메뉴 건너뛰기




Volumn 67, Issue , 2014, Pages 47-52

Identification of a β-glucosidase from the Mucor circinelloides genome by peptide pattern recognition

Author keywords

Glycoside hydrolase 3; Mucor circinelloides; Peptide pattern recognition; Glucosidase

Indexed keywords

ENCODING (SYMBOLS); ENZYMES; FUNGI; GENES; GLUCOSE; HYDROLASES; PEPTIDES; PLANT CELL CULTURE; PLANTS (BOTANY); RECOMBINANT PROTEINS; SUGARS;

EID: 84937511141     PISSN: 01410229     EISSN: 18790909     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2014.09.002     Document Type: Article
Times cited : (25)

References (43)
  • 1
    • 84866033812 scopus 로고    scopus 로고
    • Biomass converting enzymes as industrial biocatalysts for fuels and chemicals: recent developments
    • Sweeney M.D., Xu F. Biomass converting enzymes as industrial biocatalysts for fuels and chemicals: recent developments. Catalysts 2012, 2:244-263.
    • (2012) Catalysts , vol.2 , pp. 244-263
    • Sweeney, M.D.1    Xu, F.2
  • 2
    • 33846951759 scopus 로고    scopus 로고
    • Biomass recalcitrance: engineering plants and enzymes for biofuels production
    • Himmel M.E., Ding S.Y., Johnson D.K., Adney W.S., Nimlos M.R., Brady J.W., et al. Biomass recalcitrance: engineering plants and enzymes for biofuels production. Science 2007, 315:804-807.
    • (2007) Science , vol.315 , pp. 804-807
    • Himmel, M.E.1    Ding, S.Y.2    Johnson, D.K.3    Adney, W.S.4    Nimlos, M.R.5    Brady, J.W.6
  • 4
  • 5
    • 70449408785 scopus 로고    scopus 로고
    • Parallel metatranscriptome analyses of host and symbiont gene expression in the gut of the termite Reticulitermes flavipes
    • Tartar A., Wheeler M., Zhou X., Coy M., Boucias D., Scharf M. Parallel metatranscriptome analyses of host and symbiont gene expression in the gut of the termite Reticulitermes flavipes. Biotechnol Biofuels 2009, 2:25.
    • (2009) Biotechnol Biofuels , vol.2 , pp. 25
    • Tartar, A.1    Wheeler, M.2    Zhou, X.3    Coy, M.4    Boucias, D.5    Scharf, M.6
  • 6
    • 84856460892 scopus 로고    scopus 로고
    • Post-genomic analyses of fungal lignocellulosic biomass degradation reveal the unexpected potential of the plant pathogen Ustilago maydis
    • Couturier M., Navarro D., Olive C., Chevret D., Haon M., Favel A., et al. Post-genomic analyses of fungal lignocellulosic biomass degradation reveal the unexpected potential of the plant pathogen Ustilago maydis. BMC Genomics 2012, 13:1471-2164.
    • (2012) BMC Genomics , vol.13 , pp. 1471-2164
    • Couturier, M.1    Navarro, D.2    Olive, C.3    Chevret, D.4    Haon, M.5    Favel, A.6
  • 7
    • 84859143948 scopus 로고    scopus 로고
    • Deciphering transcriptional regulatory mechanisms associated with hemicellulose degradation in Neurospora crassa
    • Sun J., Tian C., Diamond S., Glass N.L. Deciphering transcriptional regulatory mechanisms associated with hemicellulose degradation in Neurospora crassa. Eukaryot Cell 2012, 11:482-493.
    • (2012) Eukaryot Cell , vol.11 , pp. 482-493
    • Sun, J.1    Tian, C.2    Diamond, S.3    Glass, N.L.4
  • 8
    • 30344451101 scopus 로고    scopus 로고
    • Accurate anchoring alignment of divergent sequences
    • Huang W., Umbach D.M., Li L. Accurate anchoring alignment of divergent sequences. Bioinformatics 2006, 22:29-34.
    • (2006) Bioinformatics , vol.22 , pp. 29-34
    • Huang, W.1    Umbach, D.M.2    Li, L.3
  • 10
    • 84871398239 scopus 로고    scopus 로고
    • Re-annotation of the CAZy genes of Trichoderma reesei and transcription in the presence of lignocellulosic substrates
    • Hakkinen M., Arvas M., Oja M., Aro N., Penttila M., Saloheimo M., et al. Re-annotation of the CAZy genes of Trichoderma reesei and transcription in the presence of lignocellulosic substrates. Microb Cell Fact 2012, 11:1475-2859.
