메뉴 건너뛰기




Volumn 63, Issue 1, 1997, Pages 169-177

Purification and characterization of extremely thermostable β- mannanase, β-mannosidase, and α-galactosidase from the hyperthermophilic eubacterium Thermotoga neapolitana 5068

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA GALACTOSIDASE; BETA MANNOSIDASE; GALACTOMANNAN;

EID: 0031023550     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/aem.63.1.169-177.1997     Document Type: Article
Times cited : (157)

References (50)
  • 1
    • 0029055215 scopus 로고
    • Extremozymes: Expanding the limits of biocatalysis
    • Adams, M. W. W., F. B. Perler, and R. M. Kelly. 1995. Extremozymes: expanding the limits of biocatalysis. Bio/Technology 13:662-668.
    • (1995) Bio/Technology , vol.13 , pp. 662-668
    • Adams, M.W.W.1    Perler, F.B.2    Kelly, R.M.3
  • 2
    • 0017578718 scopus 로고
    • Glycoprotein enzymes secreted by Aspergillus niger: Purification and properties of α-galactosidase
    • Adya, S., and A. E. Elbein. 1977. Glycoprotein enzymes secreted by Aspergillus niger: purification and properties of α-galactosidase. J. Bacteriol. 129: 850-856.
    • (1977) J. Bacteriol. , vol.129 , pp. 850-856
    • Adya, S.1    Elbein, A.E.2
  • 3
    • 85004245703 scopus 로고
    • Characterization of β-mannosidase of an alkalophilic Bacillus sp
    • Akino, T., N. Nakamura, and K. Horikoshi. 1988. Characterization of β-mannosidase of an alkalophilic Bacillus sp. Agric. Biol. Chem. 52:1459-1464.
    • (1988) Agric. Biol. Chem. , vol.52 , pp. 1459-1464
    • Akino, T.1    Nakamura, N.2    Horikoshi, K.3
  • 4
    • 85004488479 scopus 로고
    • Characterization of three β-mannanases of an alkalophilic Bacillus sp
    • Akino, T., N. Nakamura, and K. Horikoshi. 1988. Characterization of three β-mannanases of an alkalophilic Bacillus sp. Agric. Biol. Chem. 52:773-779.
    • (1988) Agric. Biol. Chem. , vol.52 , pp. 773-779
    • Akino, T.1    Nakamura, N.2    Horikoshi, K.3
  • 5
    • 0014670217 scopus 로고
    • Glycosidases of Aspergillus niger: Purification and characterization of α- and β-galactosidases and β-N-acetyl glucosaminidase
    • Bahl, O. P., and K. M. Agrawal. 1969. Glycosidases of Aspergillus niger: purification and characterization of α-and β-galactosidases and β-N-acetyl glucosaminidase. J. Biol. Chem. 244:2970-2978.
    • (1969) J. Biol. Chem. , vol.244 , pp. 2970-2978
    • Bahl, O.P.1    Agrawal, K.M.2
  • 6
    • 0022541209 scopus 로고
    • A new sulfur-reducing, extremely thermophilic eubacterium from a submarine thermal vent
    • Belkin, S., C. O. Wirsen, and H. W. Jannasch. 1986. A new sulfur-reducing, extremely thermophilic eubacterium from a submarine thermal vent. Appl. Environ. Microbiol. 51:1180-1185.
    • (1986) Appl. Environ. Microbiol. , vol.51 , pp. 1180-1185
    • Belkin, S.1    Wirsen, C.O.2    Jannasch, H.W.3
  • 7
    • 0026043410 scopus 로고
    • The characterization of a thermostable endo-β-1,4-mannanase cloned from "Caldocellum saccharolyticum"
    • Bicho, P. A., T. A. Clark, K. Mackie, H. W. Morgan, and R. M. Daniel. 1991. The characterization of a thermostable endo-β-1,4-mannanase cloned from "Caldocellum saccharolyticum". Appl. Microbiol. Biotechnol. 36:337-343.
    • (1991) Appl. Microbiol. Biotechnol. , vol.36 , pp. 337-343
    • Bicho, P.A.1    Clark, T.A.2    Mackie, K.3    Morgan, H.W.4    Daniel, R.M.5
  • 8
    • 0017848183 scopus 로고
    • Properties of a β-mannosidase from Aspergillus niger
    • Bouquelet, S., G. Spik, and J. Monteuil. 1978. Properties of a β-mannosidase from Aspergillus niger. Biochim. Biophys. Acta 522:521-530.
