메뉴 건너뛰기




Volumn 5, Issue 9, 2011, Pages 1956-1961

Expression of a new endoglucanase gene from aspergillus terreus SUK-1 suppressed by glucose

Author keywords

A. Terreus suk 1; Endoglucanase; Expression; Gene; Glucose

Indexed keywords


EID: 81755169027     PISSN: 19918178     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (2)

References (31)
  • 1
    • 34548426935 scopus 로고    scopus 로고
    • Enhanced production of cellulase-free thermostable xylanase by Bacillus pumilus ASH and its potential application in paper industry
    • Battan, B., J. Sharma, S.S. Dhiman and R.C. Kuhad, 2007. Enhanced production of cellulase-free thermostable xylanase by Bacillus pumilus ASH and its potential application in paper industry. Enzyme and Microbial Technology, 41: 733-739.
    • (2007) Enzyme and Microbial Technology , vol.41 , pp. 733-739
    • Battan, B.1    Sharma, J.2    Dhiman, S.S.3    Kuhad, R.C.4
  • 3
    • 81755180565 scopus 로고
    • Trichoderma reesei cellulases, biochemistry, genetics, physiology and applications
    • Béguin, P., 1990. Trichoderma reesei cellulases, biochemistry, genetics, physiology and applications. Biochimie, 12: 900-901.
    • (1990) Biochimie , vol.12 , pp. 900-901
    • Béguin, P.1
  • 4
    • 27244461782 scopus 로고
    • Biosynthesis and biodegradation of cellulose
    • Béguin, P., 1992. Biosynthesis and biodegradation of cellulose. Biochimie, 74: 1041-1043.
    • (1992) Biochimie , vol.74 , pp. 1041-1043
    • Béguin, P.1
  • 5
    • 0034736290 scopus 로고    scopus 로고
    • Endoglucanase activity and relative expression of glycoside hydrolase genes of Fibrobacter succinogenes S85 grown on different substrates
    • Béra-Maillet, C., G. Gaudet and E. Forano, 2000. Endoglucanase activity and relative expression of glycoside hydrolase genes of Fibrobacter succinogenes S85 grown on different substrates. Biochimica et Biophysica Acta (BBA)-Protein Structure and Molecular Enzymology, 1543: 77-85.
    • (2000) Biochimica et Biophysica Acta (BBA)-Protein Structure and Molecular Enzymology , vol.1543 , pp. 77-85
    • Béra-Maillet, C.1    Gaudet, G.2    Forano, E.3
  • 6
    • 0034253208 scopus 로고    scopus 로고
    • Cellulases and related enzymes in biotechnology
    • Bhat, M.K., 2000. Cellulases and related enzymes in biotechnology. Biotechnology Advances, 18: 355-383.
    • (2000) Biotechnology Advances , vol.18 , pp. 355-383
    • Bhat, M.K.1
  • 7
    • 71449127972 scopus 로고    scopus 로고
    • Molecular cloning, gene expression analysis and structural modelling of the cellobiohydrolase I from Penicillium occitanis
    • Bhiri, F., A. Gargouri, M.B. Ali, H. Belghith, M. Blibech and S.E. Chaabouni, 2010. Molecular cloning, gene expression analysis and structural modelling of the cellobiohydrolase I from Penicillium occitanis. Enzyme and Microbial Technology, 46: 74-81.
    • (2010) Enzyme and Microbial Technology , vol.46 , pp. 74-81
    • Bhiri, F.1    Gargouri, A.2    Ali, M.B.3    Belghith, H.4    Blibech, M.5    Chaabouni, S.E.6
  • 8
    • 58149200943 scopus 로고    scopus 로고
    • The Carbohydrate-Active EnZymes database (CAZy): An expert resource for Glycogenomics
    • (Database issue), doi:10.1093/nar/gkn663
    • Cantarel, B.L., P.M. Coutinho, C. Rancurel, T. Bernard, V. Lombard and B. Henrissat, 2009. The Carbohydrate-Active EnZymes database (CAZy): An expert resource for Glycogenomics. Nucleic Acids Research, 37(Database issue): D233-D238. doi:10.1093/nar/gkn663.
    • (2009) Nucleic Acids Research , vol.37
    • Cantarel, B.L.1    Coutinho, P.M.2    Rancurel, C.3    Bernard, T.4    Lombard, V.5    Henrissat, B.6
  • 9
    • 79960199057 scopus 로고    scopus 로고
    • Status and barriers of advanced biofuel technologies: A review
    • Cheng, J.J. and G.R. Timilsina, 2011. Status and barriers of advanced biofuel technologies: A review. Renewable Energy, 36: 3541-3549.
    • (2011) Renewable Energy , vol.36 , pp. 3541-3549
    • Cheng, J.J.1    Timilsina, G.R.2
  • 10
    • 0025804758 scopus 로고
