol 108:95-120
    • (2007) Adv Biochem Eng Biotechnol , vol.108 , pp. 95-120
    • Merino Sandra, T.1    Cherry, J.2
  • 3
    • 0036386133 scopus 로고    scopus 로고
    • Enzymatic processing of crude xylooligomer solutions obtained by autohydrolysis of eucalyptus wood
    • 10.1081/FBT-120014321 1:CAS:528:DC%2BD38XotFOmurY%3D
    • Vazquez MJ, Alonso JL, Dominguez H, Parajo JC (2002) Enzymatic processing of crude xylooligomer solutions obtained by autohydrolysis of eucalyptus wood. Food Biotechnol 16(2):91-105
    • (2002) Food Biotechnol , vol.16 , Issue.2 , pp. 91-105
    • Vazquez, M.J.1    Alonso, J.L.2    Dominguez, H.3    Parajo, J.C.4
  • 4
    • 38049026251 scopus 로고    scopus 로고
    • The impact of dilute sulfuric acid on the selectivity of xylooligomer depolymerization to monomers
    • 10.1016/j.carres.2007.10.022 1:CAS:528:DC%2BD1cXotlSntQ%3D%3D
    • Kumar R, Wyman CE (2008) The impact of dilute sulfuric acid on the selectivity of xylooligomer depolymerization to monomers. Carbohydr Res 343(2):290-300
    • (2008) Carbohydr Res , vol.343 , Issue.2 , pp. 290-300
    • Kumar, R.1    Wyman, C.E.2
  • 6
    • 2942615497 scopus 로고    scopus 로고
    • Production, characterization and application of a thermostable polygalacturonase of a thermophilic mould Sporotrichum thermophile Apinis
    • 10.1016/j.biortech.2003.05.003 1:CAS:528:DC%2BD2cXks1GmtLs%3D
    • Kaur G, Kumar S, Satyanarayana T (2004) Production, characterization and application of a thermostable polygalacturonase of a thermophilic mould Sporotrichum thermophile Apinis. Bioresour Technol 94:239-243
    • (2004) Bioresour Technol , vol.94 , pp. 239-243
    • Kaur, G.1    Kumar, S.2    Satyanarayana, T.3
  • 7
    • 0022386956 scopus 로고
    • Microbial xylanolytic systems
    • 10.1016/0167-7799(85)90004-6 1:CAS:528:DyaL28XhtVGltLg%3D
    • Biely P (1985) Microbial xylanolytic systems. Trends Biotechnol 3:286-290
    • (1985) Trends Biotechnol , vol.3 , pp. 286-290
    • Biely, P.1
  • 8
    • 79961028996 scopus 로고    scopus 로고
    • Strategies of xylanase supplementation for an efficient saccharification and co-fermentation process from pretreated wheat straw
    • 10.1002/btpr.623 1:CAS:528:DC%2BC3MXhtValt7vE
    • Alvira P, Tomás-Pejó E, José M (2011) Strategies of xylanase supplementation for an efficient saccharification and co-fermentation process from pretreated wheat straw. Biotechnol Prog 27(4):944-950
    • (2011) Biotechnol Prog , vol.27 , Issue.4 , pp. 944-950
    • Alvira, P.1    Tomás-Pejó, E.2    José, M.3
  • 9
    • 12144282020 scopus 로고    scopus 로고
    • Xylanase, xylanase families and extremophilic xylanase
    • 10.1016/j.femsre.2004.06.005
    • Collin T, Gerday C, Feller G (2005) Xylanase, xylanase families and extremophilic xylanase. FEMS Microbiol Rev 29:3-23
    • (2005) FEMS Microbiol Rev , vol.29 , pp. 3-23
    • Collin, T.1    Gerday, C.2    Feller, G.3
  • 10
    • 0037300835 scopus 로고    scopus 로고
    • Purification and characterization of a cellulase-free xylanase of a moderate thermophile Bacillus licheniformis A99
    • 10.1023/A:1022527702400 1:CAS:528:DC%2BD3sXhsFKkurc%3D
    • Archana A, Satyanarayana T (2003) Purification and characterization of a cellulase-free xylanase of a moderate thermophile Bacillus licheniformis A99. World J Microbiol Biotechnol 19:53-57