    • (1978) Biochim. Biophys. Acta , vol.522 , pp. 521-530
    • Bouquelet, S.1    Spik, G.2    Monteuil, J.3
  • 9
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 10
    • 0001224142 scopus 로고
    • Very stable enzymes from extremely thermophilic archaebacteria and eubacteria
    • Bragger, J. M., R. M. Daniels, T. Coolbear, and H. W. Morgan. 1989. Very stable enzymes from extremely thermophilic archaebacteria and eubacteria. Appl. Environ. Microbiol. 31:556-561.
    • (1989) Appl. Environ. Microbiol. , vol.31 , pp. 556-561
    • Bragger, J.M.1    Daniels, R.M.2    Coolbear, T.3    Morgan, H.W.4
  • 11
    • 0027587611 scopus 로고
    • Purification and characterization of a highly thermostable glucose isomerase produced by the extremely thermophilic eubacterium, Thermotoga maritima
    • Brown, S. H., C. Sjoholm, and R. M. Kelly. 1993. Purification and characterization of a highly thermostable glucose isomerase produced by the extremely thermophilic eubacterium, Thermotoga maritima. Biotechnol. Bioeng. 41:878-886.
    • (1993) Biotechnol. Bioeng. , vol.41 , pp. 878-886
    • Brown, S.H.1    Sjoholm, C.2    Kelly, R.M.3
  • 12
    • 0027293377 scopus 로고
    • Cloning and expression in Escherichia coli of Thermotoga neopolitana genes coding for enzymes of carbohydrate substrate synthesis
    • Dakhova, O. N., N. E. Kurepina, V. V. Zverlov, V. A. Svetlichnyi, and G. A. Velikodvorskaya. 1993. Cloning and expression in Escherichia coli of Thermotoga neopolitana genes coding for enzymes of carbohydrate substrate synthesis. Biochem. Biophys. Res. Commun. 194:1359-1364.
    • (1993) Biochem. Biophys. Res. Commun. , vol.194 , pp. 1359-1364
    • Dakhova, O.N.1    Kurepina, N.E.2    Zverlov, V.V.3    Svetlichnyi, V.A.4    Velikodvorskaya, G.A.5
  • 13
    • 84982024062 scopus 로고
    • Induction of α-galactosidase in Penicillium ochrochloron by guar (Cyamopsis tetragonobola) gum
    • Dey, P. M., S. Patel, and M. D. Brownleader. 1993. Induction of α-galactosidase in Penicillium ochrochloron by guar (Cyamopsis tetragonobola) gum. Biotechnol. Appl. Biochem. 17:361-371.
    • (1993) Biotechnol. Appl. Biochem. , vol.17 , pp. 361-371
    • Dey, P.M.1    Patel, S.2    Brownleader, M.D.3
  • 14
    • 0000910309 scopus 로고
    • Purification and characterization of a fungal β-mannanase
    • Eriksson, K. E., and M. Winell. 1968. Purification and characterization of a fungal β-mannanase. Acta Chem. Scand. 22:1924-1934.
    • (1968) Acta Chem. Scand. , vol.22 , pp. 1924-1934
    • Eriksson, K.E.1    Winell, M.2
  • 15
    • 0027253969 scopus 로고
    • Cloning and characterization of β-galactosidase and β-glucosidase hydrolyzing enzymes of Thermotoga maritima
    • Gabelsberger, J., W. Liehl, and K.-H. Schleifer. 1993. Cloning and characterization of β-galactosidase and β-glucosidase hydrolyzing enzymes of Thermotoga maritima. FEMS Microbiol. Lett. 109:131-138.
    • (1993) FEMS Microbiol. Lett. , vol.109 , pp. 131-138
    • Gabelsberger, J.1    Liehl, W.2    Schleifer, K.-H.3
  • 16
    • 0023184153 scopus 로고
    • Characterization of an outer membrane mannanase from Bacteroides ovatus
    • Gherardini, F. C., and A. A. Salyers. 1987. Characterization of an outer membrane mannanase from Bacteroides ovatus. J. Bacteriol. 169:2031-2037.
