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Volumn 44, Issue 1, 2009, Pages 2-12

Bioenergy: Sustainable fuels from biomass by yeast and fungal whole-cell biocatalysts

Author keywords

Biodiesel fuel; Bioenergy; Bioethanol; Biomass; Cell surface engineering; Whole cell biocatalyst

Indexed keywords

ACID HYDROLYSIS; ADVERSE EFFECTS; ALKALI CATALYSIS; BIODIESEL FUEL; BIOENERGY; CELL SURFACE ENGINEERING; ENERGY SECURITIES; ENZYMATIC METHODS; FUEL ETHANOLS; INTENSIVE RESEARCHES; LIGNOCELLULOSIC BIOMASS; LIPASE ENZYMES; PLANT OIL; SHORT REACTION TIME; SUSTAINABLE FUELS; TECHNOLOGICAL DEVELOPMENT; WHOLE-CELL BIOCATALYST; XYLANOLYTIC ENZYMES; YEAST CELL SURFACES; YEAST FERMENTATIONS;

EID: 60649111861     PISSN: 1369703X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bej.2008.11.016     Document Type: Review
Times cited : (110)

References (141)
  • 3
    • 43049115291 scopus 로고    scopus 로고
    • Trends in biotechnological production of fuel ethanol from different feedstocks
    • Sanchez O.J., and Cardona C.A. Trends in biotechnological production of fuel ethanol from different feedstocks. Bioresour. Technol. 99 (2008) 5270-5295
    • (2008) Bioresour. Technol. , vol.99 , pp. 5270-5295
    • Sanchez, O.J.1    Cardona, C.A.2
  • 4
    • 1642340053 scopus 로고    scopus 로고
    • Yeast cell-surface display-applications of molecular display
    • Kondo A., and Ueda M. Yeast cell-surface display-applications of molecular display. Appl. Microbiol. Biotechnol. 64 (2004) 28-40
    • (2004) Appl. Microbiol. Biotechnol. , vol.64 , pp. 28-40
    • Kondo, A.1    Ueda, M.2
  • 6
    • 0032447294 scopus 로고    scopus 로고
    • Molecular breeding of polysaccharide-utilizing yeast cells by surface engineering
    • Ueda M., Murai T., Shibasaki Y., Kamasawa N., Osumi M., and Tanaka A. Molecular breeding of polysaccharide-utilizing yeast cells by surface engineering. Ann. N. Y. Acad. Sci. 13 864 (1998) 528-537
    • (1998) Ann. N. Y. Acad. Sci. , vol.13 , Issue.864 , pp. 528-537
    • Ueda, M.1    Murai, T.2    Shibasaki, Y.3    Kamasawa, N.4    Osumi, M.5    Tanaka, A.6
  • 7
    • 0034045526 scopus 로고    scopus 로고
    • Genetic immobilization of proteins on the yeast cell surface
    • Ueda M., and Tanaka A. Genetic immobilization of proteins on the yeast cell surface. Biotechnol. Adv. 18 (2000) 121-140
    • (2000) Biotechnol. Adv. , vol.18 , pp. 121-140
    • Ueda, M.1    Tanaka, A.2
  • 9
    • 0020797283 scopus 로고
    • Winter rape oil fuel for diesel engines: recovery and utilization
    • Peterson C.L., Auld D.L., and Korus R.A. Winter rape oil fuel for diesel engines: recovery and utilization. J. Am. Oil. Chem. Soc. 60 (1983) 1579-1587
    • (1983) J. Am. Oil. Chem. Soc. , vol.60 , pp. 1579-1587
    • Peterson, C.L.1    Auld, D.L.2    Korus, R.A.3
  • 10
    • 0020796771 scopus 로고
    • Canola and high erucic rapeseed oil as substitutes for diesel fuel: preliminary tests
    • Strayer R.C., Blake J.A., and Craig W.K. Canola and high erucic rapeseed oil as substitutes for diesel fuel: preliminary tests. J. Am. Oil Chem. Soc. 60 (1983) 1587-1592
    • (1983) J. Am. Oil Chem. Soc. , vol.60 , pp. 1587-1592
    • Strayer, R.C.1    Blake, J.A.2    Craig, W.K.3
  • 11
    • 0035663815 scopus 로고    scopus 로고
    • Biodiesel fuel production by transesterification of oils
    • Fukuda H., Kondo A., and Noda H. Biodiesel fuel production by transesterification of oils. J. Biosci. Bioeng. 92 5 (2001) 405-416
    • (2001) J. Biosci. Bioeng. , vol.92 , Issue.5 , pp. 405-416
    • Fukuda, H.1    Kondo, A.2    Noda, H.3
  • 12
    • 0032907132 scopus 로고    scopus 로고
    • Biodiesel production: a review
    • Ma F., and Hanna M.A. Biodiesel production: a review. Bioresour. Technol. 70 (1999) 1-15
    • (1999) Bioresour. Technol. , vol.70 , pp. 1-15
    • Ma, F.1    Hanna, M.A.2
  • 14
    • 0034991004 scopus 로고    scopus 로고
    • Whole-cell biocatalyst for biodiesel fuel production utilizing Rhizopus oryzae cells immobilized within biomass support particles
    • Ban K., Hama S., Kaieda M., Matsumoto T., Kondo A., and Fukuda H. Whole-cell biocatalyst for biodiesel fuel production utilizing Rhizopus oryzae cells immobilized within biomass support particles. Biochem. Eng. J. 8 (2001) 39-43
    • (2001) Biochem. Eng. J. , vol.8 , pp. 39-43
    • Ban, K.1    Hama, S.2    Kaieda, M.3    Matsumoto, T.4    Kondo, A.5    Fukuda, H.6
  • 16
    • 33645716056 scopus 로고    scopus 로고
    • Display of active enzymes on the cell surface of Escherichia coli using PgsA anchor protein and their application to bioconversion
    • Narita J., Okano K., Tateno T., Tanino T., Sewaki T., Sung M.H., Fukuda H., and Kondo A. Display of active enzymes on the cell surface of Escherichia coli using PgsA anchor protein and their application to bioconversion. Appl. Microbiol. Biotechnol. 70 5 (2006) 564-572
    • (2006) Appl. Microbiol. Biotechnol. , vol.70 , Issue.5 , pp. 564-572
    • Narita, J.1    Okano, K.2    Tateno, T.3    Tanino, T.4    Sewaki, T.5    Sung, M.H.6    Fukuda, H.7    Kondo, A.8
  • 17
    • 0033827287 scopus 로고    scopus 로고
    • Stilage characterization and anaerobic treatment of ethanol stillage from conventional and cellulosic feed stocks
    • Wilkie A.C., Riedesel K.J., and Owend J.M. Stilage characterization and anaerobic treatment of ethanol stillage from conventional and cellulosic feed stocks. Biomass Bioenergy 19 (2000) 63-102
    • (2000) Biomass Bioenergy , vol.19 , pp. 63-102
    • Wilkie, A.C.1    Riedesel, K.J.2    Owend, J.M.3
  • 18
    • 84864543330 scopus 로고    scopus 로고
    • Sugar Research Institute, Australia p. 192
    • Bullock G.E. Ethanol from Sugar Cane (2002), Sugar Research Institute, Australia p. 192
    • (2002) Ethanol from Sugar Cane
    • Bullock, G.E.1
  • 20
    • 0033960040 scopus 로고    scopus 로고
    • Modelling of ethanol fermentation using Zymomonas mobilis ATCC 10988 grown on the media containing glucose and fructose
    • Lee W.G., and Huang C. Modelling of ethanol fermentation using Zymomonas mobilis ATCC 10988 grown on the media containing glucose and fructose. Biochem. Eng. J. 4 (2000) 217-227
    • (2000) Biochem. Eng. J. , vol.4 , pp. 217-227
    • Lee, W.G.1    Huang, C.2
  • 21
    • 0024835743 scopus 로고
    • Direct fermentation of raw corn starch to ethanol by yeast transformants containing a modified Rhizopus glucoamylase gene
    • Ashikari T., Kunisaki N., Matsumoto T., Amachi T., and Yoshizumi H. Direct fermentation of raw corn starch to ethanol by yeast transformants containing a modified Rhizopus glucoamylase gene. Appl. Microbiol. Biotechnol. 32 (1989) 129-133
    • (1989) Appl. Microbiol. Biotechnol. , vol.32 , pp. 129-133
    • Ashikari, T.1    Kunisaki, N.2    Matsumoto, T.3    Amachi, T.4    Yoshizumi, H.5
  • 22
    • 0024278853 scopus 로고
    • Fermentation of corn starch to ethanol with genetically engineered yeast
    • Inlow D., McRae J., and Ben-Bassat A. Fermentation of corn starch to ethanol with genetically engineered yeast. Biotechnol. Bioeng. 32 (1988) 227-234
    • (1988) Biotechnol. Bioeng. , vol.32 , pp. 227-234
    • Inlow, D.1    McRae, J.2    Ben-Bassat, A.3
  • 23
    • 0032102057 scopus 로고    scopus 로고
