메뉴 건너뛰기




Volumn 45, Issue 7, 2010, Pages 1141-1147

An efficient system for pre-delignification of gramineous biofuel feedstock in vitro: Application of a laccase from Pycnoporus sanguineus H275

Author keywords

Laccase; Lignin; Lignocellulose; Pre delignification; Pycnoporus sanguineus; White rot

Indexed keywords

BUILDING BLOCKES; EFFICIENT SYSTEMS; ENCODING GENES; EXPERIMENTAL CONDITIONS; HOMOLOGY MODELING; IN-VITRO; KINETIC CHARACTERIZATION; KLASON LIGNIN; LACCASE; LACCASES; MALDI-TOF; MICRO-FIBRILS; MICROSCOPIC OBSERVATIONS; N-GLYCOSYLATION SITES; PICHIA PASTORIS; PYCNOPORUS SANGUINEUS; RECOMBINANT LACCASE; REDUCING SUGARS; UNTREATED CONTROL; WHEAT STRAWS; WHITE ROT;

EID: 77954817592     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.procbio.2010.04.010     Document Type: Article
Times cited : (49)

References (39)
  • 1
    • 33947380509 scopus 로고    scopus 로고
    • Cellulosic ethanol: biofuel researchers prepare to reap a new harvest
    • Service R.F. Cellulosic ethanol: biofuel researchers prepare to reap a new harvest. Science 2007, 315:1488-1491.
    • (2007) Science , vol.315 , pp. 1488-1491
    • Service, R.F.1
  • 5
    • 0042039983 scopus 로고
    • Cellulose decomposition by aerobic mesophilic bacteria from soil. III. The effect of lignin
    • Fuller W.H., Norman A.G. Cellulose decomposition by aerobic mesophilic bacteria from soil. III. The effect of lignin. J Bacteriol 1943, 46:291-297.
    • (1943) J Bacteriol , vol.46 , pp. 291-297
    • Fuller, W.H.1    Norman, A.G.2
  • 6
    • 0028013536 scopus 로고
    • The structure and function of fungal laccases
    • Thurston C.F. The structure and function of fungal laccases. Microbiology 1994, 140:19-26.
    • (1994) Microbiology , vol.140 , pp. 19-26
    • Thurston, C.F.1
  • 7
    • 0000515906 scopus 로고    scopus 로고
    • Optimization of laccase production by Pycnoporus sanguineus in submerged liquid culture
    • Pointing S.B., Jones E.B.G., Vrijmoed L.L.P. Optimization of laccase production by Pycnoporus sanguineus in submerged liquid culture. Mycologia 2000, 92:139-144.
    • (2000) Mycologia , vol.92 , pp. 139-144
    • Pointing, S.B.1    Jones, E.B.G.2    Vrijmoed, L.L.P.3
  • 8
    • 0033942377 scopus 로고    scopus 로고
    • Decolorization of azo and triphenylmethane dyes by Pycnoporus sanguineus producing laccase as the sole phenoloxidase
    • Pointing S.B., Vrijmoed L.L.P. Decolorization of azo and triphenylmethane dyes by Pycnoporus sanguineus producing laccase as the sole phenoloxidase. World J Microbiol Biotechnol 2000, 16:317-318.
    • (2000) World J Microbiol Biotechnol , vol.16 , pp. 317-318
    • Pointing, S.B.1    Vrijmoed, L.L.P.2
  • 9
    • 77949300622 scopus 로고    scopus 로고
    • Ligninolytic fungal laccases and their biotechnological applications
    • Singh Arora D., Kumar Sharma R. Ligninolytic fungal laccases and their biotechnological applications. Appl Biochem Biotechnol 2010, 160:1760-1788.
    • (2010) Appl Biochem Biotechnol , vol.160 , pp. 1760-1788
    • Singh Arora, D.1    Kumar Sharma, R.2
  • 10
    • 0033846798 scopus 로고    scopus 로고
    • Isolation of a new laccase isoform from the white-rot fungi Pycnoporus cinnabarinus strain ss3
    • Otterbein L., Record E., Chereau D., Herpoël I., Asther M., Moukha S.M. Isolation of a new laccase isoform from the white-rot fungi Pycnoporus cinnabarinus strain ss3. Can J Microbiol 2000, 46:759-763.
    • (2000) Can J Microbiol , vol.46 , pp. 759-763
    • Otterbein, L.1    Record, E.2    Chereau, D.3    Herpoël, I.4    Asther, M.5    Moukha, S.M.6
  • 11
    • 33646154205 scopus 로고    scopus 로고
    • Laccases: blue enzymes for green chemistry
    • Riva S. Laccases: blue enzymes for green chemistry. Trends Biotechnol 2006, 24:219-226.
    • (2006) Trends Biotechnol , vol.24 , pp. 219-226
    • Riva, S.1
  • 12
