메뉴 건너뛰기




Volumn 21, Issue 8, 2011, Pages 861-868

Cloning, expression, and characterization of a new Xylanase from alkalophilic paenibacillus sp. 12-11

Author keywords

Alkaline xylanase; Escherichia coli; Paenibacillus sp.; Protease resistance

Indexed keywords

ARABINOXYLAN; BEECHWOOD XYLAN; BIRCHWOOD XYLAN; CARBOHYDRATE; OAT SPELT XYLAN; PROTEINASE; RECOMBINANT ENZYME; UNCLASSIFIED DRUG; WHEAT ARABINOXYLAN; XYLAN; XYLAN ENDO 1,3 BETA XYLOSIDASE; XYLOBIOSE; XYLOSE;

EID: 80052290323     PISSN: 10177825     EISSN: 17388872     Source Type: Journal    
DOI: 10.4014/jmb.1102.02024     Document Type: Article
Times cited : (21)

References (40)
  • 1
    • 0032965966 scopus 로고    scopus 로고
    • Application of enzymes in the pulp and paper industry
    • Bajpai, P. 1999. Application of enzymes in the pulp and paper industry. Biotechnol. Prog. 15: 147-157.
    • (1999) Biotechnol. Prog , vol.15 , pp. 147-157
    • Bajpai, P.1
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72: 248-254.
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 4
    • 33846610642 scopus 로고    scopus 로고
    • Improvement of dough rheology, bread quality and bread shelf-life by enzymes combination
    • Caballero, P. A., M. Gómez, and C. M. Rosell. 2007. Improvement of dough rheology, bread quality and bread shelf-life by enzymes combination. J. Food Process Eng. 81: 42-53.
    • (2007) J. Food Process Eng , vol.81 , pp. 42-53
    • Caballero, P.A.1    Gómez, M.2    Rosell, C.M.3
  • 5
    • 0033165970 scopus 로고    scopus 로고
    • Production, partial characterization and use of fungal cellulase-free xylanases in pulp bleaching
    • Christov, L. P., G. Szakacs, and H. Balakrishnan. 1999. Production, partial characterization and use of fungal cellulase-free xylanases in pulp bleaching. Process Biochem. 34: 511-517.
    • (1999) Process Biochem , vol.34 , pp. 511-517
    • Christov, L.P.1    Szakacs, G.2    Balakrishnan, H.3
  • 6
    • 12144282020 scopus 로고    scopus 로고
    • Xylanases, xylanase families and extremophilic xylanases
    • Collins, T., C. Gerday, and G. Feller. 2005. Xylanases, xylanase families and extremophilic xylanases. FEMS Microbiol. Rev. 29: 3-23.
    • (2005) FEMS Microbiol. Rev , vol.29 , pp. 3-23
    • Collins, T.1    Gerday, C.2    Feller, G.3
  • 7
    • 0037688239 scopus 로고    scopus 로고
    • Characterization of a Paenibacillus cell-associated xylanase with high activity on aryl-xylosides: A new subclass of family 10 xylanases
    • Gallardo, O., P. Diaz, and F. I. J. Pastor. 2003. Characterization of a Paenibacillus cell-associated xylanase with high activity on aryl-xylosides: A new subclass of family 10 xylanases. Appl. Microbiol. Biotechnol. 61: 226-233.
    • (2003) Appl. Microbiol. Biotechnol , vol.61 , pp. 226-233
    • Gallardo, O.1    Diaz, P.2    Pastor, F.I.J.3
  • 8
    • 0029176314 scopus 로고
    • Cloning, sequencing, and expression of a xylanase gene from the extreme thermophile Dictyoglomus thermophilum Rt46B. 1 and activity of the enzyme on fiber-bound substrate
    • Gibbs, M. D., R. A. Reeves, and P. L. Bergquist. 1995. Cloning, sequencing, and expression of a xylanase gene from the extreme thermophile Dictyoglomus thermophilum Rt46B. 1 and activity of the enzyme on fiber-bound substrate. Appl. Environ. Microbiol. 61: 4403-4408.