    • Ethanol production and fermentation characteristics of recombinant Saccharomyces cerevisiae strains grown on starch
    • Birol G., Onsan Z.I., Kirdar B., and Oliver S.G. Ethanol production and fermentation characteristics of recombinant Saccharomyces cerevisiae strains grown on starch. Enzyme Microb. Technol. 22 (1998) 672-677
    • (1998) Enzyme Microb. Technol. , vol.22 , pp. 672-677
    • Birol, G.1    Onsan, Z.I.2    Kirdar, B.3    Oliver, S.G.4
  • 24
    • 0028865920 scopus 로고
    • Development of yeast strains for the efficient utilization of starch: evaluation of constructs that express alpha amylase and glucoamylase separately or as bifunctional fusion proteins
    • De Moreas L., Astolfi-Filho S., and Oliver S.G. Development of yeast strains for the efficient utilization of starch: evaluation of constructs that express alpha amylase and glucoamylase separately or as bifunctional fusion proteins. Appl. Microbiol. Biotechnol. 43 (1995) 1067-1076
    • (1995) Appl. Microbiol. Biotechnol. , vol.43 , pp. 1067-1076
    • De Moreas, L.1    Astolfi-Filho, S.2    Oliver, S.G.3
  • 25
    • 0041392967 scopus 로고    scopus 로고
    • Starch fermentation by recombinant Saccharomyces cerevisiae strains expressing the α-amylase and glucoamylase genes from Lipomyces kononenkoae and Saccharomyces fibuligera
    • Eksteen J.M., Van Rensburg P., Otero R.R.C., and Pretorius I.S. Starch fermentation by recombinant Saccharomyces cerevisiae strains expressing the α-amylase and glucoamylase genes from Lipomyces kononenkoae and Saccharomyces fibuligera. Biotechnol. Bioeng. 84 (2003) 639-646
    • (2003) Biotechnol. Bioeng. , vol.84 , pp. 639-646
    • Eksteen, J.M.1    Van Rensburg, P.2    Otero, R.R.C.3    Pretorius, I.S.4
  • 26
    • 0030994634 scopus 로고    scopus 로고
    • Yeast surface display for screening combinatorial polypeptide libraries
    • Boder E.T., and Wittrup K.D. Yeast surface display for screening combinatorial polypeptide libraries. Nat. Biotechnol. 15 (1997) 553-557
    • (1997) Nat. Biotechnol. , vol.15 , pp. 553-557
    • Boder, E.T.1    Wittrup, K.D.2
  • 28
    • 0031767473 scopus 로고    scopus 로고
    • Assimilation of cellooligosaccharides by a cell surface-engineered yeast expressing β-glucosidase and carboxymethylcellulase from Aspergillus aculeatus
    • Murai T., Ueda M., Kawaguchi T., Arai M., and Tanaka A. Assimilation of cellooligosaccharides by a cell surface-engineered yeast expressing β-glucosidase and carboxymethylcellulase from Aspergillus aculeatus. Appl. Environ. Microbiol. 64 (1998) 4857-4861
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 4857-4861
    • Murai, T.1    Ueda, M.2    Kawaguchi, T.3    Arai, M.4    Tanaka, A.5
  • 29
    • 0034760935 scopus 로고    scopus 로고
    • Development of novel whole-cell immunoadsorbents by yeast surface display of the IgG-binding domain
    • Nakamura Y., Shibasaki S., Ueda M., Tanaka A., Fukuda H., and Kondo A. Development of novel whole-cell immunoadsorbents by yeast surface display of the IgG-binding domain. Appl. Microbiol. Biotechnol. 57 (2001) 500-505
    • (2001) Appl. Microbiol. Biotechnol. , vol.57 , pp. 500-505
    • Nakamura, Y.1    Shibasaki, S.2    Ueda, M.3    Tanaka, A.4    Fukuda, H.5    Kondo, A.6
  • 31
    • 0025785918 scopus 로고
    • The AGA1 product is involved in cell surface attachment of the Saccharomyces cerevisiae cell adhesion glycoprotein α-agglutinin
    • Roy A., Lu C.F., Marykwas D.L., Lipke P.N., and Kurjan J. The AGA1 product is involved in cell surface attachment of the Saccharomyces cerevisiae cell adhesion glycoprotein α-agglutinin. Mol. Cell. Biol. 11 (1991) 4196-4206
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 4196-4206
    • Roy, A.1    Lu, C.F.2    Marykwas, D.L.3    Lipke, P.N.4    Kurjan, J.5
  • 33
    • 0025996402 scopus 로고
    • Saccharomyces cerevisiae a- and α-agglutinin: characterization of their molecular interaction
    • Cappellaro C., Hauser K., Mrsa V., Watzele M., Watzele G., Gruber C., and Tanner W. Saccharomyces cerevisiae a- and α-agglutinin: characterization of their molecular interaction. EMBO J. 10 (1991) 4081-4088
    • (1991) EMBO J. , vol.10 , pp. 4081-4088
    • Cappellaro, C.1    Hauser, K.2    Mrsa, V.3    Watzele, M.4    Watzele, G.5    Gruber, C.6    Tanner, W.7
  • 35
    • 0031553517 scopus 로고    scopus 로고
    • Alcohol fermentation of starch by a genetic recombinant yeast having glucoamylase activity
    • Nakamura Y., Kobayashi F., Ohnaga M., and Sawada T. Alcohol fermentation of starch by a genetic recombinant yeast having glucoamylase activity. Biotechnol. Bioeng. 53 (1997) 21-25
    • (1997) Biotechnol. Bioeng. , vol.53 , pp. 21-25
    • Nakamura, Y.1    Kobayashi, F.2    Ohnaga, M.3    Sawada, T.4
  • 36
    • 0028865920 scopus 로고
    • Development of yeast strains for the efficient utilization of starch: evaluation of constructs that express α-amylase and glucoamylase separately or as bifunctional fusion proteins
    • Moreas L.M.P., Astolfi-filho S., and Oliver S.G. Development of yeast strains for the efficient utilization of starch: evaluation of constructs that express α-amylase and glucoamylase separately or as bifunctional fusion proteins. Appl. Microbiol. Technol. 43 (1995) 1067-1076
    • (1995) Appl. Microbiol. Technol. , vol.43 , pp. 1067-1076
    • Moreas, L.M.P.1    Astolfi-filho, S.2    Oliver, S.G.3
  • 37
    • 0037036093 scopus 로고    scopus 로고
    • Efficient ethanol production from starch through development of novel flocculent yeast strains displaying glucoamylase and co-displaying or secreting α-amylase
    • Shigechi H., Uyama K., Fujita T., Matsumoto T., Ueda M., Tanaka A., Fukuda H., and Kondo A. Efficient ethanol production from starch through development of novel flocculent yeast strains displaying glucoamylase and co-displaying or secreting α-amylase. J. Mol. Catal. B 17 (2002) 179-187
    • (2002) J. Mol. Catal. B , vol.17 , pp. 179-187
    • Shigechi, H.1    Uyama, K.2    Fujita, T.3    Matsumoto, T.4    Ueda, M.5    Tanaka, A.6    Fukuda, H.7    Kondo, A.8
  • 38
    • 60649091940 scopus 로고    scopus 로고
    • Energy saving direct ethanol production from low temperature cooked corn starch using a cell surface engineered yeast strain co-displaying glucoamylase and α-amylase
    • Shigechi H., Fujita Y., Koh J., Ueda M., Fukuda H., and Kondo A. Energy saving direct ethanol production from low temperature cooked corn starch using a cell surface engineered yeast strain co-displaying glucoamylase and α-amylase. Biochem. Eng. J. 350 (2000) 477-484
    • (2000) Biochem. Eng. J. , vol.350 , pp. 477-484
    • Shigechi, H.1    Fujita, Y.2    Koh, J.3    Ueda, M.4    Fukuda, H.5    Kondo, A.6
  • 39
    • 0027375692 scopus 로고
    • Molecular cloning and expression of two α-amylase genes from Streptococcus bovis 148 in Escherichia coli
    • Satoh E., Niimura Y., Uchimura T., Kozaki M., and Komagata K. Molecular cloning and expression of two α-amylase genes from Streptococcus bovis 148 in Escherichia coli. Appl. Environ. Microbiol. 59 (1993) 3669-3673
    • (1993) Appl. Environ. Microbiol. , vol.59 , pp. 3669-3673
    • Satoh, E.1    Niimura, Y.2    Uchimura, T.3    Kozaki, M.4    Komagata, K.5
  • 40
    • 4143107093 scopus 로고    scopus 로고