    • (1987) J. Bacteriol. , vol.169 , pp. 2031-2037
    • Gherardini, F.C.1    Salyers, A.A.2
  • 17
    • 0000049352 scopus 로고
    • Purification and some properties of α-galactosidase from Candida guilliermondii H-404
    • Hashimoto, H., C. Katayama, M. Goto, and S. Kitahata. 1993. Purification and some properties of α-galactosidase from Candida guilliermondii H-404. Biosci. Biotechnol. Biochem. 57:372-378.
    • (1993) Biosci. Biotechnol. Biochem. , vol.57 , pp. 372-378
    • Hashimoto, H.1    Katayama, C.2    Goto, M.3    Kitahata, S.4
  • 18
    • 85007967682 scopus 로고
    • Studies on the enzyme treatment of coffee beans. Purification of mannanase from Rhizopus niveus and its action on coffee mannan
    • Hashimoto, Y., and J. Fukumoto. 1969. Studies on the enzyme treatment of coffee beans. Purification of mannanase from Rhizopus niveus and its action on coffee mannan. Nippon Nogeikagaku Kaishi 43:317-322.
    • (1969) Nippon Nogeikagaku Kaishi , vol.43 , pp. 317-322
    • Hashimoto, Y.1    Fukumoto, J.2
  • 19
    • 0008711884 scopus 로고
    • Molecular biology of hemicellulases
    • M. P. Coughlan and G. P. Hazlewood (ed.), Portland Press Research Monosraph. Portland Press Ltd., Chapel Hill, N.C.
    • Hazlewood, G. P., and H. J. Gilbert. 1993. Molecular biology of hemicellulases, p. 103-126. In M. P. Coughlan and G. P. Hazlewood (ed.), Hemicellulose and hemicellulases. Portland Press Research Monosraph. Portland Press Ltd., Chapel Hill, N.C.
    • (1993) Hemicellulose and Hemicellulases , pp. 103-126
    • Hazlewood, G.P.1    Gilbert, H.J.2
  • 20
    • 0017654644 scopus 로고
    • Use of nucleopore filters for counting bacteria by fluorescence microscopy
    • Hobbie, J. E., R. J. Daley, and S. Jasper. 1977. Use of nucleopore filters for counting bacteria by fluorescence microscopy. Appl. Environ. Microbiol. 33:1225-1228.
    • (1977) Appl. Environ. Microbiol. , vol.33 , pp. 1225-1228
    • Hobbie, J.E.1    Daley, R.J.2    Jasper, S.3
  • 21
    • 0022522022 scopus 로고
    • Thermotoga maritima, sp. nov., represents a new genus of unique extremely thermophilic eubacteria growing up to 90°C
    • Huber, R., T. A. Langworthy, H. Konig, M. Thomm, C. R. Woese, U. B. Sletyr, and K. O. Stetter. 1986. Thermotoga maritima, sp. nov., represents a new genus of unique extremely thermophilic eubacteria growing up to 90°C. Arch. Microbiol. 144:324-333.
    • (1986) Arch. Microbiol. , vol.144 , pp. 324-333
    • Huber, R.1    Langworthy, T.A.2    Konig, H.3    Thomm, M.4    Woese, C.R.5    Sletyr, U.B.6    Stetter, K.O.7
  • 22
    • 0001218383 scopus 로고
    • Thermotoga neapolitana, sp. nov., of the extremely thermophilic, eubacterial genus thermotoga
    • Jannasch, H. W., R. Huber, S. Belkin, and K. O. Stetter. 1988. Thermotoga neapolitana, sp. nov., of the extremely thermophilic, eubacterial genus thermotoga. Arch. Microbiol. 150:103-104.
    • (1988) Arch. Microbiol. , vol.150 , pp. 103-104
    • Jannasch, H.W.1    Huber, R.2    Belkin, S.3    Stetter, K.O.4
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 24
    • 0026660023 scopus 로고
    • Purification and characterization of a novel thermostable 4-α-glucanotransferase of Thermotoga maritima cloned in Escherichia coli
    • Liebl, W., R. Feil, J. Gadelsberger, J. Kellermann, and K.-H. Schleifer. 1992. Purification and characterization of a novel thermostable 4-α-glucanotransferase of Thermotoga maritima cloned in Escherichia coli. Eur. J. Biochem. 207:81-88.