    • (2003) World J Microbiol Biotechnol , vol.19 , pp. 53-57
    • Archana, A.1    Satyanarayana, T.2
  • 11
    • 0035092271 scopus 로고    scopus 로고
    • Thermophilic adaptation of proteins
    • 10.1080/20014091074174 1:CAS:528:DC%2BD3MXit1Cjur8%3D
    • Sterner R, Liebl W (2001) Thermophilic adaptation of proteins. Crit Rev Biochem Mol Biol 36:39-106
    • (2001) Crit Rev Biochem Mol Biol , vol.36 , pp. 39-106
    • Sterner, R.1    Liebl, W.2
  • 12
    • 0035098779 scopus 로고    scopus 로고
    • Hyperthermophilic enzymes; Sources, uses, and molecular mechanisms for thermostability
    • 10.1128/MMBR.65.1.1-43.2001 1:CAS:528:DC%2BD3MXisFyms74%3D
    • Vieille C, Zeikus GJ (2001) Hyperthermophilic enzymes; sources, uses, and molecular mechanisms for thermostability. Microbiol Mol Biol Rev 65:1-42
    • (2001) Microbiol Mol Biol Rev , vol.65 , pp. 1-42
    • Vieille, C.1    Zeikus, G.J.2
  • 13
    • 33751196772 scopus 로고    scopus 로고
    • Purification and characterization of an extracellular haloalkaline protease produced by moderately halophilic bacterium salinivibrio sp strain AF-2004
    • 10.1016/j.enzmictec.2006.04.006
    • Karbalai-Heidari HR, Ziaee AA, Schaller J, Amoozegar MA (2007) Purification and characterization of an extracellular haloalkaline protease produced by moderately halophilic bacterium salinivibrio sp strain AF-2004. Enzym Microb Technol 40:266-272
    • (2007) Enzym Microb Technol , vol.40 , pp. 266-272
    • Karbalai-Heidari, H.R.1    Ziaee, A.A.2    Schaller, J.3    Amoozegar, M.A.4
  • 14
    • 0035319086 scopus 로고    scopus 로고
    • Potential of halotolerant and halophilic microorganisms for biotechnology
    • 10.1007/s007920100184 1:CAS:528:DC%2BD3MXktVSnsbY%3D
    • Margesin R, Schinner S (2001) Potential of halotolerant and halophilic microorganisms for biotechnology. Extremophiles 5:73-83
    • (2001) Extremophiles , vol.5 , pp. 73-83
    • Margesin, R.1    Schinner, S.2
  • 15
    • 20444504291 scopus 로고    scopus 로고
    • Structural basis for the specificity of reducing-end xylose-releasing exo-oligoxylanse from Bacillus halodurans C-125
    • 10.1074/jbc.M413693200 1:CAS:528:DC%2BD2MXjsFOgtb4%3D
    • Fushinobu S, Hidaka M, Honda Y, Wakagi T, Shaoun H, Kitoka M (2005) Structural basis for the specificity of reducing-end xylose-releasing exo-oligoxylanse from Bacillus halodurans C-125. J Biol Chem 280:17180-17186
    • (2005) J Biol Chem , vol.280 , pp. 17180-17186
    • Fushinobu, S.1    Hidaka, M.2    Honda, Y.3    Wakagi, T.4    Shaoun, H.5    Kitoka, M.6
  • 16
    • 33748751574 scopus 로고    scopus 로고
    • A thermostable alkaline active endo-β-1-4-xylanase from Bacillus halodurans S7: Purification and characterization
    • 10.1016/j.enzmictec.2006.03.040 1:CAS:528:DC%2BD28XpvFGhtbw%3D
    • Mamo G, Hatti-Kaul R, Mattiasson B (2006) A thermostable alkaline active endo-β-1-4-xylanase from Bacillus halodurans S7: purification and characterization. Enzym Microb Technol 39:1492-1498
    • (2006) Enzym Microb Technol , vol.39 , pp. 1492-1498
    • Mamo, G.1    Hatti-Kaul, R.2    Mattiasson, B.3
  • 18
    • 29144507093 scopus 로고    scopus 로고
    • A marked enhancement in the production of a highly alkaline and thermostable pectinase by Bacillus pumilus dcsr1 in submerged fermentation by using statistical methods
    • 10.1016/j.biortech.2005.04.012 1:CAS:528:DC%2BD2MXhtlCnsrfJ