    • Direct ethanol production from raw corn starch via fermentation by use of novel surface engineered yeast strain co-displaying glucoamylase and α-amylase
    • Shigechi H., Koh J., Fujita Y., Matsumoto T., Bito Y., Ueda M., Satoh E., Fukuda H., and Kondo A. Direct ethanol production from raw corn starch via fermentation by use of novel surface engineered yeast strain co-displaying glucoamylase and α-amylase. Appl. Environ. Microbiol. 70 8 (2004) 5037-5040
    • (2004) Appl. Environ. Microbiol. , vol.70 , Issue.8 , pp. 5037-5040
    • Shigechi, H.1    Koh, J.2    Fujita, Y.3    Matsumoto, T.4    Bito, Y.5    Ueda, M.6    Satoh, E.7    Fukuda, H.8    Kondo, A.9
  • 41
    • 0036315808 scopus 로고    scopus 로고
    • Deletion analysis of the C-terminal region of the α-amylase of Bacillus sp. strain TS-23
    • Lo H.F., Lin L.L., Chiang W.Y., Chie M.C., Hsu W.H., and Chang C.T. Deletion analysis of the C-terminal region of the α-amylase of Bacillus sp. strain TS-23. Arch. Microbiol. 178 (2002) 115-123
    • (2002) Arch. Microbiol. , vol.178 , pp. 115-123
    • Lo, H.F.1    Lin, L.L.2    Chiang, W.Y.3    Chie, M.C.4    Hsu, W.H.5    Chang, C.T.6
  • 42
    • 0034071629 scopus 로고    scopus 로고
    • Metabolic engineering applications to renewable resource utilization
    • Aristidou A., and Penttila M. Metabolic engineering applications to renewable resource utilization. Curr. Opin. Biotechnol. 11 (2000) 187-198
    • (2000) Curr. Opin. Biotechnol. , vol.11 , pp. 187-198
    • Aristidou, A.1    Penttila, M.2
  • 43
    • 0027345153 scopus 로고
    • Molecular biology of xylan degradation
    • Thomson J.A. Molecular biology of xylan degradation. FEMS Microbiol. Rev. 10 (1993) 65-82
    • (1993) FEMS Microbiol. Rev. , vol.10 , pp. 65-82
    • Thomson, J.A.1
  • 44
    • 0031890507 scopus 로고    scopus 로고
    • Molecular characterization and heterologous expression of the gene encoding a low-molecular-mass endoglucanase from Trichoderma reesei QM9414
    • Okada H., Tada K., Sekiya T., Yokoyama K., Takahashi A., Tohda H., Kumagai H., and Morikawa Y. Molecular characterization and heterologous expression of the gene encoding a low-molecular-mass endoglucanase from Trichoderma reesei QM9414. Appl. Environ. Microbiol. 64 (1998) 555-563
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 555-563
    • Okada, H.1    Tada, K.2    Sekiya, T.3    Yokoyama, K.4    Takahashi, A.5    Tohda, H.6    Kumagai, H.7    Morikawa, Y.8
  • 45
    • 0022969096 scopus 로고
    • Homology between cellulase genes of Trichoderma reesei: complete nucleotide sequence of the endoglucanase I gene
    • Penttila M., Lehtovaara P., Nevalainen H., Bhikhabhai R., and Knowles J. Homology between cellulase genes of Trichoderma reesei: complete nucleotide sequence of the endoglucanase I gene. Gene 45 (1986) 253-263
    • (1986) Gene , vol.45 , pp. 253-263
    • Penttila, M.1    Lehtovaara, P.2    Nevalainen, H.3    Bhikhabhai, R.4    Knowles, J.5
  • 46
    • 0028361655 scopus 로고
    • A novel, small endoglucanase gene, egl5, from Trichoderma reesei isolated by expression in yeast
    • Saloheimo A., Henrissat B., Hoffren A.M., Teleman O., and Penttila M. A novel, small endoglucanase gene, egl5, from Trichoderma reesei isolated by expression in yeast. Mol. Microbiol. 13 (1994) 219-228
    • (1994) Mol. Microbiol. , vol.13 , pp. 219-228
    • Saloheimo, A.1    Henrissat, B.2    Hoffren, A.M.3    Teleman, O.4    Penttila, M.5
  • 48
    • 0030669760 scopus 로고    scopus 로고
    • cDNA cloning of a Trichoderma reesei cellulase and demonstration of endoglucanase activity by expression in yeast
    • Saloheimo M., Nakari-Setäla T., Tenkanen M., and Penttila M. cDNA cloning of a Trichoderma reesei cellulase and demonstration of endoglucanase activity by expression in yeast. Eur. J. Biochem. 249 (1997) 584-591
    • (1997) Eur. J. Biochem. , vol.249 , pp. 584-591
    • Saloheimo, M.1    Nakari-Setäla, T.2    Tenkanen, M.3    Penttila, M.4
  • 49
    • 84966185447 scopus 로고
    • Synergism of cellulases from Trichoderma reesei in the degradation of cellulose
    • Henrissat B., Driguez H., Viet C., and Schülein M. Synergism of cellulases from Trichoderma reesei in the degradation of cellulose. BioTechnology 3 (1985) 722-726
    • (1985) BioTechnology , vol.3 , pp. 722-726
    • Henrissat, B.1    Driguez, H.2    Viet, C.3    Schülein, M.4
  • 50
    • 0023132478 scopus 로고
    • Homologous domains in Trichoderma reesei cellulolytic enzymes: gene sequence and expression of cellobiohydrolase II
    • Teeri T.T., Lehtovaara P., Kauppinen S., Salovouri I., and Knowles J. Homologous domains in Trichoderma reesei cellulolytic enzymes: gene sequence and expression of cellobiohydrolase II. Gene 51 (1987) 43-52
    • (1987) Gene , vol.51 , pp. 43-52
    • Teeri, T.T.1    Lehtovaara, P.2    Kauppinen, S.3    Salovouri, I.4    Knowles, J.5
  • 51
    • 0026717351 scopus 로고
    • Purification and characterization of two extracellular β-glucosidases from Trichoderma reesei
    • Chen H., Hayn M., and Esterbauer H. Purification and characterization of two extracellular β-glucosidases from Trichoderma reesei. Biochim. Biophys. Acta 1121 (1992) 54-60
    • (1992) Biochim. Biophys. Acta , vol.1121 , pp. 54-60
    • Chen, H.1    Hayn, M.2    Esterbauer, H.3
  • 52
    • 0032487130 scopus 로고    scopus 로고
    • Hydrolysis of microcrystalline cellulose by cellobiohydrolase I and endoglucanase II from Trichoderma reesei: adsorption, sugar production pattern, and synergism of the enzymes
    • Medve J., Karlsson J., Lee D., and Tjerneld F. Hydrolysis of microcrystalline cellulose by cellobiohydrolase I and endoglucanase II from Trichoderma reesei: adsorption, sugar production pattern, and synergism of the enzymes. Biotechnol. Bioeng. 59 (1998) 621-634
    • (1998) Biotechnol. Bioeng. , vol.59 , pp. 621-634
    • Medve, J.1    Karlsson, J.2    Lee, D.3    Tjerneld, F.4
  • 53
    • 0031149857 scopus 로고    scopus 로고
    • Crystalline cellulose degradation: new insight into the function of cellobiohydrolases
    • Teeri T.T. Crystalline cellulose degradation: new insight into the function of cellobiohydrolases. Trends Biotechnol. 15 (1997) 160-167
    • (1997) Trends Biotechnol. , vol.15 , pp. 160-167
    • Teeri, T.T.1
  • 54
    • 0025881549 scopus 로고
    • Synergism in cellulose systems
    • Woodward J. Synergism in cellulose systems. Bioresour. Technol. 36 (1991) 67-75
    • (1991) Bioresour. Technol. , vol.36 , pp. 67-75
    • Woodward, J.1
  • 55
    • 0028765765 scopus 로고
    • Adsorption and synergism of cellobiohydrolase I and II of Trichoderma reesei during hydrolysis of microcrystalline cellulose
    • Medve J., Stahlberg J., and Tjerneld F. Adsorption and synergism of cellobiohydrolase I and II of Trichoderma reesei during hydrolysis of microcrystalline cellulose. Biotechnol. Bioeng. 44 (1994) 1064-1073
    • (1994) Biotechnol. Bioeng. , vol.44 , pp. 1064-1073
    • Medve, J.1    Stahlberg, J.2    Tjerneld, F.3
  • 57
    • 0026639016 scopus 로고
    • Ethanol production from cellobiose, amorphous cellulose, and crystalline cellulose by recombinant Klebsiella oxytoca containing chromosomally integrated Zymomonas mobilis genes for ethanol production and plasmids expressing thermostable cellulase genes from Clostridium thermocellum