    • 0035829516 scopus 로고    scopus 로고
    • Equilibrating metal-oxide cluster ensembles for oxidation reactions using oxygen in water
    • Weinstock I.A., Barbuzzi E.M.G., Wemple M.W., Cowan J.J., Reiner R.S., Sonnen D.M., et al. Equilibrating metal-oxide cluster ensembles for oxidation reactions using oxygen in water. Nature 2001, 414:191-195.
    • (2001) Nature , vol.414 , pp. 191-195
    • Weinstock, I.A.1    Barbuzzi, E.M.G.2    Wemple, M.W.3    Cowan, J.J.4    Reiner, R.S.5    Sonnen, D.M.6
  • 15
    • 0028873593 scopus 로고
    • Effects of incubation time and temperature on in vitro selective delignification of silver leaf oak by Ganoderma colossum
    • Adaskaveg J.E., Gilbertson R.L., Dunlap M.R. Effects of incubation time and temperature on in vitro selective delignification of silver leaf oak by Ganoderma colossum. Appl Environ Microbiol 1995, 61:138-144.
    • (1995) Appl Environ Microbiol , vol.61 , pp. 138-144
    • Adaskaveg, J.E.1    Gilbertson, R.L.2    Dunlap, M.R.3
  • 16
    • 0022502613 scopus 로고
    • Biodelignification of lemon grass and citronella bagasse by white-rot fungi
    • Rolz C., De Leon R., De Arriola M.C., De Cabrera S. Biodelignification of lemon grass and citronella bagasse by white-rot fungi. Appl Environ Microbiol 1986, 52:607-611.
    • (1986) Appl Environ Microbiol , vol.52 , pp. 607-611
    • Rolz, C.1    De Leon, R.2    De Arriola, M.C.3    De Cabrera, S.4
  • 18
    • 0022971421 scopus 로고
    • Palo podrido: model for extensive delignification of wood by Ganoderma applanatum
    • Dill I., Kraepelin G. Palo podrido: model for extensive delignification of wood by Ganoderma applanatum. Appl Environ Microbiol 1986, 52:1305-1312.
    • (1986) Appl Environ Microbiol , vol.52 , pp. 1305-1312
    • Dill, I.1    Kraepelin, G.2
  • 22
    • 33646454123 scopus 로고    scopus 로고
    • Properties of laccases produced by Pycnoporus sanguineus induced by 2,5-xylidine
    • Garcia T., Santiago M., Ulhoa C. Properties of laccases produced by Pycnoporus sanguineus induced by 2,5-xylidine. Biotechnol Lett 2006, 28:633-636.
    • (2006) Biotechnol Lett , vol.28 , pp. 633-636
    • Garcia, T.1    Santiago, M.2    Ulhoa, C.3
  • 24
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976, 72:248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford1
  • 25
    • 0006705202 scopus 로고
    • Acid-precipitable polymeric lignin: production and analysis
    • Academic Press
    • Crawford D.L., Pometto A.L., Willis A.W., Scott T.K. Acid-precipitable polymeric lignin: production and analysis. Methods of Enzymology 1988, vol.161. Academic Press, p. 35-47.
    • (1988) Methods of Enzymology , vol.161 , pp. 35-47
    • Crawford, D.L.1    Pometto, A.L.2    Willis, A.W.3    Scott, T.K.4
  • 27
    • 38049032931 scopus 로고    scopus 로고
    • Arrangement of cellulose microfibrils in the wheat straw cell wall
    • Yu H., Liu R., Shen D., Wu Z., Huang Y. Arrangement of cellulose microfibrils in the wheat straw cell wall. Carbohydr Polym 2008, 72:122-127.
    • (2008) Carbohydr Polym , vol.72 , pp. 122-127
    • Yu, H.1    Liu, R.2    Shen, D.3    Wu, Z.4    Huang, Y.5
  • 28
    • 0029910752 scopus 로고    scopus 로고
    • Detection of laccase activity in polyacryamide gels after electrophoresis under denaturing condition
    • Gonclaves S. Detection of laccase activity in polyacryamide gels after electrophoresis under denaturing condition. Biotechnol Tech 1996, 10:667-668.
    • (1996) Biotechnol Tech , vol.10 , pp. 667-668
    • Gonclaves, S.1
  • 29
    • 77954818075 scopus 로고    scopus 로고
    • Silver staining, digestion, and extraction of peptides from an acrylamide gel for MS analysis. Cold Spring Harbor Protocols 2006:pdb.prot4661.
    • Niessen S, McLeod I, Yates JR. Silver staining, digestion, and extraction of peptides from an acrylamide gel for MS analysis. Cold Spring Harbor Protocols 2006; 2006:pdb.prot4661.