    • (2012) Microb Cell Fact , vol.11 , pp. 1475-2859
    • Hakkinen, M.1    Arvas, M.2    Oja, M.3    Aro, N.4    Penttila, M.5    Saloheimo, M.6
  • 11
    • 70349482673 scopus 로고    scopus 로고
    • Tracking the roots of cellulase hyperproduction by the fungus Trichoderma reesei using massively parallel DNA sequencing
    • Le Crom S., Schackwitz W., Pennacchio L., Magnuson J.K., Culley D.E., Collett J.R., et al. Tracking the roots of cellulase hyperproduction by the fungus Trichoderma reesei using massively parallel DNA sequencing. Proc Natl Acad Sci USA 2009, 106:16151-16156.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 16151-16156
    • Le Crom, S.1    Schackwitz, W.2    Pennacchio, L.3    Magnuson, J.K.4    Culley, D.E.5    Collett, J.R.6
  • 12
    • 77954676864 scopus 로고    scopus 로고
    • Array comparative genomic hybridization analysis of Trichoderma reesei strains with enhanced cellulase production properties
    • Vitikainen M., Arvas M., Pakula T., Oja M., Penttila M., Saloheimo M. Array comparative genomic hybridization analysis of Trichoderma reesei strains with enhanced cellulase production properties. BMC Genomics 2010, 11:1471-2164.
    • (2010) BMC Genomics , vol.11 , pp. 1471-2164
    • Vitikainen, M.1    Arvas, M.2    Pakula, T.3    Oja, M.4    Penttila, M.5    Saloheimo, M.6
  • 13
    • 78651390306 scopus 로고    scopus 로고
    • Carbohydrate-active enzymes from the zygomycete fungus Rhizopus oryzae: a highly specialized approach to carbohydrate degradation depicted at genome level
    • Battaglia E., Benoit I., van den Brink J., Wiebenga A., Coutinho P.M., Henrissat B., et al. Carbohydrate-active enzymes from the zygomycete fungus Rhizopus oryzae: a highly specialized approach to carbohydrate degradation depicted at genome level. BMC Genomics 2011, 12:1471-2164.
    • (2011) BMC Genomics , vol.12 , pp. 1471-2164
    • Battaglia, E.1    Benoit, I.2    van den Brink, J.3    Wiebenga, A.4    Coutinho, P.M.5    Henrissat, B.6
  • 14
    • 79958280721 scopus 로고    scopus 로고
    • Current commercial perspective of Rhizopus oryzae: a review
    • Ghosh B., Ray R.R. Current commercial perspective of Rhizopus oryzae: a review. J Applied Sci 2011, 11:2470-2486.
    • (2011) J Applied Sci , vol.11 , pp. 2470-2486
    • Ghosh, B.1    Ray, R.R.2
  • 15
    • 79952562966 scopus 로고    scopus 로고
    • Highly thermostable xylanase purified from Rhizomucor miehei NRL 3169
    • Fawzi E.M. Highly thermostable xylanase purified from Rhizomucor miehei NRL 3169. Acta Biol Hung 2011, 62:85-94.
    • (2011) Acta Biol Hung , vol.62 , pp. 85-94
    • Fawzi, E.M.1
  • 17
    • 84887209898 scopus 로고    scopus 로고
    • Cellulolytic potential of thermophilic species from four fungal orders
    • Busk P., Lange L. Cellulolytic potential of thermophilic species from four fungal orders. AMB Express 2013, 3:47.
    • (2013) AMB Express , vol.3 , pp. 47
    • Busk, P.1    Lange, L.2
  • 18
    • 17644417083 scopus 로고    scopus 로고
    • Alternative splicing produces two endoglucanases with one or two carbohydrate-binding modules in Mucor circinelloides
    • Baba Y., Shimonaka A., Koga J., Kubota H., Kono T. Alternative splicing produces two endoglucanases with one or two carbohydrate-binding modules in Mucor circinelloides. J Bacteriol 2005, 187:3045-3051.