    • Wood B.E., and Ingram L.O. Ethanol production from cellobiose, amorphous cellulose, and crystalline cellulose by recombinant Klebsiella oxytoca containing chromosomally integrated Zymomonas mobilis genes for ethanol production and plasmids expressing thermostable cellulase genes from Clostridium thermocellum. Appl. Environ. Microbiol. 58 (1992) 2103-2110
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 2103-2110
    • Wood, B.E.1    Ingram, L.O.2
  • 58
    • 0034807361 scopus 로고    scopus 로고
    • Simultaneous saccharification and fermentation of amorphous cellulose to ethanol by recombinant Klebsiella oxytoca SZ21 without supplemental cellulose
    • Zhou S., and Ingram L.O. Simultaneous saccharification and fermentation of amorphous cellulose to ethanol by recombinant Klebsiella oxytoca SZ21 without supplemental cellulose. Biotechnol. Lett. 23 (2001) 1455-1462
    • (2001) Biotechnol. Lett. , vol.23 , pp. 1455-1462
    • Zhou, S.1    Ingram, L.O.2
  • 59
    • 0345643434 scopus 로고    scopus 로고
    • Novel SSF process for ethanol production from microcrystalline cellulose using the -integrated recombinant yeast, L2612GC
    • Cho K.M., and Yoo Y.J. Novel SSF process for ethanol production from microcrystalline cellulose using the -integrated recombinant yeast, L2612GC. J. Microbiol. Biotechnol. 9 (1999) 340-345
    • (1999) J. Microbiol. Biotechnol. , vol.9 , pp. 340-345
    • Cho, K.M.1    Yoo, Y.J.2
  • 60
    • 0029790621 scopus 로고    scopus 로고
    • Co-expression of a Phanerochaete chrysosporium cellobiohydrolase gene and a Butyrivibrio fibrisolvens endo-β-1,4-glucanase gene in Saccharomyces cerevisiae
    • Van Rensburg P., Van Zyl W.H., and Pretorius I.S. Co-expression of a Phanerochaete chrysosporium cellobiohydrolase gene and a Butyrivibrio fibrisolvens endo-β-1,4-glucanase gene in Saccharomyces cerevisiae. Curr. Genet. 30 (1996) 246-250
    • (1996) Curr. Genet. , vol.30 , pp. 246-250
    • Van Rensburg, P.1    Van Zyl, W.H.2    Pretorius, I.S.3
  • 61
    • 0032518904 scopus 로고    scopus 로고
    • Engineering yeast for efficient cellulose degradation
    • Van Rensburg P., Van Zyl W.H., and Pretorius I.S. Engineering yeast for efficient cellulose degradation. Yeast 14 (1998) 67-76
    • (1998) Yeast , vol.14 , pp. 67-76
    • Van Rensburg, P.1    Van Zyl, W.H.2    Pretorius, I.S.3
  • 63
    • 0036159062 scopus 로고    scopus 로고
    • Hydrolysis of lignocellulosic materials for ethanol production: a review
    • Sun Y., and Cheng J. Hydrolysis of lignocellulosic materials for ethanol production: a review. Bioresour. Technol. 83 (2002) 1-11
    • (2002) Bioresour. Technol. , vol.83 , pp. 1-11
    • Sun, Y.1    Cheng, J.2
  • 64
    • 0034922896 scopus 로고    scopus 로고
    • Fuel ethanol production from lignocellulose: a challenge for metabolic engineering and process integration
    • Zaldivar J., Nielsen J., and Olsson L. Fuel ethanol production from lignocellulose: a challenge for metabolic engineering and process integration. Appl. Microbiol. Biotechnol. 56 (2001) 17-34
    • (2001) Appl. Microbiol. Biotechnol. , vol.56 , pp. 17-34
    • Zaldivar, J.1    Nielsen, J.2    Olsson, L.3
  • 65
    • 0036135110 scopus 로고    scopus 로고
    • Improvement of cellulolytic properties of Clostridium cellulolyticum by metabolic engineering
    • Guedon E., Desvaux M., and Petitdemange H. Improvement of cellulolytic properties of Clostridium cellulolyticum by metabolic engineering. Appl. Environ. Microbiol. 68 (2002) 53-58
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 53-58
    • Guedon, E.1    Desvaux, M.2    Petitdemange, H.3
  • 66
    • 0035747257 scopus 로고    scopus 로고
    • The Clostridium cellulovorans cellulosome: an enzyme complex with plant cell wall degrading activity
    • Doi R.H., and Tamaru Y. The Clostridium cellulovorans cellulosome: an enzyme complex with plant cell wall degrading activity. Chem. Rec. 1 (2001) 24-32
    • (2001) Chem. Rec. , vol.1 , pp. 24-32
    • Doi, R.H.1    Tamaru, Y.2
  • 67
    • 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 (1999) 275-281
    • (1999) Trends Microbiol. , vol.7 , pp. 275-281
    • Shoham, Y.1    Lamed, R.2    Bayer, E.A.3
  • 68
    • 22044442406 scopus 로고    scopus 로고
    • The cellulosome of clostridium cellulolyticum
    • Desvaux M. The cellulosome of clostridium cellulolyticum. Enzyme Microb. Technol. 37 4 (2005) 373-385
    • (2005) Enzyme Microb. Technol. , vol.37 , Issue.4 , pp. 373-385
    • Desvaux, M.1
  • 69
    • 23744447992 scopus 로고    scopus 로고
    • Clostridium cellulolyticum: model organism of mesophilic cellulolytic clostridia
    • Desvaux M. Clostridium cellulolyticum: model organism of mesophilic cellulolytic clostridia. FEMS Microbiol. Rev. 29 4 (2005) 741-764
    • (2005) FEMS Microbiol. Rev. , vol.29 , Issue.4 , pp. 741-764
    • Desvaux, M.1
  • 70
    • 0032999856 scopus 로고    scopus 로고
    • δ-Integration of endo/exoglucanase and β-glucosidase genes into the yeast chromosomes for direct conversion of cellulose to ethanol
    • Cho K.M., Yoo Y.J., and Kang H.S. δ-Integration of endo/exoglucanase and β-glucosidase genes into the yeast chromosomes for direct conversion of cellulose to ethanol. Enzyme Microb. Technol. 25 (1999) 23-30
    • (1999) Enzyme Microb. Technol. , vol.25 , pp. 23-30
    • Cho, K.M.1    Yoo, Y.J.2    Kang, H.S.3
  • 71
    • 0027984011 scopus 로고
    • The cellulosome-a treasure-trove for biotechnology
    • Bayer E.A., Morag E., and Lamed R. The cellulosome-a treasure-trove for biotechnology. Trends Biotechnol. 12 (1994) 378-386
    • (1994) Trends Biotechnol. , vol.12 , pp. 378-386
    • Bayer, E.A.1    Morag, E.2    Lamed, R.3
  • 72
    • 2342638898 scopus 로고    scopus 로고
    • Synergistic saccharification, and direct fermentation to ethanol of amorphous cellulose by use of engineered yeast strain codisplaying three types of cellulolytic enzyme
    • Fujita Y., Ito J., Uyeda M., Fukuda H., and Kondo A. Synergistic saccharification, and direct fermentation to ethanol of amorphous cellulose by use of engineered yeast strain codisplaying three types of cellulolytic enzyme. Appl. Environ. Microbiol. 70 (2004) 1207-1212
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 1207-1212
    • Fujita, Y.1    Ito, J.2    Uyeda, M.3    Fukuda, H.4    Kondo, A.5
  • 73
    • 0022386956 scopus 로고
    • Microbial xylanolytic systems
    • Biely P. Microbial xylanolytic systems. Trends Biotechnol. 3 (1985) 286-290
    • (1985) Trends Biotechnol. , vol.3 , pp. 286-290
    • Biely, P.1
  • 74
    • 0032984477 scopus 로고    scopus 로고
    • Molecular and biotechnological aspects of xylanases
    • Kulkarni N., Shendye A., and Rao M. Molecular and biotechnological aspects of xylanases. FEMS Microbiol. Rev. 23 (1999) 411-456
    • (1999) FEMS Microbiol. Rev. , vol.23 , pp. 411-456
    • Kulkarni, N.1    Shendye, A.2    Rao, M.3
  • 75
    • 0020912407 scopus 로고
    • Utilization of xylose by bacteria, yeasts, and fungi
    • Jeffries T.W. Utilization of xylose by bacteria, yeasts, and fungi. Adv. Biochem. Eng. 27 (1983) 1-32
    • (1983) Adv. Biochem. Eng. , vol.27 , pp. 1-32
    • Jeffries, T.W.1
  • 76