    • (1995) Appl. Environ. Microbiol , vol.61 , pp. 4403-4408
    • Gibbs, M.D.1    Reeves, R.A.2    Bergquist, P.L.3
  • 9
    • 70349685126 scopus 로고    scopus 로고
    • Gene cloning, expression and characterization of a new cold-active and salt-tolerant endo-β-1,4-xylanase from marine Glaciecola mesophila KMM 241
    • Guo, B., X. Chen, C. Sun, B. Zhou, and Y. Zhang. 2009. Gene cloning, expression and characterization of a new cold-active and salt-tolerant endo-β-1,4-xylanase from marine Glaciecola mesophila KMM 241. Appl. Microbiol. Biotechnol. 84: 1107-1115.
    • (2009) Appl. Microbiol. Biotechnol , vol.84 , pp. 1107-1115
    • Guo, B.1    Chen, X.2    Sun, C.3    Zhou, B.4    Zhang, Y.5
  • 10
    • 0029929874 scopus 로고    scopus 로고
    • Updating the sequence-based classification of glycosyl hydrolases
    • Henrissat, B. and A. Bairoch. 1996. Updating the sequence-based classification of glycosyl hydrolases. Biochem. J. 316: 695-696.
    • (1996) Biochem. J , vol.316 , pp. 695-696
    • Henrissat, B.1    Bairoch, A.2
  • 11
    • 29944447809 scopus 로고    scopus 로고
    • Cloning, sequencing and expression of the xylanase gene from a Bacillus subtilis strain B10 in Escherichia coli
    • Huang, J., G. Wang, and L. Xiao. 2006. Cloning, sequencing and expression of the xylanase gene from a Bacillus subtilis strain B10 in Escherichia coli. Bioresour. Technol. 97: 802-808.
    • (2006) Bioresour. Technol , vol.97 , pp. 802-808
    • Huang, J.1    Wang, G.2    Xiao, L.3
  • 12
    • 77954382503 scopus 로고    scopus 로고
    • Cloning and characterization of a xylanase, KRICT PX1 from the strain Paenibacillus sp
    • Hwang, I. T., H. K. Lim, H. Y. Song, S. J. Cho, J. S. Chang, and N. J. Park. 2010. Cloning and characterization of a xylanase, KRICT PX1 from the strain Paenibacillus sp. HPL-001. Biotechnol. Adv. 28: 594-601.
    • (2010) HPL-001. Biotechnol. Adv , vol.28 , pp. 594-601
    • Hwang, I.T.1    Lim, H.K.2    Song, H.Y.3    Cho, S.J.4    Chang, J.S.5    Park, N.J.6
  • 13
    • 77955170842 scopus 로고    scopus 로고
    • Novel intracellular GH10 xylanase from Cohnella laeviribosi HY-21: Biocatalytic properties and alterations of substrate specificities by site-directed mutagenesis of Trp residues
    • Kim, D. Y., M. K. Han, H. W. Oh, K. S. Bae, T. S. Jeong, S. U. Kim, et al. 2010. Novel intracellular GH10 xylanase from Cohnella laeviribosi HY-21: Biocatalytic properties and alterations of substrate specificities by site-directed mutagenesis of Trp residues. Bioresour. Technol. 101: 8814-8821.
    • (2010) Bioresour. Technol , vol.101 , pp. 8814-8821
    • Kim, D.Y.1    Han, M.K.2    Oh, H.W.3    Bae, K.S.4    Jeong, T.S.5    Kim, S.U.6
  • 14
    • 33947706813 scopus 로고    scopus 로고
    • Paenibacillus campinasensis BL11: A wood materialutilizing bacterial strain isolated from black liquor
    • Ko, C. H., W. L. Chen, C. H. Tsai, W. N. Jane, C. C. Liu, and J. Tu. 2007. Paenibacillus campinasensis BL11: A wood materialutilizing bacterial strain isolated from black liquor. Bioresour. Technol. 98: 2727-2733.
    • (2007) Bioresour. Technol , vol.98 , pp. 2727-2733
    • Ko, C.H.1    Chen, W.L.2    Tsai, C.H.3    Jane, W.N.4    Liu, C.C.5    Tu, J.6
  • 15
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 16
    • 0034071946 scopus 로고    scopus 로고
    • Cloning, expression and nucleotide sequences of two xylanase genes from Paenibacillus sp
    • Lee, H., D. Shin, N. Cho, H. Kim, S. Shin, S. Im, H. Blaise Lee, S. Chun, and S. Bai. 2000. Cloning, expression and nucleotide sequences of two xylanase genes from Paenibacillus sp. Biotechnol. Lett. 22: 387-392.
