메뉴 건너뛰기




Volumn 72, Issue 9, 2007, Pages

Characterization of a thermostable and acidic-tolerable β-Glucanase from aerobic fungi Trichoderma koningii ZJU-T

Author keywords

glucanase; Acidic tolerance; Thermostability; Trichoderma koningii ZJU T

Indexed keywords

DODECYL SULFATE SODIUM; EDETIC ACID; ENDO 1,3(4) BETA GLUCANASE; MERCAPTOETHANOL; METAL; POTASSIUM; UREA;

EID: 36349023786     PISSN: 00221147     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1750-3841.2007.00549.x     Document Type: Article
Times cited : (22)

References (33)
  • 1
    • 33646120574 scopus 로고    scopus 로고
    • Isolation of cellotriosyl blocks from barley β-glucan with endo-1,4-β-glucanase from Trichoderma reesei
    • Ajithkumar A, Andersson R, Siika-aho M, Tenkanen M, Åman P. 2006. Isolation of cellotriosyl blocks from barley β-glucan with endo-1,4-β-glucanase from Trichoderma reesei. Carbohydr Polym 64 (2 233 8.
    • (2006) Carbohydr Polym , vol.64 , Issue.2 , pp. 233-8
    • Ajithkumar, A.1    Andersson, R.2    Siika-Aho, M.3    Tenkanen, M.4    Åman, P.5
  • 2
    • 0033191906 scopus 로고    scopus 로고
    • Cloning, sequencing and expression of the gene encoding the Clostrikium stercorarium xylanase C in Escherichia coli
    • Ali MK, Fukumura M, Sakano K, Karita S, Kimura T, Sakka K, Ohmiya K. 1999. Cloning, sequencing and expression of the gene encoding the Clostrikium stercorarium xylanase C in Escherichia coli. Biosci Biotechnol Biochem 63 : 1596 604.
    • (1999) Biosci Biotechnol Biochem , vol.63 , pp. 1596-604
    • Ali, M.K.1    Fukumura, M.2    Sakano, K.3    Karita, S.4    Kimura, T.5    Sakka, K.6    Ohmiya, K.7
  • 3
    • 0016611070 scopus 로고
    • A new substrate for investigating the specificity of β-glucan hydrolases
    • Anderson MA, Stone BA. 1988. A new substrate for investigating the specificity of β-glucan hydrolases. FEBS Lett 52 : 202 7.
    • (1988) FEBS Lett , vol.52 , pp. 202-7
    • Anderson, M.A.1    Stone, B.A.2
  • 4
    • 1542268319 scopus 로고    scopus 로고
    • Essential role of the family-22 carbohydrate-binding modules for β-1,3-1,4-glucanase activity of Clostridium stercorarium Xyn10B
    • Araki R, Ali MK, Sakka M, Kimura T, Sakka K, Ohmiya K. 2004. Essential role of the family-22 carbohydrate-binding modules for β-1,3-1,4-glucanase activity of Clostridium stercorarium Xyn10B. FEBS Lett 561 : 155 8.
    • (2004) FEBS Lett , vol.561 , pp. 155-8
    • Araki, R.1    Ali, M.K.2    Sakka, M.3    Kimura, T.4    Sakka, K.5    Ohmiya, K.6
  • 5
    • 0032590072 scopus 로고    scopus 로고
    • An endoglucanase, eglA, from the hyperthermophilic archaeon Pyrococcus furiosus hydrolyzes β-1,4 bonds in mixed linkage (1,3-1,4)- β-D-glucans and cellulose
    • Bauer MW, Driskill LE, Callen W, Snead MA, Mathur EJ, Kelly RM. 1999. An endoglucanase, eglA, from the hyperthermophilic archaeon Pyrococcus furiosus hydrolyzes β-1,4 bonds in mixed linkage (1,3-1,4)- β-D-glucans and cellulose. J Bacteriol 181 (1 284 90.