    • 0034618210 scopus 로고    scopus 로고
    • Synergy between enzymes from Aspergillus involved in the degradation of plant cell wall polysaccharides
    • De Vries R.P., Kester H.C.M., Poulsen C.H., Benen J.A.E., and Visser J. Synergy between enzymes from Aspergillus involved in the degradation of plant cell wall polysaccharides. Carbohydr. Res. 327 (2000) 401-410
    • (2000) Carbohydr. Res. , vol.327 , pp. 401-410
    • De Vries, R.P.1    Kester, H.C.M.2    Poulsen, C.H.3    Benen, J.A.E.4    Visser, J.5
  • 77
    • 0031028023 scopus 로고    scopus 로고
    • The β-d-xylosidase of Trichoderma reesei is a multifunctional β-d-xylan xylohydrolase
    • Herrmann M.C., Vrsanska M., Jurickova M., Hirsch J., Biely P., and Kubicek C.P. The β-d-xylosidase of Trichoderma reesei is a multifunctional β-d-xylan xylohydrolase. Biochem. J. 321 (1997) 375-381
    • (1997) Biochem. J. , vol.321 , pp. 375-381
    • Herrmann, M.C.1    Vrsanska, M.2    Jurickova, M.3    Hirsch, J.4    Biely, P.5    Kubicek, C.P.6
  • 78
    • 0024729057 scopus 로고
    • Cellulose- and xylan-degrading enzymes of Aspergillus terreus and Aspergillus niger
    • Hrmova M., Biely P., and Vrsanska M. Cellulose- and xylan-degrading enzymes of Aspergillus terreus and Aspergillus niger. Enzyme Microb. Technol. 11 (1989) 610-616
    • (1989) Enzyme Microb. Technol. , vol.11 , pp. 610-616
    • Hrmova, M.1    Biely, P.2    Vrsanska, M.3
  • 79
    • 0036247302 scopus 로고    scopus 로고
    • Xylanase production in solid state fermentation by Aspergillus niger mutant using statistical experimental designs
    • Park Y.S., Kang S.W., Lee J.S., Hong S.I., and Kim S.W. Xylanase production in solid state fermentation by Aspergillus niger mutant using statistical experimental designs. Appl. Microbiol. Biotechnol. 58 (2002) 761-766
    • (2002) Appl. Microbiol. Biotechnol. , vol.58 , pp. 761-766
    • Park, Y.S.1    Kang, S.W.2    Lee, J.S.3    Hong, S.I.4    Kim, S.W.5
  • 80
    • 0001088039 scopus 로고
    • Trichoderma xylanases, their properties and application
    • Wong K.K.Y., and Saddler J.N. Trichoderma xylanases, their properties and application. Crit. Rev. Biotechnol. 12 (1992) 413-435
    • (1992) Crit. Rev. Biotechnol. , vol.12 , pp. 413-435
    • Wong, K.K.Y.1    Saddler, J.N.2
  • 81
    • 0028338985 scopus 로고
    • Three-dimensional structure of endo-1,4-xylanase II from Trichoderma reesei: two conformational states in the active site
    • Torronen A., Harkki A., and Rouvinen J. Three-dimensional structure of endo-1,4-xylanase II from Trichoderma reesei: two conformational states in the active site. EMBO J. 13 (1994) 2493-2501
    • (1994) EMBO J. , vol.13 , pp. 2493-2501
    • Torronen, A.1    Harkki, A.2    Rouvinen, J.3
  • 82
    • 0032931266 scopus 로고    scopus 로고
    • Sequence analysis, overexpression, and antisense inhibition of a β-xylosidase gene, xylA, from Aspergillus oryzae KBN616
    • Kitamoto N., Yoshino S., Ohmiya K., and Tsukagoshi N. Sequence analysis, overexpression, and antisense inhibition of a β-xylosidase gene, xylA, from Aspergillus oryzae KBN616. Appl. Environ. Microbiol. 65 (1999) 20-24
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 20-24
    • Kitamoto, N.1    Yoshino, S.2    Ohmiya, K.3    Tsukagoshi, N.4
  • 83
    • 0028805858 scopus 로고
    • Cloning and expression of an Aspergillus kawachii endo-1,4-β-xylanase gene in Saccharomyces cerevisiae
    • Crous J.M., Pretorius I.S., and Van Zyl W.H. Cloning and expression of an Aspergillus kawachii endo-1,4-β-xylanase gene in Saccharomyces cerevisiae. Curr. Genet. 28 (1995) 467-473
    • (1995) Curr. Genet. , vol.28 , pp. 467-473
    • Crous, J.M.1    Pretorius, I.S.2    Van Zyl, W.H.3
  • 84
    • 0030051146 scopus 로고    scopus 로고
    • Expression of a Trichoderma reesei β-xylanase gene (XYN2) in Saccharomyces cerevisiae
    • La Grange D.C., Pretorius I.S., and Van Zyl W.H. Expression of a Trichoderma reesei β-xylanase gene (XYN2) in Saccharomyces cerevisiae. Appl. Environ. Microbiol. 62 (1996) 1036-1044
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 1036-1044
    • La Grange, D.C.1    Pretorius, I.S.2    Van Zyl, W.H.3
  • 85
    • 0030045212 scopus 로고    scopus 로고
    • Expression of Aureobasidium pullulans xynA in, and secretion of the xylanase from, Saccharomyces cerevisiae
    • Li X.L., and Lijungdahl L.G. Expression of Aureobasidium pullulans xynA in, and secretion of the xylanase from, Saccharomyces cerevisiae. Appl. Environ. Microbiol. 62 (1996) 209-213
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 209-213
    • Li, X.L.1    Lijungdahl, L.G.2
  • 86
    • 0026688968 scopus 로고
    • Secretion of a Cryptococcus albidus xylanase in Saccharomyces cerevisiae
    • Moreau A., Durand S., and Morosoli R. Secretion of a Cryptococcus albidus xylanase in Saccharomyces cerevisiae. Gene 116 (1992) 109-113
    • (1992) Gene , vol.116 , pp. 109-113
    • Moreau, A.1    Durand, S.2    Morosoli, R.3
  • 87
    • 0029890518 scopus 로고    scopus 로고
    • Molecular cloning and expression in Saccharomyces cerevisiae of two Aspergillus nidulans xylanase genes
    • Perez-Gonzalez J.A., De Graff L.H., Visser J., and Ramon D. Molecular cloning and expression in Saccharomyces cerevisiae of two Aspergillus nidulans xylanase genes. Appl. Environ. Microbiol. 62 (1996) 2179-2182
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 2179-2182
    • Perez-Gonzalez, J.A.1    De Graff, L.H.2    Visser, J.3    Ramon, D.4
  • 88
    • 0030980134 scopus 로고    scopus 로고
    • Cloning of the Bacillus pumilus β-xylosidase gene (xynB) and its expression in Saccharomyces cerevisiae
    • La Grange D.C., Pretorius I.S., and Van Zyl W.H. Cloning of the Bacillus pumilus β-xylosidase gene (xynB) and its expression in Saccharomyces cerevisiae. Appl. Microbiol. Biotechnol. 47 (1997) 262-266
    • (1997) Appl. Microbiol. Biotechnol. , vol.47 , pp. 262-266
    • La Grange, D.C.1    Pretorius, I.S.2    Van Zyl, W.H.3
  • 89
    • 0029739169 scopus 로고    scopus 로고
    • Cloning of genes encoding α-l-arabinofuranosidase and β-xylosidase from Trichoderma reesei by expression in Saccharomyces cerevisiae
    • Margolles-Clark E., Tenkanen M., Nakari-Setala T., and Penttila M. Cloning of genes encoding α-l-arabinofuranosidase and β-xylosidase from Trichoderma reesei by expression in Saccharomyces cerevisiae. Appl. Environ. Microbiol. 62 (1996) 3840-3846
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 3840-3846
    • Margolles-Clark, E.1    Tenkanen, M.2    Nakari-Setala, T.3    Penttila, M.4
  • 90
    • 0035650539 scopus 로고    scopus 로고
    • Degradation of xylan to D-xylose by recombinant Saccharomyces cerevisiae coexpressing the Aspergillus niger β-xylosidase (xlnD) and the Trichoderma reesei xylanase II (xyn2) genes
    • La Grange D.C., Pretorius I.S., Claeyssens M., and Van Zyl W.H. Degradation of xylan to D-xylose by recombinant Saccharomyces cerevisiae coexpressing the Aspergillus niger β-xylosidase (xlnD) and the Trichoderma reesei xylanase II (xyn2) genes. Appl. Environ. Microbiol. 67 (2001) 5512-5519
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 5512-5519
    • La Grange, D.C.1    Pretorius, I.S.2    Claeyssens, M.3    Van Zyl, W.H.4
  • 91
    • 0033856888 scopus 로고    scopus 로고