    • Domains in microbial beta-1,4-glycanases: Sequence conservation, function, and enzyme families
    • Gilkes, N.R., B. Henrissat, D.G. Kilburn, R.C. Miller and R.A. Warren, 1991. Domains in microbial beta-1,4-glycanases: sequence conservation, function, and enzyme families. Microbiological Reviews, 55: 303-315.
    • (1991) Microbiological Reviews , vol.55 , pp. 303-315
    • Gilkes, N.R.1    Henrissat, B.2    Kilburn, D.G.3    Miller, R.C.4    Warren, R.A.5
  • 11
    • 78149464840 scopus 로고    scopus 로고
    • Transcriptional analysis of catabolite repression in Clostridium acetobutylicum growing on mixtures of D-glucose and D-xylose
    • Grimmler, C., C. Held, W. Liebl and A. Ehrenreich, 2010. Transcriptional analysis of catabolite repression in Clostridium acetobutylicum growing on mixtures of D-glucose and D-xylose. Journal of Biotechnology, 150: 315-323.
    • (2010) Journal of Biotechnology , vol.150 , pp. 315-323
    • Grimmler, C.1    Held, C.2    Liebl, W.3    Ehrenreich, A.4
  • 12
    • 76049115434 scopus 로고    scopus 로고
    • The application of exogenous cellulase to improve soil fertility and plant growth due to acceleration of straw decomposition
    • Han, W. and M. He, 2010. The application of exogenous cellulase to improve soil fertility and plant growth due to acceleration of straw decomposition. Bioresource Technology, 101: 3724-3731.
    • (2010) Bioresource Technology , vol.101 , pp. 3724-3731
    • Han, W.1    He, M.2
  • 13
    • 2942624371 scopus 로고    scopus 로고
    • Induction, production, repression, and de-repression of exoglucanase synthesis in Aspergillus niger
    • Hanif, A., A. Yasmeen and M.I. Rajoka, 2004. Induction, production, repression, and de-repression of exoglucanase synthesis in Aspergillus niger. Bioresource Technology, 94: 311-319.
    • (2004) Bioresource Technology , vol.94 , pp. 311-319
    • Hanif, A.1    Yasmeen, A.2    Rajoka, M.I.3
  • 14
    • 0029645404 scopus 로고
    • Structures and mechanisms of glycosyl hydrolases
    • Henrissat, B. and G. Davies, 1995. Structures and mechanisms of glycosyl hydrolases. Structure, 3: 853-859.
    • (1995) Structure , vol.3 , pp. 853-859
    • Henrissat, B.1    Davies, G.2
  • 15
    • 41949123091 scopus 로고    scopus 로고
    • Development of applications of industrial enzymes from Malaysian indigenous microbial sources
    • Ibrahim, C.O., 2008. Development of applications of industrial enzymes from Malaysian indigenous microbial sources. Bioresource Technology, 99: 4572-4582.
    • (2008) Bioresource Technology , vol.99 , pp. 4572-4582
    • Ibrahim, C.O.1
  • 16
    • 0030480099 scopus 로고    scopus 로고
    • Functional analysis of the cellobiohydrolase I promoter of the filamentous fungus Trichoderma reesei
    • Ilmén, M., M.L. Onnela, S. Klemsdal, S. Keränen and M. Penttilä, 1996. Functional analysis of the cellobiohydrolase I promoter of the filamentous fungus Trichoderma reesei. Molecular and General Genetics, 253: 303-314.
    • (1996) Molecular and General Genetics , vol.253 , pp. 303-314
    • Ilmén, M.1    Onnela, M.L.2    Klemsdal, S.3    Keränen, S.4    Penttilä, M.5
  • 18
    • 33750024444 scopus 로고    scopus 로고
    • Characterization of a new β-1,4-endoglucanase gene from the root-knot nematode Meloidogyne incognita and evolutionary scheme for phytonematode family 5 glycosyl hydrolases
    • Ledger, T.N., S. Jaubert, N. Bosselut, P. Abad and M-N. Rosso, 2006. Characterization of a new β-1,4-endoglucanase gene from the root-knot nematode Meloidogyne incognita and evolutionary scheme for phytonematode family 5 glycosyl hydrolases. Gene, 382: 121-128.
    • (2006) Gene , vol.382 , pp. 121-128
    • Ledger, T.N.1    Jaubert, S.2    Bosselut, N.3    Abad, P.4    Rosso, M.-N.5
  • 19
    • 65449137881 scopus 로고    scopus 로고
    • Simultaneous cloning and expression of two cellulase genes from Bacillus subtilis newly isolated from Golden Takin (Budorcas taxicolor Bedfordi)