    • (1999) J Bacteriol , vol.181 , Issue.1 , pp. 284-90
    • Bauer, M.W.1    Driskill, L.E.2    Callen, W.3    Snead, M.A.4    Mathur, E.J.5    Kelly, R.M.6
  • 6
    • 0030883632 scopus 로고    scopus 로고
    • Sequencing of a 1,3-1,4-β-D-glucanase (Lichenase) from the anaerobic fungus Orpinomyces strain PC-2: Properties of the enzyme expressed in Escherichia coli and evidence that the gene has a bacterial origin
    • Chen HZ, Li XL, Ljungdahl LG. 1997. Sequencing of a 1,3-1,4-β-D- glucanase (Lichenase) from the anaerobic fungus Orpinomyces strain PC-2: properties of the enzyme expressed in Escherichia coli and evidence that the gene has a bacterial origin. J Bacteriol 179 (19 6028 34.
    • (1997) J Bacteriol , vol.179 , Issue.19 , pp. 6028-34
    • Chen, H.Z.1    Li, X.L.2    Ljungdahl, L.G.3
  • 7
    • 0032697046 scopus 로고    scopus 로고
    • Purification and characterization of a cobalt-activated carboxypeptidase from the hyperthermophilic archaeon Pyrococcus furiosus
    • Cheng TC, Ramakrishnan V, Chan SI. 1999. Purification and characterization of a cobalt-activated carboxypeptidase from the hyperthermophilic archaeon Pyrococcus furiosus. Protein Sci 8 : 2474 86.
    • (1999) Protein Sci , vol.8 , pp. 2474-86
    • Cheng, T.C.1    Ramakrishnan, V.2    Chan, S.I.3
  • 8
    • 0026173105 scopus 로고
    • Isolation and characterization of two endo-β-glucanases from solid-state cultures of the aerobic fungus Penicillium capsulatum
    • Connelly IC, Coughlan MP. 1991. Isolation and characterization of two endo-β-glucanases from solid-state cultures of the aerobic fungus Penicillium capsulatum. Enzyme Microbial Technol 13 : 462 9.
    • (1991) Enzyme Microbial Technol , vol.13 , pp. 462-9
    • Connelly, I.C.1    Coughlan, M.P.2
  • 9
    • 33749946901 scopus 로고
    • Colorimetric method for determination of sugars and related substances
    • Dubois M, Gilles K, Hamillton PA, Rebers PA, Smith F. 1956. Colorimetric method for determination of sugars and related substances. Anal Chem 28 : 350 6.
    • (1956) Anal Chem , vol.28 , pp. 350-6
    • Dubois, M.1    Gilles, K.2    Hamillton, P.A.3    Rebers, P.A.4    Smith, F.5
  • 10
    • 0023684974 scopus 로고
    • Purification and properties of a 1,3-1,4-β-D-glucanase (lichenase, 1,3-1,4-β-D-glucan 4-glucanohydrolase, EC3.2.1.73) from Bccteroides succinogenes cloned in Escherichia coli
    • Erfle JD, Teather RM, Irvin JE. 1988. Purification and properties of a 1,3-1,4-β-D-glucanase (lichenase, 1,3-1,4-β-D-glucan 4-glucanohydrolase, EC3.2.1.73) from Bccteroides succinogenes cloned in Escherichia coli. Biochem J 255 : 833 41.
    • (1988) Biochem J , vol.255 , pp. 833-41
    • Erfle, J.D.1    Teather, R.M.2    Irvin, J.E.3
  • 11
    • 84978566967 scopus 로고
    • Morphology and chemical composition of barley endosperm cell walls
    • Fincher GB. 1975. Morphology and chemical composition of barley endosperm cell walls. J Inst Brew 81 (2 116 22.
    • (1975) J Inst Brew , vol.81 , Issue.2 , pp. 116-22
    • Fincher, G.B.1
  • 12
    • 0028949132 scopus 로고
    • Evidence for a general role for non-catalytic thermostabilizing domains in xylanases from thermophilic bacteria
    • Fontes CMGA, Hazlewood GP, Morag E, Hall J, Hirst BH, Gilbert HJ. 1995. Evidence for a general role for non-catalytic thermostabilizing domains in xylanases from thermophilic bacteria. Biochem J 307 : 151 8.