    • (2005) J Bacteriol , vol.187 , pp. 3045-3051
    • Baba, Y.1    Shimonaka, A.2    Koga, J.3    Kubota, H.4    Kono, T.5
  • 19
    • 4344678139 scopus 로고    scopus 로고
    • Production, purification and properties of endoglucanase from a newly isolated strain of Mucor circinelloides
    • Saha B.C. Production, purification and properties of endoglucanase from a newly isolated strain of Mucor circinelloides. Process Biochem 2004, 39:1871-1876.
    • (2004) Process Biochem , vol.39 , pp. 1871-1876
    • Saha, B.C.1
  • 20
    • 84877108120 scopus 로고    scopus 로고
    • Function-based classification of carbohydrate-active enzymes by recognition of short, conserved peptide motifs
    • Busk P.K., Lange L. Function-based classification of carbohydrate-active enzymes by recognition of short, conserved peptide motifs. Appl Environ Microbiol 2013, 79:3380-3391.
    • (2013) Appl Environ Microbiol , vol.79 , pp. 3380-3391
    • Busk, P.K.1    Lange, L.2
  • 22
    • 10844286172 scopus 로고    scopus 로고
    • Toward an aggregated understanding of enzymatic hydrolysis of cellulose: noncomplexed cellulase systems
    • Zhang Y.H., Lynd L.R. Toward an aggregated understanding of enzymatic hydrolysis of cellulose: noncomplexed cellulase systems. Biotechnol Bioeng 2004, 88:797-824.
    • (2004) Biotechnol Bioeng , vol.88 , pp. 797-824
    • Zhang, Y.H.1    Lynd, L.R.2
  • 23
    • 36549070666 scopus 로고    scopus 로고
    • Enzymatic hydrolysis of maize straw polysaccharides for the production of reducing sugars
    • Chen M., Zhao J., Xia L. Enzymatic hydrolysis of maize straw polysaccharides for the production of reducing sugars. Carbohyd Polym 2008, 71:411-415.
    • (2008) Carbohyd Polym , vol.71 , pp. 411-415
    • Chen, M.1    Zhao, J.2    Xia, L.3
  • 24
    • 0031574072 scopus 로고    scopus 로고
    • The ClustalX windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson J.D., Gibson T.J., Plewniak F., Jeanmougin F., Higgins D.G. The ClustalX windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res 1997, 25:4876-4882.
    • (1997) Nucleic Acids Res , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 25
    • 79957613599 scopus 로고    scopus 로고
    • MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods
    • Tamura K., Peterson D., Peterson N., Stecher G., Nei M., Kumar S. MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods. Mol Biol Evol 2011, 28:2731-2739.
    • (2011) Mol Biol Evol , vol.28 , pp. 2731-2739
    • Tamura, K.1    Peterson, D.2    Peterson, N.3    Stecher, G.4    Nei, M.5    Kumar, S.6
  • 26
    • 84860483860 scopus 로고    scopus 로고
    • Characterization of a beta-glucosidase with transgalactosylation capacity from the zygomycete Rhizomucor miehei
    • Krisch J., Bencsik O., Papp T., Vagvolgyi C., Tako M. Characterization of a beta-glucosidase with transgalactosylation capacity from the zygomycete Rhizomucor miehei. Bioresource Technol 2012, 114:555-560.
    • (2012) Bioresource Technol , vol.114 , pp. 555-560
    • Krisch, J.1    Bencsik, O.2    Papp, T.3    Vagvolgyi, C.4    Tako, M.5
  • 27
    • 0001369336 scopus 로고
    • A buffer solution for colorimetric comparison
    • McIlvaine T.C. A buffer solution for colorimetric comparison. J Biol Chem 1921, 49:183-186.
    • (1921) J Biol Chem , vol.49 , pp. 183-186
    • McIlvaine, T.C.1
  • 28
    • 84856984996 scopus 로고    scopus 로고
    • Characterization of a thermostable beta-glucosidase from Aspergillus fumigatus Z5, and its functional expression in Pichia pastoris X33
    • Liu D., Zhang R., Yang X., Zhang Z., Song S., Miao Y., et al. Characterization of a thermostable beta-glucosidase from Aspergillus fumigatus Z5, and its functional expression in Pichia pastoris X33. Microb Cell Fact 2012, 11:1475-2859.
    • (2012) Microb Cell Fact , vol.11 , pp. 1475-2859
    • Liu, D.1    Zhang, R.2    Yang, X.3    Zhang, Z.4    Song, S.5    Miao, Y.6
  • 29
    • 0000785528 scopus 로고
    • Graphical methods in enzyme chemistry
    • Haldane J.B.S. Graphical methods in enzyme chemistry. Nature 1957, 179:832.