    • (2000) Biotechnol. Lett , vol.22 , pp. 387-392
    • Lee, H.1    Shin, D.2    Cho, N.3    Kim, H.4    Shin, S.5    Im, S.6    Blaise Lee, H.7    Chun, S.8    Bai, S.9
  • 17
    • 48349109120 scopus 로고    scopus 로고
    • Cloning, expression, and characterization of a new xylanase with broad temperature adaptability from Streptomyces sp
    • Li, N., K. Meng, Y. Wang, P. Shi, H. Luo, Y. Bai, P. Yang, and B. Yao. 2008. Cloning, expression, and characterization of a new xylanase with broad temperature adaptability from Streptomyces sp. S9. Appl. Microbiol. Biotechnol. 80: 231-240.
    • (2008) S9. Appl. Microbiol. Biotechnol , vol.80 , pp. 231-240
    • Li, N.1    Meng, K.2    Wang, Y.3    Shi, P.4    Luo, H.5    Bai, Y.6    Yang, P.7    Yao, B.8
  • 18
    • 33751330608 scopus 로고
    • The determination of enzyme dissociation constants
    • Lineweaver, H. and D. Burk. 1934. The determination of enzyme dissociation constants. J. Am. Chem. Soc. 56: 658-666.
    • (1934) J. Am. Chem. Soc , vol.56 , pp. 658-666
    • Lineweaver, H.1    Burk, D.2
  • 19
    • 3242759047 scopus 로고    scopus 로고
    • Computational analysis of responsible dipeptides for optimum pH in G/11 xylanase
    • Liu, L., X. Li, and W. Shao. 2004 Computational analysis of responsible dipeptides for optimum pH in G/11 xylanase. Biochem. Biophys. Res. Commun. 321: 391-396.
    • (2004) Biochem. Biophys. Res. Commun , vol.321 , pp. 391-396
    • Liu, L.1    Li, X.2    Shao, W.3
  • 20
    • 0028949381 scopus 로고
    • Thermal asymmetric interlaced PCR: Automatable amplification and sequencing of insert end fragments from P1 and YAC clones for chromosome walking
    • Liu, Y. and R. F. Whittier. 1995. Thermal asymmetric interlaced PCR: Automatable amplification and sequencing of insert end fragments from P1 and YAC clones for chromosome walking. Genomics 25: 674-681.
    • (1995) Genomics , vol.25 , pp. 674-681
    • Liu, Y.1    Whittier, R.F.2
  • 21
    • 0000491882 scopus 로고
    • Xylanases and their application in bakery
    • Progress In Biotechnology, No. 7. Elsevier Science Publishers. In J. Visser, M. A. Kusters van Someren, G. Beldman, and A. G. J. Voragen (eds.), Amsterdam, The Netherlands
    • Maat, J., M. Roza, J. Verbakel, H. Stam, M. J. Santos Da Silva, M. Bosse, et al. 1992. Xylanases and their application in bakery, pp. 349-360. In J. Visser, M. A. Kusters van Someren, G. Beldman, and A. G. J. Voragen (eds.). Xylans and Xylanases. Progress in Biotechnology, No. 7. Elsevier Science Publishers, Amsterdam, The Netherlands.
    • (1992) Xylans and Xylanases , pp. 349-360
    • Maat, J.1    Roza, M.2    Verbakel, J.3    Stam, H.4    Santos da Silva, M.J.5    Bosse, M.6
  • 22
    • 33748751574 scopus 로고    scopus 로고
    • A thermostable alkaline active endo-β-1-4-xylanase from Bacillus halodurans S7: Purification and characterization
    • Mamo, G., R. Hatti-Kaul, and B. Mattiasson. 2006. A thermostable alkaline active endo-β-1-4-xylanase from Bacillus halodurans S7: Purification and characterization. Enzyme Microb. Technol. 39: 1492-1498.
    • (2006) Enzyme Microb. Technol , vol.39 , pp. 1492-1498
    • Mamo, G.1    Hatti-Kaul, R.2    Mattiasson, B.3
  • 23
    • 67651236276 scopus 로고    scopus 로고
    • An alkaline active xylanase: Insights into mechanisms of high pH catalytic adaptation
    • Mamo, G., M. Thunnissen, R. Hatti-Kaul, and B. Mattiasson. 2009. An alkaline active xylanase: Insights into mechanisms of high pH catalytic adaptation. Biochimie 91: 1187-1196.