    • (1995) Biochem J , vol.307 , pp. 151-8
    • Cmga, F.1    Hazlewood, G.P.2    Morag, E.3    Hall, J.4    Hirst, B.H.5    Gilbert, H.J.6
  • 13
    • 0036718872 scopus 로고    scopus 로고
    • A thermostable Clostridium thermocellum lichenase-based reporter system for studying the gene expression regulation in prokaryotic and eukaryotic cells
    • Goldenkova IV, Musiychuk KA, Piruzian ES. 2002. A thermostable Clostridium thermocellum lichenase-based reporter system for studying the gene expression regulation in prokaryotic and eukaryotic cells. Mol Biol 36 (5 698 704.
    • (2002) Mol Biol , vol.36 , Issue.5 , pp. 698-704
    • Goldenkova, I.V.1    Musiychuk, K.A.2    Piruzian, E.S.3
  • 14
    • 0042412981 scopus 로고    scopus 로고
    • Cloning and targeted disruption of MLG1, a gene encoding two of three extracellular mixed-linked glucanases of Cochliobolus carbonum
    • Gorlach JM, Knaap EVD, Walton JD. 1998. Cloning and targeted disruption of MLG1, a gene encoding two of three extracellular mixed-linked glucanases of Cochliobolus carbonum. Appl Environ Microbiol 64 : 385 91.
    • (1998) Appl Environ Microbiol , vol.64 , pp. 385-91
    • Gorlach, J.M.1    Knaap, E.V.D.2    Walton, J.D.3
  • 15
    • 0025748793 scopus 로고
    • Two β-glucanase genes are clustered in Bacillus polymyxa - Molecular cloning, expression, and sequence analysis of genes encoding xylanase, and an endo-β- (1,3)-(1,4)-glucanase
    • Gosalbes MJ, Perezgonzalez JA, Gonzalez R, Navarro A. 1991. Two β-glucanase genes are clustered in Bacillus polymyxa - Molecular cloning, expression, and sequence analysis of genes encoding xylanase, and an endo-β- (1,3)-(1,4)-glucanase. J Bacteriol 173 : 7705 10.
    • (1991) J Bacteriol , vol.173 , pp. 7705-10
    • Gosalbes, M.J.1    Perezgonzalez, J.A.2    Gonzalez, R.3    Navarro, A.4
  • 16
    • 0030878526 scopus 로고    scopus 로고
    • Sequence of xynC and properties of XynC, a major component of the Clostridium thermocellum cellulosome
    • Hayashi H, Takagi KI, Fukumura M, Kimura T, Karita S, Sakka K, Ohmiya K. 1997. Sequence of xynC and properties of XynC, a major component of the Clostridium thermocellum cellulosome. J Bacteriol 179 : 4246 53.
    • (1997) J Bacteriol , vol.179 , pp. 4246-53
    • Hayashi, H.1    Takagi, K.I.2    Fukumura, M.3    Kimura, T.4    Karita, S.5    Sakka, K.6    Ohmiya, K.7
  • 17
    • 0030790212 scopus 로고    scopus 로고
    • Cloning and expression of an endo-1,3-1,4-β-glucanase gene from Bacillus macerans in Lactobacillus reuteri
    • Heng NCK, Jenkinson HF, Tannock GW. 1997. Cloning and expression of an endo-1,3-1,4-β-glucanase gene from Bacillus macerans in Lactobacillus reuteri. Appl Environ Microbiol 63 (8 3336 40.
    • (1997) Appl Environ Microbiol , vol.63 , Issue.8 , pp. 3336-40
    • Heng, N.C.K.1    Jenkinson, H.F.2    Tannock, G.W.3
  • 19
    • 0035111310 scopus 로고    scopus 로고
    • Growth of Trichoderma viride on crude cell wall preparations from barley
    • Kanauchi M, Bamforth CW. 2001. Growth of Trichoderma viride on crude cell wall preparations from barley. J Agric Food Chem 49 : 883 7.
