메뉴 건너뛰기




Volumn 95, Issue 6, 2003, Pages 549-561

Application of microbial genes to recalcitrant biomass utilization and environmental conservation

Author keywords

Biomass; Cellulase; Cellulosome; Environmental conservation; Hydrogen; Microbial gene

Indexed keywords

BIOMASS; CROPS; ENVIRONMENTAL PROTECTION; HYDROGEN; MICROORGANISMS; PLANTS (BOTANY);

EID: 0038006957     PISSN: 13891723     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1389-1723(03)80161-5     Document Type: Review
Times cited : (35)

References (51)
  • 1
    • 0031468763 scopus 로고    scopus 로고
    • Structure of cellulases and their application
    • Ohmiya, K., Sakka, K., Karita, S., and Kimura, T.: Structure of cellulases and their application. Genet. Rev., 14, 365-414 (1997).
    • (1997) Genet. Rev. , vol.14 , pp. 365-414
    • Ohmiya, K.1    Sakka, K.2    Karita, S.3    Kimura, T.4
  • 2
    • 0033787896 scopus 로고    scopus 로고
    • Molecular breeding of cellulolytic microbes, plants, and animals for biomass utilization
    • Sakka, K., Kimura, T., Karita, S., and Ohmiya, K.: Molecular breeding of cellulolytic microbes, plants, and animals for biomass utilization. J. Biosci. Bioeng., 90, 227-233 (2000).
    • (2000) J. Biosci. Bioeng. , vol.90 , pp. 227-233
    • Sakka, K.1    Kimura, T.2    Karita, S.3    Ohmiya, K.4
  • 4
    • 0029645404 scopus 로고
    • Structures and mechanisms of glycosyl hydrolases
    • Davies, G. and Henrissat, B.: Structures and mechanisms of glycosyl hydrolases. Structure, 3, 853-859 (1995).
    • (1995) Structure , vol.3 , pp. 853-859
    • Davies, G.1    Henrissat, B.2
  • 5
    • 0029929874 scopus 로고    scopus 로고
    • Updating the sequence-based classification of glycosyl hydrolases
    • Henrissat, B. and Bairoch, A.: Updating the sequence-based classification of glycosyl hydrolases. Biochem. J., 316, 695-696 (1996).
    • (1996) Biochem. J. , vol.316 , pp. 695-696
    • Henrissat, B.1    Bairoch, A.2
  • 6
    • 0001594653 scopus 로고
    • Cellulose-binding domains: Classification and properties
    • Saddler, J. M. and Penner, M. (ed.). American Chemical Society, Washington, D.C.
    • Tomme, P., Warren, R. A. J., Miller, R. C., Jr., Kilburn, D. G., and Gilkes, N. R.: Cellulose-binding domains: classification and properties, p. 142-161. In Saddler, J. M. and Penner, M. (ed.), The enzyme degradation of insoluble polysaccharides. American Chemical Society, Washington, D.C. (1995).
    • (1995) The Enzyme Degradation of Insoluble Polysaccharides , pp. 142-161
    • Tomme, P.1    Warren, R.A.J.2    Miller R.C., Jr.3    Kilburn, D.G.4    Gilkes, N.R.5
  • 9
    • 0031799314 scopus 로고    scopus 로고
    • The cellulosome of Clostridium thermocellum
    • Beguin, P. and Alzari, P.: The cellulosome of Clostridium thermocellum. Biochem. Soc. Trans., 26, 178-185 (1998).
    • (1998) Biochem. Soc. Trans. , vol.26 , pp. 178-185
    • Beguin, P.1    Alzari, P.2
  • 10
    • 0033167973 scopus 로고    scopus 로고
    • The cellulosome concept as an efficient microbial strategy for the degradation of insoluble polysaccharides
    • Shoham, Y., Lamed, R., and Bayer, E. A.: The cellulosome concept as an efficient microbial strategy for the degradation of insoluble polysaccharides. Trends Microbiol., 7, 275-281 (1999).