    • (1992) Eur. J. Biochem. , vol.207 , pp. 81-88
    • Liebl, W.1    Feil, R.2    Gadelsberger, J.3    Kellermann, J.4    Schleifer, K.-H.5
  • 25
    • 0025877830 scopus 로고
    • Cloning, sequence analysis, and expression in Escherichia coli of a gene coding for a β-mannanase from the extremely thermophilic bacterium "Caldocellum saccharolyticum."
    • Lüthi, E., N. B. Jasmat, R. A. Grayling, D. R. Love, and P. L. Bergquist. 1991. Cloning, sequence analysis, and expression in Escherichia coli of a gene coding for a β-mannanase from the extremely thermophilic bacterium "Caldocellum saccharolyticum." Appl. Environ. Microbiol. 57:694-700.
    • (1991) Appl. Environ. Microbiol. , vol.57 , pp. 694-700
    • Lüthi, E.1    Jasmat, N.B.2    Grayling, R.A.3    Love, D.R.4    Bergquist, P.L.5
  • 26
    • 0018035738 scopus 로고
    • A simple assay procedure for β-D-mannanase
    • McCleary, B. V. 1978. A simple assay procedure for β-D-mannanase. Carbohydr. Res. 67:213-221.
    • (1978) Carbohydr. Res. , vol.67 , pp. 213-221
    • McCleary, B.V.1
  • 27
    • 0000395079 scopus 로고
    • α-Galactosidase from lucerne and guar seed
    • McCleary, B. V. 1988. α-Galactosidase from lucerne and guar seed. Methods Enzymol. 160:627-632.
    • (1988) Methods Enzymol. , vol.160 , pp. 627-632
    • McCleary, B.V.1
  • 28
    • 77957095730 scopus 로고
    • Soluble, dye-labeled polysaccharides for the assay of endohydrolases
    • McCleary, B. V. 1988. Soluble, dye-labeled polysaccharides for the assay of endohydrolases. Methods Enzymol. 160:74-86.
    • (1988) Methods Enzymol. , vol.160 , pp. 74-86
    • McCleary, B.V.1
  • 30
    • 0001559287 scopus 로고
    • Action patterns and substrate-binding requirements of β-D-mannanase with mannosaccharides and mannan-type polysaccharides
    • McCleary, B. V., and N. K. Matheson. 1983. Action patterns and substrate-binding requirements of β-D-mannanase with mannosaccharides and mannan-type polysaccharides. Carbohydr. Res. 119:191-219.
    • (1983) Carbohydr. Res. , vol.119 , pp. 191-219
    • McCleary, B.V.1    Matheson, N.K.2
  • 31
    • 0022984526 scopus 로고
    • Enzymic analysis of polysaccharide structure
    • R. S. Tipson and D. Horton (ed.), Academic Press Ltd., London, United Kingdom
    • McCleary, B. V., and N. K. Matheson. 1986. Enzymic analysis of polysaccharide structure, p. 147-276. In R. S. Tipson and D. Horton (ed.), Advances in carbohydrate chemistry and biochemistry. Academic Press Ltd., London, United Kingdom.
    • (1986) Advances in Carbohydrate Chemistry and Biochemistry , pp. 147-276
    • McCleary, B.V.1    Matheson, N.K.2
  • 32
    • 10144234125 scopus 로고    scopus 로고
    • Characterization of extremely thermostable enzymatic breakers (α-1,6-galactosidase and β-1,4 mannanase) from the hyperthermophilic bacterium Thermotoga neapolitana 5068 for hydrolysis of guar gum
    • McCutchen, C. M., G. D. Duffaud, P. Leduc, A. R. H. Peterson, A. Tayal, S. A. Khan, and R. M. Kelly. 1996. Characterization of extremely thermostable enzymatic breakers (α-1,6-galactosidase and β-1,4 mannanase) from the hyperthermophilic bacterium Thermotoga neapolitana 5068 for hydrolysis of guar gum. Biotechnol. Bioeng. 52:332-339.
    • (1996) Biotechnol. Bioeng. , vol.52 , pp. 332-339
    • McCutchen, C.M.1    Duffaud, G.D.2    Leduc, P.3    Peterson, A.R.H.4    Tayal, A.5    Khan, S.A.6    Kelly, R.M.7
  • 33
    • 0000606416 scopus 로고
    • Crystal structures of mannan and glucomannans
    • Millane, R. P., and T. L. Hendrixson. 1994. Crystal structures of mannan and glucomannans. Carbohydr. Polym. 25:245-251.