    • Anaerobic xylose fermentation by recombinant Saccharomyces cerevisiae carrying XYL1, XYL2, and XKS1 in mineral medium chemostat cultures
    • Eliasson A., Christensson C., Wahlbom C.F., and Hahn-Hagerdal B. Anaerobic xylose fermentation by recombinant Saccharomyces cerevisiae carrying XYL1, XYL2, and XKS1 in mineral medium chemostat cultures. Appl. Environ. Microbiol. 66 (2000) 3381-3386
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 3381-3386
    • Eliasson, A.1    Christensson, C.2    Wahlbom, C.F.3    Hahn-Hagerdal, B.4
  • 92
    • 0031832290 scopus 로고    scopus 로고
    • Genetically engineered Saccharomyces yeast capable of effective cofermentation of glucose and xylose
    • Ho N.W.Y., Chen Z., and Brainard A. Genetically engineered Saccharomyces yeast capable of effective cofermentation of glucose and xylose. Appl. Environ. Microbiol. 64 (1998) 1852-1859
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 1852-1859
    • Ho, N.W.Y.1    Chen, Z.2    Brainard, A.3
  • 93
    • 0036208491 scopus 로고    scopus 로고
    • Reduced oxidative pentose phosphate pathway flux in recombinant xylose-utilizing Saccharomyces cerevisiae strains improves the ethanol yield from xylose
    • Jeppsson M., Johansson B., Hahn-Hägerdal B., and Gorwa-Grauslund M.F. Reduced oxidative pentose phosphate pathway flux in recombinant xylose-utilizing Saccharomyces cerevisiae strains improves the ethanol yield from xylose. Appl. Environ. Microbiol. 68 (2002) 1604-1609
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 1604-1609
    • Jeppsson, M.1    Johansson, B.2    Hahn-Hägerdal, B.3    Gorwa-Grauslund, M.F.4
  • 94
    • 0035458838 scopus 로고    scopus 로고
    • Xylulokinase overexpression in two strains of Saccharomyces cerevisiae also expressing xylose reductase and xylitol dehydrogenase and its effect on fermentation of xylose and lignocellulosic hydrolysate
    • Johansson B., Christensson C., Hobley T., and Hahn-Hagerdal B. Xylulokinase overexpression in two strains of Saccharomyces cerevisiae also expressing xylose reductase and xylitol dehydrogenase and its effect on fermentation of xylose and lignocellulosic hydrolysate. Appl. Environ. Microbiol. 67 (2001) 4249-4255
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 4249-4255
    • Johansson, B.1    Christensson, C.2    Hobley, T.3    Hahn-Hagerdal, B.4
  • 95
    • 0034740497 scopus 로고    scopus 로고
    • Differential expression of the Trichoderma reesei β-xylanase II (xyn2) gene in the xylose-fermenting yeast Pichia stipitis
    • Den Haan R., and Van Zyl W.H. Differential expression of the Trichoderma reesei β-xylanase II (xyn2) gene in the xylose-fermenting yeast Pichia stipitis. Appl. Microbiol. Biotechnol. 57 (2001) 521-527
    • (2001) Appl. Microbiol. Biotechnol. , vol.57 , pp. 521-527
    • Den Haan, R.1    Van Zyl, W.H.2
  • 96
    • 0042882508 scopus 로고    scopus 로고
    • Enhanced xylan degradation and utilisation by Pichia stipitis overproducing fungal xylanolytic enzymes
    • Den Haan R., and Van Zyl W.H. Enhanced xylan degradation and utilisation by Pichia stipitis overproducing fungal xylanolytic enzymes. Enzyme Microb. Technol. 33 (2003) 620-628
    • (2003) Enzyme Microb. Technol. , vol.33 , pp. 620-628
    • Den Haan, R.1    Van Zyl, W.H.2
  • 97
    • 0027171272 scopus 로고
    • Secretion of a Cryptococcus albidus xylanase in Pichia stipitis resulting in a xylan fermenting transformant
    • Morosoli R., Zalce E., and Durand S. Secretion of a Cryptococcus albidus xylanase in Pichia stipitis resulting in a xylan fermenting transformant. Curr. Genet. 24 (1993) 94-99
    • (1993) Curr. Genet. , vol.24 , pp. 94-99
    • Morosoli, R.1    Zalce, E.2    Durand, S.3
  • 98
    • 4644280289 scopus 로고    scopus 로고
    • Construction of a xylan fermenting yeast strain through codisplay of xylanolytic enzymes on the surface of xylose utilizing Saccharomyces cerevisiae cells
    • Katahira S., Fujita Y., Mizukie A., Fukuda H., and Kondo A. Construction of a xylan fermenting yeast strain through codisplay of xylanolytic enzymes on the surface of xylose utilizing Saccharomyces cerevisiae cells. Appl. Environ. Microbiol. 70 9 (2004) 5407-5414
    • (2004) Appl. Environ. Microbiol. , vol.70 , Issue.9 , pp. 5407-5414
    • Katahira, S.1    Fujita, Y.2    Mizukie, A.3    Fukuda, H.4    Kondo, A.5
  • 99
    • 0000607694 scopus 로고
    • Fermentative performance of bacteria and yeasts in lignocellulose hydrolysate
    • Olsson L., and Hahn-Hägerdal B. Fermentative performance of bacteria and yeasts in lignocellulose hydrolysate. Proc. Biochem. 28 (1993) 249-257
    • (1993) Proc. Biochem. , vol.28 , pp. 249-257
    • Olsson, L.1    Hahn-Hägerdal, B.2
  • 101
    • 0033856888 scopus 로고    scopus 로고
    • Anaerobic xylose fermentation by recombinant Saccharomyces cerevisiae carrying XYL1, XYL2, and XKS1 in minimal medium chemostat cultures
    • Eliasson A., Christensson C., Wahlbom C.F., and Hahn-Hägerdal B. Anaerobic xylose fermentation by recombinant Saccharomyces cerevisiae carrying XYL1, XYL2, and XKS1 in minimal medium chemostat cultures. Appl. Environ. Microbiol. 66 (2000) 3381-3386
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 3381-3386
    • Eliasson, A.1    Christensson, C.2    Wahlbom, C.F.3    Hahn-Hägerdal, B.4
  • 102
    • 1242264261 scopus 로고    scopus 로고
    • Metabolic engineering for improved fermentation of pentoses by yeasts
    • Jeffries T.W., and Jin Y.S. Metabolic engineering for improved fermentation of pentoses by yeasts. Appl. Microbiol. Biotechnol. 63 (2004) 495-509
    • (2004) Appl. Microbiol. Biotechnol. , vol.63 , pp. 495-509
    • Jeffries, T.W.1    Jin, Y.S.2
  • 103
    • 0021959310 scopus 로고
    • Properties of the NAD(P)H-dependent xylose reductase from the xylose-fermenting yeast Pichia stipitis
    • Verduyn C., van Kleef R., Frank J., Schreuder H., van Dijken J.P., and Scheffers W.A. Properties of the NAD(P)H-dependent xylose reductase from the xylose-fermenting yeast Pichia stipitis. Biochem. J. 226 (1985) 669-677
    • (1985) Biochem. J. , vol.226 , pp. 669-677
    • Verduyn, C.1    van Kleef, R.2    Frank, J.3    Schreuder, H.4    van Dijken, J.P.5    Scheffers, W.A.6
  • 104
    • 0025139414 scopus 로고
    • Purification, characterization, and amino terminal sequence of xylose reductase from Candida shehatae
    • Ho N.W., Lin F.P., Huang S., Andrews P.C., and Tsao G.T. Purification, characterization, and amino terminal sequence of xylose reductase from Candida shehatae. Enzyme Microb. Technol. 12 (1990) 33-39
    • (1990) Enzyme Microb. Technol. , vol.12 , pp. 33-39
    • Ho, N.W.1    Lin, F.P.2    Huang, S.3    Andrews, P.C.4    Tsao, G.T.5
  • 105
    • 0142124355 scopus 로고    scopus 로고
    • Cloning and characterization of xyl1 gene, encoding an NADH-preferring xylose reductase from Candida parapsilosis, and its functional expression in Candida tropicalis
    • Lee J.K., Bong-Seong K., and Sang-Yong K. Cloning and characterization of xyl1 gene, encoding an NADH-preferring xylose reductase from Candida parapsilosis, and its functional expression in Candida tropicalis. Appl. Environ. Microbiol. 69 (2003) 6179-6188
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 6179-6188