    • (1999) Trends Microbiol. , vol.7 , pp. 275-281
    • Shoham, Y.1    Lamed, R.2    Bayer, E.A.3
  • 11
    • 0031857381 scopus 로고    scopus 로고
    • Cloning and DNA sequencing of the genes encoding Clostridium josui scaffolding protein CipA and cellulase CelD and identification of their gene products as major components of the cellulosome
    • Kakiuchi, M., Isui, A., Suzuki, K., Fujino, T., Fujino, E., Kimura, T., Karita, S., Sakka, K., and Ohmiya, K.: Cloning and DNA sequencing of the genes encoding Clostridium josui scaffolding protein CipA and cellulase CelD and identification of their gene products as major components of the cellulosome. J. Bacteriol., 180, 4303-4308 (1998).
    • (1998) J. Bacteriol. , vol.180 , pp. 4303-4308
    • Kakiuchi, M.1    Isui, A.2    Suzuki, K.3    Fujino, T.4    Fujino, E.5    Kimura, T.6    Karita, S.7    Sakka, K.8    Ohmiya, K.9
  • 12
    • 0027502582 scopus 로고
    • Organization of a Clostridium thermocellum gene cluster encoding the cellulosomal scaffolding protein CipA and a protein possibly involved in attachment of the cellulosome to the cell surface
    • Fujino, T., Beguin, P., and Aubert, J. P.: Organization of a Clostridium thermocellum gene cluster encoding the cellulosomal scaffolding protein CipA and a protein possibly involved in attachment of the cellulosome to the cell surface. J. Bacteriol., 175, 1891-1899 (1993).
    • (1993) J. Bacteriol. , vol.175 , pp. 1891-1899
    • Fujino, T.1    Beguin, P.2    Aubert, J.P.3
  • 14
    • 0034132054 scopus 로고    scopus 로고
    • Characterization of the cellulolytic complex (cellulosome) from Ruminococcus albus
    • Ohara, H., Karita, S., Kimura, T., Sakka, K., and Ohmiya, K.: Characterization of the cellulolytic complex (cellulosome) from Ruminococcus albus. Biosci. Biotechnol. Biochem., 64, 254-260 (2000).
    • (2000) Biosci. Biotechnol. Biochem. , vol.64 , pp. 254-260
    • Ohara, H.1    Karita, S.2    Kimura, T.3    Sakka, K.4    Ohmiya, K.5
  • 16
    • 0032754343 scopus 로고    scopus 로고
    • A novel cellulosomal scaffoldin from Acetivibrio cellulolyticus that contains a family-9 glycosyl hydrolase
    • Ding, S.-Y., Bayer, E. A., Steiner, D., Shoham, Y., and Lamed, R.: A novel cellulosomal scaffoldin from Acetivibrio cellulolyticus that contains a family-9 glycosyl hydrolase. J. Bacteriol., 181, 6720-6729 (1999).
    • (1999) J. Bacteriol. , vol.181 , pp. 6720-6729
    • Ding, S.-Y.1    Bayer, E.A.2    Steiner, D.3    Shoham, Y.4    Lamed, R.5
  • 18
    • 0035970297 scopus 로고    scopus 로고
    • Solution structure of a type I dockerin domain, a novel prokaryotic, extracellular calcium-binding domain
    • Lytle, B. L., Volkman, B. F., Westler, W. M., Heckman, M. P., and Wu, J. H.: Solution structure of a type I dockerin domain, a novel prokaryotic, extracellular calcium-binding domain. J. Mol. Biol., 307, 745-753 (2001).