    • (2009) Biochimie , vol.91 , pp. 1187-1196
    • Mamo, G.1    Thunnissen, M.2    Hatti-Kaul, R.3    Mattiasson, B.4
  • 24
    • 33746528621 scopus 로고    scopus 로고
    • Crystal structures of native and xylosaccharide-bound alkali thermostable xylanase from an alkalophilic Bacillus sp. NG-27: Structural insights into alkalophilicity and implications for adaptation to polyextreme conditions
    • Manikandan, K., A. Bhardwaj, N. Gupta, N. K. Lokanath, A. Ghosh, V. S. Reddy, and S. Ramakumar. 2006. Crystal structures of native and xylosaccharide-bound alkali thermostable xylanase from an alkalophilic Bacillus sp. NG-27: Structural insights into alkalophilicity and implications for adaptation to polyextreme conditions. Protein Sci. 15: 1951-1960.
    • (2006) Protein Sci , vol.15 , pp. 1951-1960
    • Manikandan, K.1    Bhardwaj, A.2    Gupta, N.3    Lokanath, N.K.4    Ghosh, A.5    Reddy, V.S.6    Ramakumar, S.7
  • 25
    • 64249099161 scopus 로고    scopus 로고
    • Expression of an alkalo-tolerant fungal xylanase enhanced by directed evolution in Pichia pastoris and Escherichia coli
    • Mchunu, N. P., S. Singh, and K. Permaul. 2009. Expression of an alkalo-tolerant fungal xylanase enhanced by directed evolution in Pichia pastoris and Escherichia coli. J. Biotechnol. 141: 26-30.
    • (2009) J. Biotechnol , vol.141 , pp. 26-30
    • McHunu, N.P.1    Singh, S.2    Permaul, K.3
  • 26
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for determination of reducing sugar
    • Miller, G. L. 1959. Use of dinitrosalicylic acid reagent for determination of reducing sugar. Anal. Chem. 31: 426-428.
    • (1959) Anal. Chem , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 27
    • 15544371286 scopus 로고    scopus 로고
    • Comparison of SYTO9 and SYBR Green I for real-time polymerase chain reaction and investigation of the effect of dye concentration on amplification and DNA melting curve analysis
    • Monis, P. T., S. Giglio, and C. P. Saint. 2005. Comparison of SYTO9 and SYBR Green I for real-time polymerase chain reaction and investigation of the effect of dye concentration on amplification and DNA melting curve analysis. Anal. Biochem. 340: 24-34.
    • (2005) Anal. Biochem , vol.340 , pp. 24-34
    • Monis, P.T.1    Giglio, S.2    Saint, C.P.3
  • 28
    • 0345791436 scopus 로고    scopus 로고
    • Scouring of flax rove with the aid of enzymes
    • Ossola, M. and Y. M. Galante. 2004. Scouring of flax rove with the aid of enzymes. Enzyme Microb. Technol. 34: 177-186.
    • (2004) Enzyme Microb. Technol , vol.34 , pp. 177-186
    • Ossola, M.1    Galante, Y.M.2
  • 29
    • 77950340101 scopus 로고    scopus 로고
    • A xylanase with broad pH and temperature adaptability from Streptomyces megasporus DSM 41476, and its potential application in brewing industry
    • Qiu, Z., P. Shi, H. Luo, Y. Bai, T. Yuan, P. Yang, S. Liu, and B. Yao. 2010. A xylanase with broad pH and temperature adaptability from Streptomyces megasporus DSM 41476, and its potential application in brewing industry. Enzyme Microb. Technol. 46: 506-512.
    • (2010) Enzyme Microb. Technol , vol.46 , pp. 506-512
    • Qiu, Z.1    Shi, P.2    Luo, H.3    Bai, Y.4    Yuan, T.5    Yang, P.6    Liu, S.7    Yao, B.8
  • 30
    • 0031841904 scopus 로고    scopus 로고
    • Site-directed mutagenesis study of a conserved residue in family 10 glycanases: Histidine 86 of xylanase A from Streptomyces lividans
    • Roberge, M., F. Shareck, R. Morosoli, D. Kluepfel, and C. Dupont. 1998. Site-directed mutagenesis study of a conserved residue in family 10 glycanases: Histidine 86 of xylanase A from Streptomyces lividans. Protein Eng. 11: 399-404.