    • Sharma DC, Satyanarayana T (2006) A marked enhancement in the production of a highly alkaline and thermostable pectinase by Bacillus pumilus dcsr1 in submerged fermentation by using statistical methods. Bioresour Technol 97:727-733
    • (2006) Bioresour Technol , vol.97 , pp. 727-733
    • Sharma, D.C.1    Satyanarayana, T.2
  • 19
    • 0031194474 scopus 로고    scopus 로고
    • Xylanase production by thermophilic Bacillus lichenformis A99 in solid-state fermentation
    • 10.1016/S0141-0229(96)00207-4 1:CAS:528:DyaK2sXkt1Cjtr0%3D
    • Archana A, Satyanarayana T (1997) Xylanase production by thermophilic Bacillus lichenformis A99 in solid-state fermentation. Enzym Microb Technol 21:12-17
    • (1997) Enzym Microb Technol , vol.21 , pp. 12-17
    • Archana, A.1    Satyanarayana, T.2
  • 20
    • 0016177685 scopus 로고
    • Enzymatic hydrolysis of waste cellulose
    • 10.1002/bit.260161105 1:CAS:528:DyaE2MXmtVajsA%3D%3D
    • Mandels M, Hontz L, Nystrom J (1974) Enzymatic hydrolysis of waste cellulose. Biotechnol Bioeng 16:1471-1493
    • (1974) Biotechnol Bioeng , vol.16 , pp. 1471-1493
    • Mandels, M.1    Hontz, L.2    Nystrom, J.3
  • 21
    • 0001131698 scopus 로고
    • The design of optimum multifactorial experiments
    • 10.1093/biomet/33.4.305
    • Plackett RL, Burman JP (1946) The design of optimum multifactorial experiments. Biometrika 33:305-325
    • (1946) Biometrika , vol.33 , pp. 305-325
    • Plackett, R.L.1    Burman, J.P.2
  • 22
    • 2242495182 scopus 로고
    • Isolation and classification of alkalophilic microorganisms
    • K. Horikoshi (eds) Kodansha Limited Tokyo
    • Horikoshi K (1991) Isolation and classification of alkalophilic microorganisms. In: Horikoshi K (ed) Microorganisms in alkaline environments. Kodansha Limited, Tokyo, pp 15-24
    • (1991) Microorganisms in Alkaline Environments , pp. 15-24
    • Horikoshi, K.1
  • 23
    • 0021835929 scopus 로고
    • Two types of xylanases of alkalophilic Bacillus sp. No. C-125
    • 10.1139/m85-100 1:CAS:528:DyaL2MXksFShsbY%3D
    • Honda H, Kudo T, Ikura Y, Horikoshi K (1985) Two types of xylanases of alkalophilic Bacillus sp. No. C-125. Can J Microbiol 31:538-542
    • (1985) Can J Microbiol , vol.31 , pp. 538-542
    • Honda, H.1    Kudo, T.2    Ikura, Y.3    Horikoshi, K.4
  • 24
    • 80053188771 scopus 로고    scopus 로고
    • Applicability of thermo-alkali-stable and cellulase-free xylanase from a novel thermo-halo-alkaliphilic Bacillus halodurans in producing xylooligosaccharides
    • 10.1007/s10529-011-0698-1 1:CAS:528:DC%2BC3MXht1eitb3K
    • Kumar V, Satyanarayana T (2011) Applicability of thermo-alkali-stable and cellulase-free xylanase from a novel thermo-halo-alkaliphilic Bacillus halodurans in producing xylooligosaccharides. Biotechnol Lett 33:2279-2285
    • (2011) Biotechnol Lett , vol.33 , pp. 2279-2285
    • Kumar, V.1    Satyanarayana, T.2
  • 25
    • 2342436107 scopus 로고    scopus 로고
    • Biotechnological advantages of laboratory scale solid-state fermentation with fungi
    • 10.1007/s00253-003-1504-3
    • Hölker U, Höfer M, Lenz MJ (2004) Biotechnological advantages of laboratory scale solid-state fermentation with fungi. Appl Microbiol Biotechnol 64:175-186
    • (2004) Appl Microbiol Biotechnol , vol.64 , pp. 175-186
    • Hölker, U.1    Höfer, M.2    Lenz, M.J.3