    • (2006)
    • Niessen, S.1    McLeod, I.2    Yates, J.R.3
  • 30
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins D.N., Pappin D.J.C., Creasy D.M., Cottrell J.S. Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 1999, 20:3551-3567.
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.C.2    Creasy, D.M.3    Cottrell, J.S.4
  • 31
    • 0035168979 scopus 로고    scopus 로고
    • Isolation of five laccase gene sequences from the white-rot fungus Trametes sanguinea by PCR, and cloning, characterization and expression of the laccase cDNA in yeasts
    • Hoshida H., Nakao M., Kanazawa H., Kubo K., Hakukawa T., Morimasa K., et al. Isolation of five laccase gene sequences from the white-rot fungus Trametes sanguinea by PCR, and cloning, characterization and expression of the laccase cDNA in yeasts. J Biosci Bioeng 2001, 92:372-380.
    • (2001) J Biosci Bioeng , vol.92 , pp. 372-380
    • Hoshida, H.1    Nakao, M.2    Kanazawa, H.3    Kubo, K.4    Hakukawa, T.5    Morimasa, K.6
  • 32
    • 0037143788 scopus 로고    scopus 로고
    • Fermentation strategies for improved heterologous expression of laccase in Pichia pastoris
    • Hong F., Meinander N.Q., Jönsson L.J. Fermentation strategies for improved heterologous expression of laccase in Pichia pastoris. Biotechnol Bioeng 2002, 79:438-449.
    • (2002) Biotechnol Bioeng , vol.79 , pp. 438-449
    • Hong, F.1    Meinander, N.Q.2    Jönsson, L.J.3
  • 33
    • 2642622879 scopus 로고
    • Isolation and partial nucleotide sequence of the laccase gene from Neurospora crassa: amino acid sequence homology of the protein to human ceruloplasmin
    • Germann U.A., Lerch K. Isolation and partial nucleotide sequence of the laccase gene from Neurospora crassa: amino acid sequence homology of the protein to human ceruloplasmin. PNAS 1986, 83:8854-8858.
    • (1986) PNAS , vol.83 , pp. 8854-8858
    • Germann, U.A.1    Lerch, K.2
  • 34
    • 33750601808 scopus 로고    scopus 로고
    • Heterologous expression of lcc1 gene from Trametes trogii in Pichia pastoris and characterization of the recombinant enzyme
    • Colao M., Lupino S., Garzillo A., Buonocore V., Ruzzi M. Heterologous expression of lcc1 gene from Trametes trogii in Pichia pastoris and characterization of the recombinant enzyme. Microbial Cell Factories 2006, 5:31.
    • (2006) Microbial Cell Factories , vol.5 , pp. 31
    • Colao, M.1    Lupino, S.2    Garzillo, A.3    Buonocore, V.4    Ruzzi, M.5
  • 35
    • 1642527943 scopus 로고    scopus 로고
    • Global potential bioethanol production from wasted crops and crop residues
    • Kim S., Dale B.E. Global potential bioethanol production from wasted crops and crop residues. Biomass Bioenergy 2004, 26:361-375.
    • (2004) Biomass Bioenergy , vol.26 , pp. 361-375
    • Kim, S.1    Dale, B.E.2
  • 38
    • 0032959440 scopus 로고    scopus 로고
    • Overview of N- and O-linked oligosaccharide structures found in various yeast species
    • Gemmill T.R., Trimble R.B. Overview of N- and O-linked oligosaccharide structures found in various yeast species. Biochim Biophys Acta (BBA)-Gen Subjects 1999, 1426:227-237.
    • (1999) Biochim Biophys Acta (BBA)-Gen Subjects , vol.1426 , pp. 227-237
    • Gemmill, T.R.1    Trimble, R.B.2
  • 39
    • 0141905893 scopus 로고    scopus 로고
    • N-Linked glycosylation of native and recombinant cauliflower xyloglucan endotransglycosylase 16A
    • Henriksson H., Denman S.E., Campuzano I.D.G., Ademark P., Master E.R., Teeri T.T., et al. N-Linked glycosylation of native and recombinant cauliflower xyloglucan endotransglycosylase 16A. Biochem J 2003, 375:61-73.
    • (2003) Biochem J , vol.375 , pp. 61-73
    • Henriksson, H.1    Denman, S.E.2    Campuzano, I.D.G.3    Ademark, P.4    Master, E.R.5    Teeri, T.T.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.