    • Lee, J.K.1    Bong-Seong, K.2    Sang-Yong, K.3
  • 106
    • 0032607356 scopus 로고    scopus 로고
    • Successful design and development of genetically engineered Saccharomyces yeasts for effective co-fermentation of glucose and xylose from cellulosic biomass to fuel ethanol
    • Ho N.W., Chen Z., Brainard A.P., and Sedlak M. Successful design and development of genetically engineered Saccharomyces yeasts for effective co-fermentation of glucose and xylose from cellulosic biomass to fuel ethanol. Adv. Biochem. Eng. Biotechnol. 65 (1999) 163-192
    • (1999) Adv. Biochem. Eng. Biotechnol. , vol.65 , pp. 163-192
    • Ho, N.W.1    Chen, Z.2    Brainard, A.P.3    Sedlak, M.4
  • 107
    • 0034878314 scopus 로고    scopus 로고
    • Conversion of xylose to ethanol by recombinant Saccharomyces cerevisiae: importance of xylulokinase (XKS1) and oxygen availability
    • Toivari M.H., Aristidou A., Ruohonen L., and Penttilä M. Conversion of xylose to ethanol by recombinant Saccharomyces cerevisiae: importance of xylulokinase (XKS1) and oxygen availability. Metab. Eng. 3 (2001) 236-249
    • (2001) Metab. Eng. , vol.3 , pp. 236-249
    • Toivari, M.H.1    Aristidou, A.2    Ruohonen, L.3    Penttilä, M.4
  • 108
    • 0242576754 scopus 로고    scopus 로고
    • Xylose and cellobiose fermentation to ethanol by the thermotolerant methylotrophic yeast Hansenula polymorpha
    • Ryabova O.B., Chmil O.M., and Sibirny A.A. Xylose and cellobiose fermentation to ethanol by the thermotolerant methylotrophic yeast Hansenula polymorpha. FEMS Yeast Res. 4 (2003) 157-164
    • (2003) FEMS Yeast Res. , vol.4 , pp. 157-164
    • Ryabova, O.B.1    Chmil, O.M.2    Sibirny, A.A.3
  • 109
    • 33749828025 scopus 로고    scopus 로고
    • Ethanol from lignocellulosic hydrolysate by a recombinant xylose- and cellooligosachharide-assimilating yeast strain
    • Katahira S., Mizuike A., Fukuda H., and Kondo A. Ethanol from lignocellulosic hydrolysate by a recombinant xylose- and cellooligosachharide-assimilating yeast strain. Appl. Mircobiol. Biotechnol. 72 (2006) 1136-1143
    • (2006) Appl. Mircobiol. Biotechnol. , vol.72 , pp. 1136-1143
    • Katahira, S.1    Mizuike, A.2    Fukuda, H.3    Kondo, A.4
  • 110
    • 44449171842 scopus 로고    scopus 로고
    • Improvement of ethanol productivity during xylose and glucose co-fermenttion by xylose-assimilating S. cerevisiae via expression of glucose transporter Sut 1
    • Katahira S., Ito M., Takema H., Fujita Y., Tanino T., Tanaka T., Fukuda H., and Kondo A. Improvement of ethanol productivity during xylose and glucose co-fermenttion by xylose-assimilating S. cerevisiae via expression of glucose transporter Sut 1. Enyme Microb. Technol. 43 (2008) 115-119
    • (2008) Enyme Microb. Technol. , vol.43 , pp. 115-119
    • Katahira, S.1    Ito, M.2    Takema, H.3    Fujita, Y.4    Tanino, T.5    Tanaka, T.6    Fukuda, H.7    Kondo, A.8
  • 111
    • 0020835361 scopus 로고
    • Variables affecting the yields of fatty esters from transesterified vegetable oils
    • Freedman B., Pryde E.H., and Mounts T.L. Variables affecting the yields of fatty esters from transesterified vegetable oils. J. Am. Oil Chem. Soc. 61 (1984) 1638-1643
    • (1984) J. Am. Oil Chem. Soc. , vol.61 , pp. 1638-1643
    • Freedman, B.1    Pryde, E.H.2    Mounts, T.L.3
  • 115
    • 0033736945 scopus 로고    scopus 로고
    • Continuous production of biodiesel fuel from vegetable oil using immobilized Candida antarctica lipase
    • Watanabe Y., Shimada Y., Sugihara A., Noda H., Fukuda H., and Tominaga Y. Continuous production of biodiesel fuel from vegetable oil using immobilized Candida antarctica lipase. J. Am. Oil Chem. Soc. 77 (2000) 355-360
    • (2000) J. Am. Oil Chem. Soc. , vol.77 , pp. 355-360
    • Watanabe, Y.1    Shimada, Y.2    Sugihara, A.3    Noda, H.4    Fukuda, H.5    Tominaga, Y.6
  • 118
    • 11844296097 scopus 로고    scopus 로고
    • Facilitatory effect of immobilized lipase-producing Rhizopus oryzae cells on acyl migration in biodiesel-fuel production
    • Oda M., Kaieda M., Hama S., Yamaji H., Kondo A., Izumoto E., and Fukuda H. Facilitatory effect of immobilized lipase-producing Rhizopus oryzae cells on acyl migration in biodiesel-fuel production. Biochem. Eng. J. 23 (2005) 45-51
    • (2005) Biochem. Eng. J. , vol.23 , pp. 45-51
    • Oda, M.1    Kaieda, M.2    Hama, S.3    Yamaji, H.4    Kondo, A.5    Izumoto, E.6    Fukuda, H.7
  • 119
    • 0037036126 scopus 로고    scopus 로고
    • Enzymatic alcoholysis for biodiesel fuel production and application of the reaction to oil processing
    • Shimada Y., Watanabe Y., Sugihara A., and Tominaga Y. Enzymatic alcoholysis for biodiesel fuel production and application of the reaction to oil processing. J. Mol. Catal. B: Enzymatic 17 (2002) 133-142
    • (2002) J. Mol. Catal. B: Enzymatic , vol.17 , pp. 133-142
    • Shimada, Y.1    Watanabe, Y.2    Sugihara, A.3    Tominaga, Y.4
  • 120
    • 35148885321 scopus 로고    scopus 로고
    • Rhizopus orzae IFO 4697l whole cell catalyzed methanolysis of crude and acidified rapeseed oils for biodiesel production in ter-butanol system
    • Li W., Du W., and Liu D. Rhizopus orzae IFO 4697l whole cell catalyzed methanolysis of crude and acidified rapeseed oils for biodiesel production in ter-butanol system. Process Biochem. 42 (2007) 1481-1485
    • (2007) Process Biochem. , vol.42 , pp. 1481-1485
    • Li, W.1    Du, W.2    Liu, D.3
  • 121
    • 0025157819 scopus 로고
    • Cell aggregation as a trigger for enhancement of intracellular lipase production by a Rhizopus species
    • Nakashima T., Kyotani T., Izumoto E., and Fukuda H. Cell aggregation as a trigger for enhancement of intracellular lipase production by a Rhizopus species. J. Ferment. Bioeng. 70 (1990) 83-89
    • (1990) J. Ferment. Bioeng. , vol.70 , pp. 83-89
    • Nakashima, T.1    Kyotani, T.2    Izumoto, E.3    Fukuda, H.4
  • 122
    • 33745784439 scopus 로고    scopus 로고
    • Lipase localization in Rhizopus oryzae cells immobilized within biomass support particles for use as whole-cell biocatalysts in biodiesel-fuel production
    • Hama S., Tamalampudi S., Fukumizu T., Miura K., yamaji H., Kondo A., and Fukuda H. Lipase localization in Rhizopus oryzae cells immobilized within biomass support particles for use as whole-cell biocatalysts in biodiesel-fuel production. J. Biosci. Bioeng. 101 4 (2006) 328-333
    • (2006) J. Biosci. Bioeng. , vol.101 , Issue.4 , pp. 328-333
    • Hama, S.1    Tamalampudi, S.2    Fukumizu, T.3    Miura, K.4    yamaji, H.5    Kondo, A.6    Fukuda, H.7
  • 123
    • 0027426916 scopus 로고
    • Whole cell biocatalysis in nonconventional media
    • Nikolova P., and Ward O.P. Whole cell biocatalysis in nonconventional media. J. Ind. Microbiol. Biotechnol 12 (1993) 76-86
    • (1993) J. Ind. Microbiol. Biotechnol , vol.12 , pp. 76-86
    • Nikolova, P.1    Ward, O.P.2
  • 124
    • 33847369923 scopus 로고    scopus 로고
    • Optimization of whole-cell catalyze methanolysis of soybean oil for biodiesel production using response surface methodology
    • Li W., Du W., and Liu D. Optimization of whole-cell catalyze methanolysis of soybean oil for biodiesel production using response surface methodology. J. Mol. Catal. B: Enzymatic 45 (2007) 122-127