  • 26
    • 36749038823 scopus 로고    scopus 로고
    • Cost-effective xylanase production from free and immobilized Bacillus pumilus strain MK001 and its application in saccharification of Prosopis juliflora
    • 10.1016/j.bej.2007.06.009 1:CAS:528:DC%2BD2sXhsVWjsbjF
    • Kapoor M, Nair LM, Chander Kuhad R (2008) Cost-effective xylanase production from free and immobilized Bacillus pumilus strain MK001 and its application in saccharification of Prosopis juliflora. Biochem Eng J 38:88-97
    • (2008) Biochem Eng J , vol.38 , pp. 88-97
    • Kapoor, M.1    Nair, L.M.2    Chander Kuhad, R.3
  • 27
    • 33750385638 scopus 로고    scopus 로고
    • Optimization of culture variables for improving glucoamylase production by alginate-trapped Thermomucor indicae-seudaticae using statistical methods
    • 10.1016/j.biortech.2006.05.019 1:CAS:528:DC%2BD28XhtFKms7jO
    • Kumar P, Satyanarayana T (2007) Optimization of culture variables for improving glucoamylase production by alginate-trapped Thermomucor indicae-seudaticae using statistical methods. Bioresour Technol 98:1252-1259
    • (2007) Bioresour Technol , vol.98 , pp. 1252-1259
    • Kumar, P.1    Satyanarayana, T.2
  • 28
    • 79954800374 scopus 로고    scopus 로고
    • 2+-independent α-amylase by Bacillus acidicola
    • 10.1016/j.jbiosc.2011.01.004 1:CAS:528:DC%2BC3MXpvFeqtrs%3D
    • 2+-independent α-amylase by Bacillus acidicola. J Biosci Bioeng 111(5):550-553
    • (2011) J Biosci Bioeng , vol.111 , Issue.5 , pp. 550-553
    • Sharma, A.1    Satyanarayana, T.2
  • 29
    • 26844534995 scopus 로고    scopus 로고
    • Application of response surface methodology to optimize the process variables for reactive red and acid brown dye removal using a novel adsorbent
    • 10.1016/j.dyepig.2005.02.004 1:CAS:528:DC%2BD2MXhtVCktrbN
    • Ravi kumar K, Ramalingam S, Krishnan S, Balu K (2006) Application of response surface methodology to optimize the process variables for reactive red and acid brown dye removal using a novel adsorbent. Dyes Pigm 70:18-26
    • (2006) Dyes Pigm , vol.70 , pp. 18-26
    • Ravi Kumar, K.1    Ramalingam, S.2    Krishnan, S.3    Balu, K.4
  • 30
    • 80053970835 scopus 로고    scopus 로고
    • Xylanase production using agro residue in solid-state fermentation from Bacillus pumilus ASH for biodelignification of wheat straw pulp
    • 10.1007/s10532-011-9470-4 1:CAS:528:DC%2BC3MXhtlSqtrnE
    • Garg G, Mahajan R, Kaur A, Sharma J (2011) Xylanase production using agro residue in solid-state fermentation from Bacillus pumilus ASH for biodelignification of wheat straw pulp. Biodegradation 22:1143-1154
    • (2011) Biodegradation , vol.22 , pp. 1143-1154
    • Garg, G.1    Mahajan, R.2    Kaur, A.3    Sharma, J.4
  • 31
    • 79953780105 scopus 로고    scopus 로고
    • Optimization of cellulase-free xylanase production by thermophilic Streptomyces thermovulgaris TISTR1948 through Plackett-Burman and response surface methodological approaches
    • 10.1271/bbb.100756 1:CAS:528:DC%2BC3MXltF2lsLw%3D
    • Chaiyaso T, Kuntiya A, Techapun C, Leksawasdi N, Seesuriyachan P, Hanmoungjai P (2011) Optimization of cellulase-free xylanase production by thermophilic Streptomyces thermovulgaris TISTR1948 through Plackett-Burman and response surface methodological approaches. Biosci Biotechnol Biochem 75:531-537
    • (2011) Biosci Biotechnol Biochem , vol.75 , pp. 531-537