    • (1957) Nature , vol.179 , pp. 832
    • Haldane, J.B.S.1
  • 30
    • 77955503215 scopus 로고    scopus 로고
    • Identification of activity related amino acid mutations of a GH9 termite cellulase
    • Ni J., Takehara M., Watanabe H. Identification of activity related amino acid mutations of a GH9 termite cellulase. Bioresource Technol 2010, 101:6438-6443.
    • (2010) Bioresource Technol , vol.101 , pp. 6438-6443
    • Ni, J.1    Takehara, M.2    Watanabe, H.3
  • 31
    • 77952889939 scopus 로고    scopus 로고
    • Characterization of beta-glucosidase from a strain of Penicillium purpurogenum KJS506
    • Jeya M., Joo A.R., Lee K.M., Tiwari M.K., Kim S.H., Lee J.K. Characterization of beta-glucosidase from a strain of Penicillium purpurogenum KJS506. Appl Microbiol Biot 2010, 86:1473-1484.
    • (2010) Appl Microbiol Biot , vol.86 , pp. 1473-1484
    • Jeya, M.1    Joo, A.R.2    Lee, K.M.3    Tiwari, M.K.4    Kim, S.H.5    Lee, J.K.6
  • 32
    • 0032545669 scopus 로고    scopus 로고
    • The cloning, expression and characterization of a cellobiase gene encoding a secretory enzyme from Cellulomonas biazotea
    • Wong W.K., Ali A., Chan W.K., Ho V., Lee N.T. The cloning, expression and characterization of a cellobiase gene encoding a secretory enzyme from Cellulomonas biazotea. Gene 1998, 207:79-86.
    • (1998) Gene , vol.207 , pp. 79-86
    • Wong, W.K.1    Ali, A.2    Chan, W.K.3    Ho, V.4    Lee, N.T.5
  • 33
    • 84861051737 scopus 로고    scopus 로고
    • High level expression of extracellular secretion of a beta-glucosidase gene (PtBglu3) from Paecilomyces thermophila in Pichia pastoris
    • Yan Q., Hua C., Yang S., Li Y., Jiang Z. High level expression of extracellular secretion of a beta-glucosidase gene (PtBglu3) from Paecilomyces thermophila in Pichia pastoris. Protein Expr Purif 2012, 84:64-72.
    • (2012) Protein Expr Purif , vol.84 , pp. 64-72
    • Yan, Q.1    Hua, C.2    Yang, S.3    Li, Y.4    Jiang, Z.5
  • 34
    • 84877148215 scopus 로고    scopus 로고
    • Cloning, expression and characterization of an ethanol tolerant GH3 beta-glucosidase from Myceliophthora thermophila
    • Karnaouri A., Topakas E., Paschos T., Taouki I., Christakopoulos P. Cloning, expression and characterization of an ethanol tolerant GH3 beta-glucosidase from Myceliophthora thermophila. PeerJ 2013, 1:e46.
    • (2013) PeerJ , vol.1 , pp. e46
    • Karnaouri, A.1    Topakas, E.2    Paschos, T.3    Taouki, I.4    Christakopoulos, P.5
  • 35
    • 84861163349 scopus 로고    scopus 로고
    • Overexpression of an exotic thermotolerant beta-glucosidase in trichoderma reesei and its significant increase in cellulolytic activity and saccharification of barley straw
    • Dashtban M., Qin W. Overexpression of an exotic thermotolerant beta-glucosidase in trichoderma reesei and its significant increase in cellulolytic activity and saccharification of barley straw. Microb Cell Fact 2012, 11:1475-2859.
    • (2012) Microb Cell Fact , vol.11 , pp. 1475-2859
    • Dashtban, M.1    Qin, W.2
  • 36
    • 84859210787 scopus 로고    scopus 로고
    • Characterization of a GH family 3 β-glycoside hydrolase from Chrysosporium lucknowense and its application to the hydrolysis of β-glucan and xylan
    • Dotsenko G.S., Sinitsyna O.A., Hinz S.W.A., Wery J., Sinitsyn A.P. Characterization of a GH family 3 β-glycoside hydrolase from Chrysosporium lucknowense and its application to the hydrolysis of β-glucan and xylan. Bioresource Technol 2012, 112:345-349.