    • (2001) J. Mol. Biol. , vol.307 , pp. 745-753
    • Lytle, B.L.1    Volkman, B.F.2    Westler, W.M.3    Heckman, M.P.4    Wu, J.H.5
  • 19
    • 0035971154 scopus 로고    scopus 로고
    • Cohesin-dockerin interaction in cellulosome assembly: A single hydroxyl group of a dockerin domain distinguishes between nonrecognition and high affinity recognition
    • Mechaly, A., Fierobe, H. P., Belaich, A., Belaich, J. P., Lamed, R., Shoham, Y., and Bayer, E. A.: Cohesin-dockerin interaction in cellulosome assembly: a single hydroxyl group of a dockerin domain distinguishes between nonrecognition and high affinity recognition. J. Biol. Chem., 276, 9883-9888 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 9883-9888
    • Mechaly, A.1    Fierobe, H.P.2    Belaich, A.3    Belaich, J.P.4    Lamed, R.5    Shoham, Y.6    Bayer, E.A.7
  • 20
    • 0034878833 scopus 로고    scopus 로고
    • Cohesin-dockerin interactions of cellulosomal subunits of Clostridium cellulovorans
    • Park, J. S., Matano, Y., and Doi, R. H.: Cohesin-dockerin interactions of cellulosomal subunits of Clostridium cellulovorans. J. Bacteriol., 183, 5431-5435 (2001).
    • (2001) J. Bacteriol. , vol.183 , pp. 5431-5435
    • Park, J.S.1    Matano, Y.2    Doi, R.H.3
  • 21
    • 0347579849 scopus 로고    scopus 로고
    • Degradation of cellulose substrates by cellulosome chimeras. Substrate targeting versus proximity of enzyme components
    • Fierobe, H. P., Bayer, E. A., Tardif, C., Czjzek, M., Mechaly, A., Belaich, A., Lamed, R., Shoham, Y., and Belaich, J. P.: Degradation of cellulose substrates by cellulosome chimeras. Substrate targeting versus proximity of enzyme components. J. Biol. Chem., 277, 49621-49630 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 49621-49630
    • Fierobe, H.P.1    Bayer, E.A.2    Tardif, C.3    Czjzek, M.4    Mechaly, A.5    Belaich, A.6    Lamed, R.7    Shoham, Y.8    Belaich, J.P.9
  • 22
    • 0035877619 scopus 로고    scopus 로고
    • Design and production of active cellulosome chimeras. Selective incorporation of dockerin-containing enzymes into defined functional complexes
    • Fierobe, H. P., Mechaly, A., Tardif, C., Belaich, A., Lamed, R., Shoham, Y., Belaich, J. P., and Bayer, E. A.: Design and production of active cellulosome chimeras. Selective incorporation of dockerin-containing enzymes into defined functional complexes. J. Biol. Chem., 276, 21257-21261 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 21257-21261
    • Fierobe, H.P.1    Mechaly, A.2    Tardif, C.3    Belaich, A.4    Lamed, R.5    Shoham, Y.6    Belaich, J.P.7    Bayer, E.A.8
  • 23
    • 0036136163 scopus 로고    scopus 로고
    • Heterologous production of Clostridium cellulovorans EngB, using protease-deficient Bacillus subtilis, and preparation of active recombinant cellulosomes
    • Murashima, K., Chen, C. L., Kosugi, A., Tamaru, Y., Doi, R. H., and Wong, S. L.: Heterologous production of Clostridium cellulovorans EngB, using protease-deficient Bacillus subtilis, and preparation of active recombinant cellulosomes. J. Bacteriol., 184, 76-81 (2002).
    • (2002) J. Bacteriol. , vol.184 , pp. 76-81
    • Murashima, K.1    Chen, C.L.2    Kosugi, A.3    Tamaru, Y.4    Doi, R.H.5    Wong, S.L.6
  • 25
    • 0032724310 scopus 로고    scopus 로고
    • Expression of bacterial endoglucanase gene in tobacco increases digestibility of its cell wall fibers
    • Kawazu, T., Sun, J.-L., Shibata, M., Kimura, T., Sakka, K., and Ohmiya, K.: Expression of bacterial endoglucanase gene in tobacco increases digestibility of its cell wall fibers. J. Biosci. Bioeng., 88, 421-425 (1999).