    • Chaiyaso, T.1    Kuntiya, A.2    Techapun, C.3    Leksawasdi, N.4    Seesuriyachan, P.5    Hanmoungjai, P.6
  • 32
    • 33947509518 scopus 로고    scopus 로고
    • Alkali-thermostable and cellulose-free xylanase production by an extreme thermophile Geobacillus thermoleovorans
    • 10.1007/s11274-006-9250-1 1:CAS:528:DC%2BD2sXjtlCisrg%3D
    • Sharma A, Adhikari S, Satyanarayana T (2007) Alkali-thermostable and cellulose-free xylanase production by an extreme thermophile Geobacillus thermoleovorans. World J Microbiol Biotechnol 23:483-490
    • (2007) World J Microbiol Biotechnol , vol.23 , pp. 483-490
    • Sharma, A.1    Adhikari, S.2    Satyanarayana, T.3
  • 33
    • 77956062586 scopus 로고    scopus 로고
    • Production and properties of xylanases from Aspergillus terricola Marchal and Aspergillus ochraceus and their use in cellulose pulp Bleaching
    • 10.1007/s00449-009-0403-0 1:CAS:528:DC%2BC3cXhtVSmurjO
    • Michelin M, Peixoto-Nogueira SC, Betini JHA, da Silva TM, Jorge JA, Terenzi HF, Polizeli MLTM (2010) Production and properties of xylanases from Aspergillus terricola Marchal and Aspergillus ochraceus and their use in cellulose pulp Bleaching. Bioprocess Biosyst Eng 33:813-821
    • (2010) Bioprocess Biosyst Eng , vol.33 , pp. 813-821
    • Michelin, M.1    Peixoto-Nogueira, S.C.2    Betini, J.H.A.3    Da Silva, T.M.4    Jorge, J.A.5    Terenzi, H.F.6    Polizeli, M.7
  • 34
    • 84872331479 scopus 로고    scopus 로고
    • Process optimization of xylanase production using cheap solid substrate by Trichoderma reesei SAF3 and study on the alteration of behavioural properties of enzyme obtained from SSF and SmF
    • doi: 10.1007/s00449-012-0761-x
    • Kar S, Gauri SS, Das A, Jana A, Maity C, Mandal A, Mohapatra PKD, Pati R, Mondal KC (2012) Process optimization of xylanase production using cheap solid substrate by Trichoderma reesei SAF3 and study on the alteration of behavioural properties of enzyme obtained from SSF and SmF. Bioprocess Biosyst Eng. doi: 10.1007/s00449-012-0761-x
    • (2012) Bioprocess Biosyst Eng.
    • Kar, S.1    Gauri, S.S.2    Das, A.3    Jana, A.4    Maity, C.5    Mandal, A.6    Mohapatra, P.K.D.7    Pati, R.8    Mondal, K.C.9
  • 35
    • 0038814320 scopus 로고    scopus 로고
    • Why whole grains are protective: Biological mechanisms
    • 10.1079/PNS2002221 1:CAS:528:DC%2BD3sXjslyhtbk%3D
    • Slavin J (2003) Why whole grains are protective: biological mechanisms. Proc Nutr Soc 62:129-134
    • (2003) Proc Nutr Soc , vol.62 , pp. 129-134
    • Slavin, J.1
  • 38
    • 0344406096 scopus 로고    scopus 로고
    • Three-dimensional structures of thermophilic beta-1,4-xylanases from Chaetomium thermophilum and Nonomuraea flexuosa. Comparison of twelve xylanases in relation to their thermal stability
    • 10.1046/j.1432-1033.2003.03496.x 1:CAS:528:DC%2BD3sXivFWnsLk%3D
    • Hakulinen N, Turunen O, Janis J, Leisola M, Rouvinen J (2003) Three-dimensional structures of thermophilic beta-1,4-xylanases from Chaetomium thermophilum and Nonomuraea flexuosa. Comparison of twelve xylanases in relation to their thermal stability. Eur J Biochem 270:1399-1412
    • (2003) Eur J Biochem , vol.270 , pp. 1399-1412
    • Hakulinen, N.1    Turunen, O.2    Janis, J.3    Leisola, M.4    Rouvinen, J.5
  • 39
    • 0036217687 scopus 로고    scopus 로고