    • (2007) J. Mol. Catal. B: Enzymatic , vol.45 , pp. 122-127
    • Li, W.1    Du, W.2    Liu, D.3
  • 125
    • 39749197534 scopus 로고    scopus 로고
    • Biodiesel production catalyzed by whole-cell lipase from Rhizopus chinensis
    • Qin H.E., Yan X.U., Teng Y., and Wang D. Biodiesel production catalyzed by whole-cell lipase from Rhizopus chinensis. Chin. J. Catal. 29 1 (2008) 41-46
    • (2008) Chin. J. Catal. , vol.29 , Issue.1 , pp. 41-46
    • Qin, H.E.1    Yan, X.U.2    Teng, Y.3    Wang, D.4
  • 126
    • 43849102878 scopus 로고    scopus 로고
    • Culture condition improvement for whole-cell lipase production in submerged fermentation by Rhizopus chinensis using statistical method
    • Teng Y., and Xu Y. Culture condition improvement for whole-cell lipase production in submerged fermentation by Rhizopus chinensis using statistical method. Bioresour. Technol. 99 (2008) 3900-3907
    • (2008) Bioresour. Technol. , vol.99 , pp. 3900-3907
    • Teng, Y.1    Xu, Y.2
  • 127
  • 128
    • 34247636646 scopus 로고    scopus 로고
    • Synthetic activity enhancement of membrane-bound lipase from Rhizopus chinensis by pretreatment with isooctane
    • Wang D., Xu Y., and Teng Y. Synthetic activity enhancement of membrane-bound lipase from Rhizopus chinensis by pretreatment with isooctane. Bioprocess Biosyst. Eng. 30 (2007) 147-155
    • (2007) Bioprocess Biosyst. Eng. , vol.30 , pp. 147-155
    • Wang, D.1    Xu, Y.2    Teng, Y.3
  • 129
    • 0033965278 scopus 로고    scopus 로고
    • Effect of free fatty acids on the permeability of 1,2-dimyristoyl-sn-glycero-3-phosphocholine bilayer at the main phase transition
    • Langer M., and Hui S.W. Effect of free fatty acids on the permeability of 1,2-dimyristoyl-sn-glycero-3-phosphocholine bilayer at the main phase transition. Biochem. Biophys. Acta 1463 (2000) 439-447
    • (2000) Biochem. Biophys. Acta , vol.1463 , pp. 439-447
    • Langer, M.1    Hui, S.W.2
  • 130
    • 0035036355 scopus 로고    scopus 로고
    • LUV's lipid composition modulates diffusion of bile acids
    • Locher U., and Leuschner U. LUV's lipid composition modulates diffusion of bile acids. Chem. Phys. Lipids 110 (2000) 165-171
    • (2000) Chem. Phys. Lipids , vol.110 , pp. 165-171
    • Locher, U.1    Leuschner, U.2
  • 131
    • 0031055097 scopus 로고    scopus 로고
    • Ethanol induces alterations in lipid composition of Saccahromyces cerevisiae in the presence of exogenous fatty acid
    • Mizoguchi H., and Hara S. Ethanol induces alterations in lipid composition of Saccahromyces cerevisiae in the presence of exogenous fatty acid. J. Ferment. Bioeng. 81 (1997) 12-16
    • (1997) J. Ferment. Bioeng. , vol.81 , pp. 12-16
    • Mizoguchi, H.1    Hara, S.2
  • 132
    • 4444300886 scopus 로고    scopus 로고
    • Effect of fatty acid membrane composition on whole-cell biocatalysts for biodiesel-fuel production
    • Hama S., Yamaji H., Kaieda M., Oda M., Kondo A., and Fukuda H. Effect of fatty acid membrane composition on whole-cell biocatalysts for biodiesel-fuel production. Biochem. Eng. J. 21 (2004) 155-160
    • (2004) Biochem. Eng. J. , vol.21 , pp. 155-160
    • Hama, S.1    Yamaji, H.2    Kaieda, M.3    Oda, M.4    Kondo, A.5    Fukuda, H.6
  • 133
    • 40249101011 scopus 로고    scopus 로고
    • Enzymatic production of biodiesel from jatropha oil: A comparative study of immobilized-whole cell and commercial lipases as a biocatalyst
    • Tamalampudi S., Talukder M.M.R., Hama S., Numata T., Kondo A., and Fukuda H. Enzymatic production of biodiesel from jatropha oil: A comparative study of immobilized-whole cell and commercial lipases as a biocatalyst. Biochem. Eng. J. 39 (2008) 185-189
    • (2008) Biochem. Eng. J. , vol.39 , pp. 185-189
    • Tamalampudi, S.1    Talukder, M.M.R.2    Hama, S.3    Numata, T.4    Kondo, A.5    Fukuda, H.6
  • 134
    • 0842326550 scopus 로고    scopus 로고
    • Biodiesel preparation by lipase-catalyzed transesetrification of jatropha oil
    • Shah S., Sharma S., and Gupta M.N. Biodiesel preparation by lipase-catalyzed transesetrification of jatropha oil. Enegry Fuels 18 (2004) 154-159
    • (2004) Enegry Fuels , vol.18 , pp. 154-159
    • Shah, S.1    Sharma, S.2    Gupta, M.N.3
  • 135
  • 136
    • 33947617349 scopus 로고    scopus 로고
    • Biodiesel from microalgae
    • Chisti Y. Biodiesel from microalgae. Biotechnol. Adv. 25 (2007) 294-306
    • (2007) Biotechnol. Adv. , vol.25 , pp. 294-306
    • Chisti, Y.1
  • 137
    • 39149105620 scopus 로고    scopus 로고
    • Biodiesel from microalgae beats bioethanol
    • Chisti Y. Biodiesel from microalgae beats bioethanol. Trends Biotechnol. 26 (2008) 126-131
    • (2008) Trends Biotechnol. , vol.26 , pp. 126-131
    • Chisti, Y.1
  • 138
    • 33947601150 scopus 로고    scopus 로고
    • Biodiesel fuel production in a packed-bed reactor using lipase-producing Rhizopus oryzae cells immobilized within biomass support particles
    • Hama S., Yamaji H., Fukumizu T., Numata T., Tamalampudi S., Kondo A., Noda H., and Fukuda H. Biodiesel fuel production in a packed-bed reactor using lipase-producing Rhizopus oryzae cells immobilized within biomass support particles. Biochem. Eng. J. 34 (2007) 273-278
    • (2007) Biochem. Eng. J. , vol.34 , pp. 273-278
    • Hama, S.1    Yamaji, H.2    Fukumizu, T.3    Numata, T.4    Tamalampudi, S.5    Kondo, A.6    Noda, H.7    Fukuda, H.8
  • 139
    • 0036727246 scopus 로고    scopus 로고
    • Construction of yeast strains with high cell surface lipase activity by using novel display systems based on the Flo1p flocculation functional domain
    • Matsumoto T., Fukuda H., Ueda M., Tanaka A., and Kondo A. Construction of yeast strains with high cell surface lipase activity by using novel display systems based on the Flo1p flocculation functional domain. Appl. Environ. Microbiol. 68 9 (2002) 4517-4522
    • (2002) Appl. Environ. Microbiol. , vol.68 , Issue.9 , pp. 4517-4522
    • Matsumoto, T.1    Fukuda, H.2    Ueda, M.3    Tanaka, A.4    Kondo, A.5
  • 140
    • 0034764034 scopus 로고    scopus 로고
    • Yeast whole-cell biocatalyst constructed by intracellular overproduction of Rhyzopus oryzae lipase is applicable to biodiesel fuel production
    • Matsumoto T., Takahashi S., Kaieda M., Ueda M., Tanaka A., Fukuda H., and Kondo A. Yeast whole-cell biocatalyst constructed by intracellular overproduction of Rhyzopus oryzae lipase is applicable to biodiesel fuel production. Appl. Microbiol. Biotechnol. 57 (2001) 515-520
    • (2001) Appl. Microbiol. Biotechnol. , vol.57 , pp. 515-520
    • Matsumoto, T.1    Takahashi, S.2    Kaieda, M.3    Ueda, M.4    Tanaka, A.5    Fukuda, H.6    Kondo, A.7
  • 141
    • 0034210138 scopus 로고    scopus 로고
    • Preparation of high-activity whole-cell biocatalyst by permeabilization of recombinant yeasts with alcohol
    • Kondo A., Liu Y., Furuta M., Fujita Y., Matsumoto T., and Fukuda H. Preparation of high-activity whole-cell biocatalyst by permeabilization of recombinant yeasts with alcohol. J. Biosci. Bioeng. 89 (2000) 554-558
    • (2000) J. Biosci. Bioeng. , vol.89 , pp. 554-558
    • Kondo, A.1    Liu, Y.2    Furuta, M.3    Fujita, Y.4    Matsumoto, T.5    Fukuda, H.6


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