    • (2001) J Agric Food Chem , vol.49 , pp. 883-7
    • Kanauchi, M.1    Bamforth, C.W.2
  • 20
    • 0027274760 scopus 로고
    • Characterization of the active site and thermostability regions of endoxylanase from Thermoanaerobacterium saccharolyticum B6A-RI
    • Lee Y-E, Lowe SE, Henrissat B, Zeikus G. 1993. Characterization of the active site and thermostability regions of endoxylanase from Thermoanaerobacterium saccharolyticum B6A-RI. J Bacteriol 175 : 5890 8.
    • (1993) J Bacteriol , vol.175 , pp. 5890-8
    • Lee, Y.-E.1    Lowe, S.E.2    Henrissat, B.3    Zeikus, G.4
  • 21
    • 0027475578 scopus 로고
    • Characterization, cloning, and sequencing of a thermostable endo-(1,3-1,4)-β-glucanase-encoding gene from an alkalophilic Bacillus brevis
    • Louw ME, Reid SJ, Watson TG. 1993. Characterization, cloning, and sequencing of a thermostable endo-(1,3-1,4)-β-glucanase-encoding gene from an alkalophilic Bacillus brevis. Appl Microbiol Biotechnol 38 : 507 13.
    • (1993) Appl Microbiol Biotechnol , vol.38 , pp. 507-13
    • Louw, M.E.1    Reid, S.J.2    Watson, T.G.3
  • 22
    • 33746543618 scopus 로고    scopus 로고
    • Construction and characterization of a bifunctional fusion enzyme of bacillus-sourced β-glucanase and xylanase expressed in Escherichia coli
    • Lu P, Feng MG, Li WF, Hu CX. 2006. Construction and characterization of a bifunctional fusion enzyme of bacillus-sourced β-glucanase and xylanase expressed in Escherichia coli. FEMS Microbiol Letters 261 (2 224 30.
    • (2006) FEMS Microbiol Letters , vol.261 , Issue.2 , pp. 224-30
    • Lu, P.1    Feng, M.G.2    Li, W.F.3    Hu, C.X.4
  • 23
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for the determination of reducing sugar
    • Miller GL. 1959. Use of dinitrosalicylic acid reagent for the determination of reducing sugar. Anal Chem 31 : 426 8.
    • (1959) Anal Chem , vol.31 , pp. 426-8
    • Miller, G.L.1
  • 24
    • 0035811982 scopus 로고    scopus 로고
    • Isolation and characterization of a thermostable endo-β-glucanase active on 1,3-1,4-β-D-glucans from the aerobic fungus Talaromyces emersonii CBS 814.70
    • Murray PG, Grassick A, Laffey CD, Cuffe MM, Higgins T, Savage AV, Planas A, Tuohy MG. 2001. Isolation and characterization of a thermostable endo-β-glucanase active on 1,3-1,4-β-D-glucans from the aerobic fungus Talaromyces emersonii CBS 814.70. Enzyme Microbiol Technol 29 (1 90 8.
    • (2001) Enzyme Microbiol Technol , vol.29 , Issue.1 , pp. 90-8
    • Murray, P.G.1    Grassick, A.2    Laffey, C.D.3    Cuffe, M.M.4    Higgins, T.5    Savage, A.V.6    Planas, A.7    Tuohy, M.G.8
  • 25
    • 0034731485 scopus 로고    scopus 로고
    • Bacterial 1,3-1,4-β-glucanases: Structure, function and protein engineering
    • Planas A. 2000. Bacterial 1,3-1,4-β-glucanases: structure, function and protein engineering. Biochim Biophys Acta 1543 : 361 82.
    • (2000) Biochim Biophys Acta , vol.1543 , pp. 361-82
    • Planas, A.1
  • 26
    • 9144229563 scopus 로고    scopus 로고
    • Stability and kinetics of β-1,3-glucan from Trichoderma harzianum
    • Rana DS, Theodore K, Naidu GSN, Panda T. 2003. Stability and kinetics of β-1,3-glucan from Trichoderma harzianum. Process Biochem 39 : 149 55.