    • Engineering of multiple arginines into the Ser/Thr surface of Trichoderma reesei endo-1, 4-beta-xylanase II increases the thermotolerance and shifts the pH optimum towards alkaline pH
    • 10.1093/protein/15.2.141 1:CAS:528:DC%2BD38XivFKlsLc%3D
    • Turunen O, Vuorio M, Fenel F, Leisola M (2002) Engineering of multiple arginines into the Ser/Thr surface of Trichoderma reesei endo-1, 4-beta-xylanase II increases the thermotolerance and shifts the pH optimum towards alkaline pH. Protein Eng 15:141-145
    • (2002) Protein Eng , vol.15 , pp. 141-145
    • Turunen, O.1    Vuorio, M.2    Fenel, F.3    Leisola, M.4
  • 40
    • 0029008857 scopus 로고
    • Two extremely thermostable xylanases of the hyperthermophilic bacterium Thermotoga maritima MSB8
    • 1:CAS:528:DyaK2MXlsFykt78%3D
    • Winterhalter C, Liebel W (1995) Two extremely thermostable xylanases of the hyperthermophilic bacterium Thermotoga maritima MSB8. Appl Environ Microbiol 61(5):1810-1815
    • (1995) Appl Environ Microbiol , vol.61 , Issue.5 , pp. 1810-1815
    • Winterhalter, C.1    Liebel, W.2
  • 41
    • 0029916417 scopus 로고    scopus 로고
    • The multidomain xylanase A of the hyperthermophilic bacterium Thermotoga neapolitana is extremely thermoresistant
    • 10.1007/s002530050678 1:CAS:528:DyaK28XitVCru7k%3D
    • Zverlov V, Piotukh K, Dakhova O, Velikodvorskaya G, Borriss R (1996) The multidomain xylanase A of the hyperthermophilic bacterium Thermotoga neapolitana is extremely thermoresistant. Appl Microbiol Biotechnol 45:245-247
    • (1996) Appl Microbiol Biotechnol , vol.45 , pp. 245-247
    • Zverlov, V.1    Piotukh, K.2    Dakhova, O.3    Velikodvorskaya, G.4    Borriss, R.5
  • 42
    • 0034695422 scopus 로고    scopus 로고
    • The tertiary structure at 1.59 AËš resolution and the proposed amino acid sequence of a family-11 xylanase from the thermophilic fungus Paecilomyces variotii Bainier
    • 10.1006/jmbi.1999.3348
    • Kumar PR, Eswaramoorthy S, Vithayathil PJ, Viswamitra MA (2000) The tertiary structure at 1.59 AËš resolution and the proposed amino acid sequence of a family-11 xylanase from the thermophilic fungus Paecilomyces variotii Bainier. J Mol Biol 295:58-593
    • (2000) J Mol Biol , vol.295 , pp. 58-593
    • Kumar, P.R.1    Eswaramoorthy, S.2    Vithayathil, P.J.3    Viswamitra, M.A.4
  • 43
    • 0035370202 scopus 로고    scopus 로고
    • A combination of weakly stabilizing mutations with a disulfide bridge in the alpha-helix region of Trichoderma reesei endo-1, 4-beta-xylanase II increases the thermal stability through synergism
    • 10.1016/S0168-1656(01)00253-X 1:CAS:528:DC%2BD3MXjslSls70%3D
    • Turunen O, Etuaho K, Fenel F, Vehmaanpera J, Wu X, Rouvinen J, Leisola M (2001) A combination of weakly stabilizing mutations with a disulfide bridge in the alpha-helix region of Trichoderma reesei endo-1, 4-beta-xylanase II increases the thermal stability through synergism. J Biotechnol 88:37-46
    • (2001) J Biotechnol , vol.88 , pp. 37-46
    • Turunen, O.1    Etuaho, K.2    Fenel, F.3    Vehmaanpera, J.4    Wu, X.5    Rouvinen, J.6    Leisola, M.7
  • 44
    • 77956170113 scopus 로고    scopus 로고
    • Production of novel halo-alkali-thermo-stable xylanase by a newly isolated moderately halophilic and alkali-tolerant Gracilibacillus sp TSCPVG
    • 10.1016/j.procbio.2010.07.012 1:CAS:528:DC%2BC3cXhtV2gtL3F