    • (2012) Bioresource Technol , vol.112 , pp. 345-349
    • Dotsenko, G.S.1    Sinitsyna, O.A.2    Hinz, S.W.A.3    Wery, J.4    Sinitsyn, A.P.5
  • 38
    • 0027565969 scopus 로고
    • Isolation and characterization of two forms of beta-d-glucosidase from Aspergillus niger
    • Himmel M.E., Adney W.S., Fox J.W., Mitchell D.J., Baker J.O. Isolation and characterization of two forms of beta-d-glucosidase from Aspergillus niger. Appl Biochem Biotech 1993, 40:213-225.
    • (1993) Appl Biochem Biotech , vol.40 , pp. 213-225
    • Himmel, M.E.1    Adney, W.S.2    Fox, J.W.3    Mitchell, D.J.4    Baker, J.O.5
  • 39
    • 16544375812 scopus 로고    scopus 로고
    • Physical and kinetic properties of the family 3 beta-glucosidase from Aspergillus niger which is important for cellulose breakdown
    • Seidle H.F., Marten I., Shoseyov O., Huber R.E. Physical and kinetic properties of the family 3 beta-glucosidase from Aspergillus niger which is important for cellulose breakdown. Protein J 2004, 23:11-23.
    • (2004) Protein J , vol.23 , pp. 11-23
    • Seidle, H.F.1    Marten, I.2    Shoseyov, O.3    Huber, R.E.4
  • 40
    • 34247098005 scopus 로고    scopus 로고
    • Purification and biochemical characterization of an extracellular β-glucosidase from the wood-decaying fungus Daldinia eschscholzii (Ehrenb.:Fr.) Rehm
    • Karnchanatat A., Petsom A., Sangvanich P., Piaphukiew J., Whalley A.J.S., Reynolds C.D., et al. Purification and biochemical characterization of an extracellular β-glucosidase from the wood-decaying fungus Daldinia eschscholzii (Ehrenb.:Fr.) Rehm. FEMS Microbiol Lett 2007, 270:162-170.
    • (2007) FEMS Microbiol Lett , vol.270 , pp. 162-170
    • Karnchanatat, A.1    Petsom, A.2    Sangvanich, P.3    Piaphukiew, J.4    Whalley, A.J.S.5    Reynolds, C.D.6
  • 41
    • 0035156434 scopus 로고    scopus 로고
    • Biochemical characterization and mechanism of action of a thermostable beta-glucosidase purified from Thermoascus aurantiacus
    • Parry N.J., Beever D.E., Owen E., Vandenberghe I., Van Beeumen J., Bhat M.K. Biochemical characterization and mechanism of action of a thermostable beta-glucosidase purified from Thermoascus aurantiacus. Biochem J 2001, 353:117-127.
    • (2001) Biochem J , vol.353 , pp. 117-127
    • Parry, N.J.1    Beever, D.E.2    Owen, E.3    Vandenberghe, I.4    Van Beeumen, J.5    Bhat, M.K.6
  • 42
    • 84860852677 scopus 로고    scopus 로고
    • Thermoanaerobacterium thermosaccharolyticum beta-glucosidase: a glucose-tolerant enzyme with high specific activity for cellobiose
    • Pei J., Pang Q., Zhao L., Fan S., Shi H. Thermoanaerobacterium thermosaccharolyticum beta-glucosidase: a glucose-tolerant enzyme with high specific activity for cellobiose. Biotechnol Biofuels 2012, 5:1754-6834.
    • (2012) Biotechnol Biofuels , vol.5 , pp. 1754-6834
    • Pei, J.1    Pang, Q.2    Zhao, L.3    Fan, S.4    Shi, H.5
  • 43
    • 84887847362 scopus 로고    scopus 로고
    • Aspergillus niger beta-glucosidase has a cellulase-like tadpole molecular shape: insights into glycoside hydrolase family 3 (GH3) beta-glucosidase structure and function
    • Lima M.A., Oliveira-Neto M., Kadowaki M.A., Rosseto F.R., Prates E.T., Squina F.M., et al. Aspergillus niger beta-glucosidase has a cellulase-like tadpole molecular shape: insights into glycoside hydrolase family 3 (GH3) beta-glucosidase structure and function. J Biol Chem 2013, 288:32991-33005.
    • (2013) J Biol Chem , vol.288 , pp. 32991-33005
    • Lima, M.A.1    Oliveira-Neto, M.2    Kadowaki, M.A.3    Rosseto, F.R.4    Prates, E.T.5    Squina, F.M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.