    • (2003) Process Biochem , vol.39 , pp. 149-55
    • Rana, D.S.1    Theodore, K.2    Naidu, G.S.N.3    Panda, T.4
  • 27
    • 33748501893 scopus 로고    scopus 로고
    • A highly thermostable and alkaline amylase from a Bacillus sp
    • Saxena RK, Dutt K, Agarwal L, Nayyar P. 2007. A highly thermostable and alkaline amylase from a Bacillus sp. PN5. Biores Technol 98 : 260 5.
    • (2007) PN5. Biores Technol , vol.98 , pp. 260-5
    • Saxena, R.K.1    Dutt, K.2    Agarwal, L.3    Nayyar, P.4
  • 28
    • 84978555634 scopus 로고
    • The viscosity of worts in relation to their content of β-glucan
    • Scott RW. 1972. The viscosity of worts in relation to their content of β-glucan. J Inst Brew 78 (2 179 86.
    • (1972) J Inst Brew , vol.78 , Issue.2 , pp. 179-86
    • Scott, R.W.1
  • 29
    • 0017083431 scopus 로고
    • Degradation of barley glucan and lichenan by a Bacillus pumilus enzyme
    • Suzuki H, Kaneko T. 1976. Degradation of barley glucan and lichenan by a Bacillus pumilus enzyme. Agri Biol Chem 40 : 577 86.
    • (1976) Agri Biol Chem , vol.40 , pp. 577-86
    • Suzuki, H.1    Kaneko, T.2
  • 30
    • 1642446551 scopus 로고    scopus 로고
    • Medium optimization for the production of thermal stable β-glucanase by Bacillus subtilis ZJF-1A5 using response surface methodology
    • Tang XJ, He GQ, Chen QH, Zhang XY, Ali MAM. 2004. Medium optimization for the production of thermal stable β-glucanase by Bacillus subtilis ZJF-1A5 using response surface methodology. Biores Technol 93 : 175 81.
    • (2004) Biores Technol , vol.93 , pp. 175-81
    • Tang, X.J.1    He, G.Q.2    Chen, Q.H.3    Zhang, X.Y.4    Ali, M.A.M.5
  • 31
    • 0020032328 scopus 로고
    • Use of Congo red-polysaccharide interactions in enumeration and characterization of cellulolytic bacteria from the bovine rumen
    • Teather RM, Wood PJ. 1982. Use of Congo red-polysaccharide interactions in enumeration and characterization of cellulolytic bacteria from the bovine rumen. Appl Environ Microbiol 43 : 777 80.
    • (1982) Appl Environ Microbiol , vol.43 , pp. 777-80
    • Teather, R.M.1    Wood, P.J.2
  • 32
    • 21744452510 scopus 로고    scopus 로고
    • A truncated Fibrobacter succinogenes 1,3-1,4-β-D-glucanase with improved enzymatic activity and thermotolerance
    • Wen TN, Chen JL, Lee SH, Yang NS, Shyur LF. 2005. A truncated Fibrobacter succinogenes 1,3-1,4-β-D-glucanase with improved enzymatic activity and thermotolerance. Biochemistry 44 (25 9197 205.
    • (2005) Biochemistry , vol.44 , Issue.25 , pp. 9197-205
    • Wen, T.N.1    Chen, J.L.2    Lee, S.H.3    Yang, N.S.4    Shyur, L.F.5
  • 33
    • 23644445055 scopus 로고    scopus 로고
    • A major new component in the cellulosome of Clostridium thermocellum is a processive endo-β-1,4-glucanase producing cellotetraose
    • Zverlov VV, Schantz N, Schwarz WH. 2005. A major new component in the cellulosome of Clostridium thermocellum is a processive endo-β-1,4- glucanase producing cellotetraose. FEMS Microbiol Lett 249 : 353 8.
    • (2005) FEMS Microbiol Lett , vol.249 , pp. 353-8
    • Zverlov, V.V.1    Schantz, N.2    Schwarz, W.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.