    • (1998) Protein Eng , vol.11 , pp. 399-404
    • Roberge, M.1    Shareck, F.2    Morosoli, R.3    Kluepfel, D.4    Dupont, C.5
  • 32
    • 0033972584 scopus 로고    scopus 로고
    • Cellulase-free xylanases from Bacillus and other microorganisms
    • Subramaniyan, S. and P. Prema. 2000. Cellulase-free xylanases from Bacillus and other microorganisms. FEMS Microbiol. Lett. 183: 1-7.
    • (2000) FEMS Microbiol. Lett , vol.183 , pp. 1-7
    • Subramaniyan, S.1    Prema, P.2
  • 33
    • 0036210191 scopus 로고    scopus 로고
    • Biotechnology of microbial xylanases: Enzymology, molecular biology, and application
    • Subramaniyan, S. and P. Prema. 2002. Biotechnology of microbial xylanases: Enzymology, molecular biology, and application. Crit. Rev. Biotechnol. 22: 33-64.
    • (2002) Crit. Rev. Biotechnol , vol.22 , pp. 33-64
    • Subramaniyan, S.1    Prema, P.2
  • 34
    • 78649771410 scopus 로고    scopus 로고
    • Characterization of Paenibacillus curdlanolyticus intracellular xylanase Xyn10B encoded by the xyn10B gene
    • Sudo, M., M. Sakka, T. Kimyra, K. Ratanakhanokchai, and K. Sakka. 2010. Characterization of Paenibacillus curdlanolyticus intracellular xylanase Xyn10B encoded by the xyn10B gene. Biosci. Biotechnol. Biochem. 74: 2358-2360.
    • (2010) Biosci. Biotechnol. Biochem , vol.74 , pp. 2358-2360
    • Sudo, M.1    Sakka, M.2    Kimyra, T.3    Ratanakhanokchai, K.4    Sakka, K.5
  • 35
    • 0036240195 scopus 로고    scopus 로고
    • Separation of two functional domains of the family F/10 β-xylanase from Streptomyces olivaceoviridis E-86 limited proteolysis with papain and some of their properties
    • Sun, H. J., S. Yoshida, Y. Kawabata, N. H. Park, and I. Kusakabe. 2002. Separation of two functional domains of the family F/10 β-xylanase from Streptomyces olivaceoviridis E-86 limited proteolysis with papain and some of their properties. Biotechnol. Lett. 24: 595-601.
    • (2002) Biotechnol. Lett , vol.24 , pp. 595-601
    • Sun, H.J.1    Yoshida, S.2    Kawabata, Y.3    Park, N.H.4    Kusakabe, I.5
  • 37
    • 77952242284 scopus 로고    scopus 로고
    • A new xylanase from thermoalkaline Anoxybacillus sp. E2 with high activity and stability over a broad pH range
    • Wang, J., Y. Bai, P. Yang, P. Shi, H. Luo, K. Meng, H. Huang, J. Yin, and B. Yao. 2010. A new xylanase from thermoalkaline Anoxybacillus sp. E2 with high activity and stability over a broad pH range. World J. Microbiol. Biotechnol. 26: 917-924.
    • (2010) World J. Microbiol. Biotechnol , vol.26 , pp. 917-924
    • Wang, J.1    Bai, Y.2    Yang, P.3    Shi, P.4    Luo, H.5    Meng, K.6    Huang, H.7    Yin, J.8    Yao, B.9
  • 38
    • 49949086944 scopus 로고    scopus 로고
    • Scouring of knitted cotton fabrics with compound enzymes
    • Wang, Q., X. Fan, W. Gao, and J. Chen. 2006. Scouring of knitted cotton fabrics with compound enzymes. J. Text. Res. 27: 27-30.
    • (2006) J. Text. Res , vol.27 , pp. 27-30
    • Wang, Q.1    Fan, X.2    Gao, W.3    Chen, J.4
  • 39
    • 0002499398 scopus 로고
    • Use of complex formation between Congo red and polysaccharides in detection and assay of polysaccharide hydrolases
    • Wood, P. J., J. D. Erfle, and R. M. Teather. 1988. Use of complex formation between Congo red and polysaccharides in detection and assay of polysaccharide hydrolases. Methods Enzymol. 160: 59-74.
    • (1988) Methods Enzymol , vol.160 , pp. 59-74
    • Wood, P.J.1    Erfle, J.D.2    Teather, R.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.