    • Li, W., X. Huan, Y. Zhou, Q. Mac and Y. Chen, 2009. Simultaneous cloning and expression of two cellulase genes from Bacillus subtilis newly isolated from Golden Takin (Budorcas taxicolor Bedfordi). Biochemical and Biophysical Research Communications, 383: 397-400.
    • (2009) Biochemical and Biophysical Research Communications , vol.383 , pp. 397-400
    • Li, W.1    Huan, X.2    Zhou, Y.3    Mac, Q.4    Chen, Y.5
  • 20
    • 0000187295 scopus 로고
    • Induction of cellulose in fungi by cellobiose
    • Mandels, M. and E.T. Reese, 1957. Induction of cellulose in fungi by cellobiose. Journal of Bacteriology, 73: 816-826.
    • (1957) Journal of Bacteriology , vol.73 , pp. 816-826
    • Mandels, M.1    Reese, E.T.2
  • 21
    • 79551469651 scopus 로고    scopus 로고
    • Improved mannan-degrading enzymes' production by Aspergillus niger through medium optimization
    • Mohamad, S.N., R.N. Ramanan, R. Mohamad and A.B. Ariff, 2011. Improved mannan-degrading enzymes' production by Aspergillus niger through medium optimization. New Biotechnology, 28: 146-152.
    • (2011) New Biotechnology , vol.28 , pp. 146-152
    • Mohamad, S.N.1    Ramanan, R.N.2    Mohamad, R.3    Ariff, A.B.4
  • 23
    • 33947652782 scopus 로고    scopus 로고
    • The effect of carbohydrate carbon sources on the production of cellulase by Phlebia gigantean
    • Niranjane, A.P., P. Madhou and T.W. Stevenson, 2007. The effect of carbohydrate carbon sources on the production of cellulase by Phlebia gigantean. Enzyme and Microbial Technology, 40: 1464-1468.
    • (2007) Enzyme and Microbial Technology , vol.40 , pp. 1464-1468
    • Niranjane, A.P.1    Madhou, P.2    Stevenson, T.W.3
  • 24
    • 61649117486 scopus 로고    scopus 로고
    • Molecular cloning of endogenous β-glucosidase from common Japanese brackish water clam Corbicula japonica
    • Sakamoto, K., S. Uji, T. Kurokawa and H. Toyohara, 2009. Molecular cloning of endogenous β-glucosidase from common Japanese brackish water clam Corbicula japonica. Gene, 435: 72-79.
    • (2009) Gene , vol.435 , pp. 72-79
    • Sakamoto, K.1    Uji, S.2    Kurokawa, T.3    Toyohara, H.4
  • 27
    • 42749096854 scopus 로고    scopus 로고
    • The composition of basal and induced cellulase systems in Penicillium decumbens under induction or repression conditions
    • Sun, X., Z. Liu, K. Zheng, X. Song and Y. Qu, 2008. The composition of basal and induced cellulase systems in Penicillium decumbens under induction or repression conditions. Enzyme and Microbial Technology, 42: 560-567.
    • (2008) Enzyme and Microbial Technology , vol.42 , pp. 560-567
    • Sun, X.1    Liu, Z.2    Zheng, K.3    Song, X.4    Qu, Y.5
  • 28
    • 0035163298 scopus 로고    scopus 로고
    • Induction and catabolite repression mechanisms of cellulase in fungi
    • Suto, M. and F. Tomita, 2001. Induction and catabolite repression mechanisms of cellulase in fungi. Journal of Bioscience and Bioengineering, 92: 305-311.
    • (2001) Journal of Bioscience and Bioengineering , vol.92 , pp. 305-311
    • Suto, M.1    Tomita, F.2
  • 29
    • 0032233476 scopus 로고    scopus 로고
    • Isolation of the creA gene from the cellulolytic fungus Humicola grisea and analysis of CreA binding sites upstream from the cellulase genes
    • Takashima, S., A. Nakamura, M. Hidaka, H. Masaki and T. Uozumi, 1998. Isolation of the creA gene from the cellulolytic fungus Humicola grisea and analysis of CreA binding sites upstream from the cellulase genes. Bioscience, Biotechnology, and Biochemistry, 62: 2364-2370.
    • (1998) Bioscience, Biotechnology, and Biochemistry , vol.62 , pp. 2364-2370
    • Takashima, S.1    Nakamura, A.2    Hidaka, M.3    Masaki, H.4    Uozumi, T.5
  • 31
    • 0031149857 scopus 로고    scopus 로고
    • Crystalline cellulose degradation: New insight into the function of cellobiohydrolases
    • Teeri, T.T., 1997. Crystalline cellulose degradation: new insight into the function of cellobiohydrolases. Trends in Biotechnology, 15: 160-167.
    • (1997) Trends in Biotechnology , vol.15 , pp. 160-167
    • Teeri, T.T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.