    • Giridhar PV, Chandra TS (2010) Production of novel halo-alkali-thermo- stable xylanase by a newly isolated moderately halophilic and alkali-tolerant Gracilibacillus sp TSCPVG. Process Biochem 45(10):1730-1737
    • (2010) Process Biochem , vol.45 , Issue.10 , pp. 1730-1737
    • Giridhar, P.V.1    Chandra, T.S.2
  • 45
    • 79958772678 scopus 로고    scopus 로고
    • Characterization of a novel GH10 thermostable, halophilic xylanase from the marine bacterium Thermoanaerobacterium saccharolyticum NTOU1
    • 10.1007/s10529-011-0579-7 1:CAS:528:DC%2BC3MXnsVequr0%3D
    • Hung KS, Liu SM, Fang TY, Tzou WS, Lin FP, Sun KH, Tang SJ (2011) Characterization of a novel GH10 thermostable, halophilic xylanase from the marine bacterium Thermoanaerobacterium saccharolyticum NTOU1. Biotechnol Lett 33:1441-1447
    • (2011) Biotechnol Lett , vol.33 , pp. 1441-1447
    • Hung, K.S.1    Liu, S.M.2    Fang, T.Y.3    Tzou, W.S.4    Lin, F.P.5    Sun, K.H.6    Tang, S.J.7
  • 46
    • 3042825524 scopus 로고    scopus 로고
    • Purification and characterization of two extremely halotolerant xylanases from a novel halophilic bacterium
    • 10.1007/s00792-003-0342-7 1:CAS:528:DC%2BD3sXnslSnsbk%3D
    • Wejse PL, Ingvorsen K, Mortensen KK (2003) Purification and characterization of two extremely halotolerant xylanases from a novel halophilic bacterium. Extremophiles 7:423-443
    • (2003) Extremophiles , vol.7 , pp. 423-443
    • Wejse, P.L.1    Ingvorsen, K.2    Mortensen, K.K.3
  • 47
    • 0028414129 scopus 로고
    • Catalytic properties and potential of an extracellular protease from an extreme halophile
    • 10.1016/0141-0229(94)90165-1 1:CAS:528:DyaK2cXkslKku7c%3D
    • Ryu K, Kim J, Dordick JS (1994) Catalytic properties and potential of an extracellular protease from an extreme halophile. Enzyme Microb Technol 16:266-275
    • (1994) Enzyme Microb Technol , vol.16 , pp. 266-275
    • Ryu, K.1    Kim, J.2    Dordick, J.S.3
  • 48
    • 45449090225 scopus 로고    scopus 로고
    • Xylanase production by Burkholderia sp. DMAX strain under solid state fermentation using distillery spent wash
    • 10.1016/j.biortech.2008.02.009 1:CAS:528:DC%2BD1cXns1aks7g%3D
    • Mohana S, Shah A, Divecha J, Madamwar D (2008) Xylanase production by Burkholderia sp. DMAX strain under solid state fermentation using distillery spent wash. Bioresour Technol 99(16):7553-7564
    • (2008) Bioresour Technol , vol.99 , Issue.16 , pp. 7553-7564
    • Mohana, S.1    Shah, A.2    Divecha, J.3    Madamwar, D.4
  • 49
    • 84655163970 scopus 로고    scopus 로고
    • The family II carbohydrate-binding module of xylanase CflXyn11A from Cellulomonas flavigena increases the synergy with cellulase TrCel7B from Trichoderma reesei during the hydrolysis of sugar cane bagasse
    • 10.1016/j.biortech.2011.11.068
    • Orozco PP, Hernández AS, Rosengren A, Lara MEH, Stålbrand H (2012) The family II carbohydrate-binding module of xylanase CflXyn11A from Cellulomonas flavigena increases the synergy with cellulase TrCel7B from Trichoderma reesei during the hydrolysis of sugar cane bagasse. Bioresour Technol 104:622-630
    • (2012) Bioresour Technol , vol.104 , pp. 622-630
    • Orozco, P.P.1    Hernández, A.S.2    Rosengren, A.3    Lara, M.E.H.4    Stålbrand, H.5


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