    • (1999) J. Biosci. Bioeng. , vol.88 , pp. 421-425
    • Kawazu, T.1    Sun, J.-L.2    Shibata, M.3    Kimura, T.4    Sakka, K.5    Ohmiya, K.6
  • 26
    • 0038185184 scopus 로고    scopus 로고
    • Stable expression of thermostable xylanase of Clostridium thermocellum in cultured tobacco cells
    • Kimura, T., Mizutani, T., Sakka, K., and Ohmiya, K.: Stable expression of thermostable xylanase of Clostridium thermocellum in cultured tobacco cells. J. Biosci. Bioeng., 95, 397-400 (2003).
    • (2003) J. Biosci. Bioeng. , vol.95 , pp. 397-400
    • Kimura, T.1    Mizutani, T.2    Sakka, K.3    Ohmiya, K.4
  • 27
    • 0342444416 scopus 로고
    • GUS fusions: β-glucuronidase as a sensitive and versatile gene fusion marker in higher plants
    • Jefferson, R. A., Kavanagh, T. A., and Bevan, M. W.: GUS fusions: β-glucuronidase as a sensitive and versatile gene fusion marker in higher plants. EMBO J., 6, 3901-3907 (1987).
    • (1987) EMBO J. , vol.6 , pp. 3901-3907
    • Jefferson, R.A.1    Kavanagh, T.A.2    Bevan, M.W.3
  • 28
    • 0025335898 scopus 로고
    • Efficient transformation of Agrobacterium tumefaciens by electroporation
    • Mersereau, M., Pazour, G. J., and Das, A.: Efficient transformation of Agrobacterium tumefaciens by electroporation. Gene, 90, 149-151 (1990).
    • (1990) Gene , vol.90 , pp. 149-151
    • Mersereau, M.1    Pazour, G.J.2    Das, A.3
  • 29
    • 0015422557 scopus 로고
    • Interaction of halogenated pesticides and microorganisms: A review
    • Laskin, A. I. and Lechevalier, H. (ed.). CRC press, CL
    • Pfister, R. M.: Interaction of halogenated pesticides and microorganisms: a review, p. 1-33. In Laskin, A. I. and Lechevalier, H. (ed.), Handbook of microbiology. CRC press, CL (1973).
    • (1973) Handbook of Microbiology , pp. 1-33
    • Pfister, R.M.1
  • 30
    • 0038151901 scopus 로고    scopus 로고
    • Molecular breeding of transgenic rice expressing a xylanase domain of the xynA gene from Clostridium termocellum
    • in press
    • Kimura, T., Mizutani, T., Tanaka, T., Koyama, T., Sakka, K., and Ohmiya, K.: Molecular breeding of transgenic rice expressing a xylanase domain of the xynA gene from Clostridium termocellum. Appl. Microbiol. Biotechnol. (2003) (in press).
    • (2003) Appl. Microbiol. Biotechnol.
    • Kimura, T.1    Mizutani, T.2    Tanaka, T.3    Koyama, T.4    Sakka, K.5    Ohmiya, K.6
  • 31
    • 0019469975 scopus 로고
    • Biodegradation of chemicals of environmental concern
    • Alexander, M.: Biodegradation of chemicals of environmental concern. Science, 211, 132-138 (1981).
    • (1981) Science , vol.211 , pp. 132-138
    • Alexander, M.1
  • 32
  • 33
    • 0028874677 scopus 로고
    • Recombination of a 3-chlorobenzoate catabolic plasmid from Alcanigenes eutrophus NH9 mediated by direct repeat elements
    • Ogawa, N. and Miyashita, K.: Recombination of a 3-chlorobenzoate catabolic plasmid from Alcanigenes eutrophus NH9 mediated by direct repeat elements. Appl. Environ. Microbiol., 61, 3788-3795 (1995).
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 3788-3795
    • Ogawa, N.1    Miyashita, K.2
  • 34
    • 0031756487 scopus 로고    scopus 로고
    • Development of hybrid strains for the mineralization of chloriaromatics by patchwark assembley
    • Reineke, W.: Development of hybrid strains for the mineralization of chloriaromatics by patchwark assembley. Annu. Rev. Microbiol., 52, 287-331 (1998).
    • (1998) Annu. Rev. Microbiol. , vol.52 , pp. 287-331
    • Reineke, W.1
  • 36
    • 0034911456 scopus 로고    scopus 로고
    • The use of transgenic plants in the bioremediation of soils contaminated with trace elements
    • Kramer, U. and Chardonnens, A. N.: The use of transgenic plants in the bioremediation of soils contaminated with trace elements. Appl. Microbiol. Biotechnol., 55, 661-672 (2001).
    • (2001) Appl. Microbiol. Biotechnol. , vol.55 , pp. 661-672
    • Kramer, U.1    Chardonnens, A.N.2
  • 39
    • 0029763232 scopus 로고    scopus 로고
    • Hydrogen biotechnology: Progress and prospects
    • Benemann, J.: Hydrogen biotechnology: progress and prospects. Nat. Biotechnol., 14, 1101-1103 (1996).
    • (1996) Nat. Biotechnol. , vol.14 , pp. 1101-1103
    • Benemann, J.1
  • 40
    • 0030900026 scopus 로고    scopus 로고
    • Purification and characterization of two bifunctional chitinases/lysozymes extracellularly produced by Pseudomonas aeruginosa K-187 in a shrimp and crab shell powder medium
    • Wang, S. L. and Chang, W. T.: Purification and characterization of two bifunctional chitinases/lysozymes extracellularly produced by Pseudomonas aeruginosa K-187 in a shrimp and crab shell powder medium. Appl. Environ. Microbiol., 63, 380-386 (1997).
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 380-386
    • Wang, S.L.1    Chang, W.T.2
  • 42
    • 0029844652 scopus 로고    scopus 로고
    • Hydrogen production from industrial wastewater by anaerobic microflora in chemostat culture
    • Ueno, Y., Otsuka, S., and Morimoto, M.: Hydrogen production from industrial wastewater by anaerobic microflora in chemostat culture. J. Ferment. Bioeng., 92, 194-197 (1996).
    • (1996) J. Ferment. Bioeng. , vol.92 , pp. 194-197
    • Ueno, Y.1    Otsuka, S.2    Morimoto, M.3
  • 43
    • 0023103436 scopus 로고
    • Effect of various external factors on the fermentative production of hydrogen gas from glucose by Clostridium butyricum
    • Heyndrick, X. M., De Vos, P., Thibau, B., Stevebs, P., and DeLey, J.: Effect of various external factors on the fermentative production of hydrogen gas from glucose by Clostridium butyricum. Syst. Appl. Microbiol., 9, 163-168 (1987).
    • (1987) Syst. Appl. Microbiol. , vol.9 , pp. 163-168
    • Heyndrick, X.M.1    De Vos, P.2    Thibau, B.3    Stevebs, P.4    DeLey, J.5
  • 44
    • 0028338285 scopus 로고
    • Microbial conversion of arabinose and xylose to hydrogen by a newly isolated Clostridium sp. no. 2
    • Taguchi, F., Mizukami, N., Hasegawa, K., and Saito-Taki, K.: Microbial conversion of arabinose and xylose to hydrogen by a newly isolated Clostridium sp. no. 2. Can. J. Microbiol., 40, 228-233 (1994).
    • (1994) Can. J. Microbiol. , vol.40 , pp. 228-233
    • Taguchi, F.1    Mizukami, N.2    Hasegawa, K.3    Saito-Taki, K.4
  • 45
    • 0029239739 scopus 로고
    • Direct conversion of cellulosic materials to hydrogen by Clostridium sp. strain no. 2
    • Taguchi, F., Mizukami, N., Yamada, K., Hasegawa, K., and Saito-Taki, T.: Direct conversion of cellulosic materials to hydrogen by Clostridium sp. strain no. 2. Enzyme Microb. Technol., 17, 147-150 (1995).
    • (1995) Enzyme Microb. Technol. , vol.17 , pp. 147-150
    • Taguchi, F.1    Mizukami, N.2    Yamada, K.3    Hasegawa, K.4    Saito-Taki, T.5
  • 46
    • 0034210171 scopus 로고    scopus 로고
    • Identification and characterization of Clostridium paraputrificum M-21, a chitinolytic, mesophilic and hydrogen-producing bacterium
    • Evvyernie, D., Yamazaki, S., Morimoto, K., Karita, S., Kimura, T., Sakka, K., and Ohmiya, K.: Identification and characterization of Clostridium paraputrificum M-21, a chitinolytic, mesophilic and hydrogen-producing bacterium. J. Biosci. Bioeng., 89, 596-601 (2000).
    • (2000) J. Biosci. Bioeng. , vol.89 , pp. 596-601
    • Evvyernie, D.1    Yamazaki, S.2    Morimoto, K.3    Karita, S.4    Kimura, T.5    Sakka, K.6    Ohmiya, K.7
  • 47
    • 0027203953 scopus 로고
    • Isolation of a hydrogen-producing bacterium, Clostridium deijerinckii strain AM21B, from termites
    • Taguchi, F., Chang, J. D., Mizukami, N., Staito-Taki, T., and Hasegawa, K.: Isolation of a hydrogen-producing bacterium, Clostridium deijerinckii strain AM21B, from termites. Can. J. Microbiol., 39, 726-730 (1993).
    • (1993) Can. J. Microbiol. , vol.39 , pp. 726-730
    • Taguchi, F.1    Chang, J.D.2    Mizukami, N.3    Staito-Taki, T.4    Hasegawa, K.5
  • 48
    • 0023103436 scopus 로고
    • Effect of various external factors on the fermentative production of hydrogen gas from glucose by Clostridium butyricum strains in batch culture
    • Heyndrick, M., De Vos, P., Thibau, B., Stivens, P., and DeLey, J.: Effect of various external factors on the fermentative production of hydrogen gas from glucose by Clostridium butyricum strains in batch culture. Syst. Appl. Microbiol., 9, 163-168 (1987).
    • (1987) Syst. Appl. Microbiol. , vol.9 , pp. 163-168
    • Heyndrick, M.1    De Vos, P.2    Thibau, B.3    Stivens, P.4    DeLey, J.5
  • 49
    • 0030726362 scopus 로고    scopus 로고
    • Cloning, sequencing, and expression of the gene encoding Clostridium paraputrificum chitinase ChiB and analysis of the functions of novel cadherin-like domains and a chitin-binding domain
    • Morimoto, K., Karita, S., Kimura, T., Sakka, K., and Ohmiya, K.: Cloning, sequencing, and expression of the gene encoding Clostridium paraputrificum chitinase ChiB and analysis of the functions of novel cadherin-like domains and a chitin-binding domain. J. Bacteriol., 179, 7306-7314 (1997).
    • (1997) J. Bacteriol. , vol.179 , pp. 7306-7314
    • Morimoto, K.1    Karita, S.2    Kimura, T.3    Sakka, K.4    Ohmiya, K.5
  • 50
    • 0032906183 scopus 로고    scopus 로고
    • Sequencing, expression, and transcription analysis of the Clostridium paraputrificum chlA gene encoding chitinase ChiA
    • Morimoto, K., Karita, S., Kimura, T., Sakka, K., and Ohmiya, K.: Sequencing, expression, and transcription analysis of the Clostridium paraputrificum chlA gene encoding chitinase ChiA. Appl. Microbiol. Biotechnol., 51, 340-347 (1999).
    • (1999) Appl. Microbiol. Biotechnol. , vol.51 , pp. 340-347
    • Morimoto, K.1    Karita, S.2    Kimura, T.3    Sakka, K.4    Ohmiya, K.5
  • 51
    • 0027263622 scopus 로고
    • Clostridium perfringens-Escherichia coli shuttle vectors that carry single antibiotic resistance determinants
    • Bannam, T. L. and Rood, J. I.: Clostridium perfringens-Escherichia coli shuttle vectors that carry single antibiotic resistance determinants. Plasmid, 29, 233-235 (1993).
    • (1993) Plasmid , vol.29 , pp. 233-235
    • Bannam, T.L.1    Rood, J.I.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.