    • (1994) Carbohydr. Polym. , vol.25 , pp. 245-251
    • Millane, R.P.1    Hendrixson, T.L.2
  • 34
    • 0028065197 scopus 로고
    • Identification and sequencing of the Thermotoga maritima lacZ gene, part of a divergently transcribed operon
    • Moore, J. B., P. Markiewicz, and J. H. Miller. 1994. Identification and sequencing of the Thermotoga maritima lacZ gene, part of a divergently transcribed operon. Gene 147:101-106.
    • (1994) Gene , vol.147 , pp. 101-106
    • Moore, J.B.1    Markiewicz, P.2    Miller, J.H.3
  • 36
    • 0027267888 scopus 로고
    • Purification and properties of extracellular β-mannanases produced by Enterococcus casseliflavus FL2121 isolated from decayed konjac
    • Oda, Y., T. Komaki, and K. Tonomura. 1993. Purification and properties of extracellular β-mannanases produced by Enterococcus casseliflavus FL2121 isolated from decayed konjac. J. Ferment. Bioeng. 76:14-18.
    • (1993) J. Ferment. Bioeng. , vol.76 , pp. 14-18
    • Oda, Y.1    Komaki, T.2    Tonomura, K.3
  • 37
    • 0000278629 scopus 로고
    • Production of β-mannanase and β-mannosidase by Enterococcus casseliflavus FL2121 isolated from decayed Konjac
    • Oda, Y., T. Komaki, and K. Tonomura. 1993. Production of β-mannanase and β-mannosidase by Enterococcus casseliflavus FL2121 isolated from decayed Konjac. Food Microbiol. 10:353-358.
    • (1993) Food Microbiol. , vol.10 , pp. 353-358
    • Oda, Y.1    Komaki, T.2    Tonomura, K.3
  • 38
    • 0019140123 scopus 로고
    • Isozymes of α-galactosidase from Bacillus stearothermophilus
    • Pederson, D. M., and R. E. and Goodman. 1980. Isozymes of α-galactosidase from Bacillus stearothermophilus. Can. J. Microbiol. 26:978-984.
    • (1980) Can. J. Microbiol. , vol.26 , pp. 978-984
    • Pederson, D.M.1    Goodman, R.E.2
  • 39
    • 0029959528 scopus 로고    scopus 로고
    • Growth physiology of the hyperthermophilic archaeon Thermococcus litoralis: Development of a sulfur-free defined medium, characterization of an exopolysaccharide, and evidence of biofilm formation
    • Rinker, K. D., and R. M. Kelly. 1996. Growth physiology of the hyperthermophilic archaeon Thermococcus litoralis: development of a sulfur-free defined medium, characterization of an exopolysaccharide, and evidence of biofilm formation. Appl. Environ. Microbiol. 62:4478-4485.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 4478-4485
    • Rinker, K.D.1    Kelly, R.M.2
  • 40
    • 0027292499 scopus 로고
    • Purification and molecular properties of an α-galactosidase synthesized and secreted by Aspergillus nidulans
    • Rios, S., A. M. Pedregosa, I. F. Monistrol, and F. Laborda. 1993. Purification and molecular properties of an α-galactosidase synthesized and secreted by Aspergillus nidulans. FEMS Microbiol. Lett. 112:35-42.
    • (1993) FEMS Microbiol. Lett. , vol.112 , pp. 35-42
    • Rios, S.1    Pedregosa, A.M.2    Monistrol, I.F.3    Laborda, F.4
  • 41
    • 0025913198 scopus 로고
    • Thermostable cellobiohydrolase from the thermophilic eubacterium Thermotoga sp strain FjSS3-B.1
    • Ruttersmith, L. D., and R. M. Daniel. 1991. Thermostable cellobiohydrolase from the thermophilic eubacterium Thermotoga sp strain FjSS3-B.1. Biochem. J. 277:887-890.
    • (1991) Biochem. J. , vol.277 , pp. 887-890
    • Ruttersmith, L.D.1    Daniel, R.M.2
  • 42
    • 0027483030 scopus 로고
    • Thermostable β-glucosidase and β-xylosidase from Thermotoga sp. strain FjSS3-B.1
    • Ruttersmith, L. D., and R. M. Daniel. 1993. Thermostable β-glucosidase and β-xylosidase from Thermotoga sp. strain FjSS3-B.1. Biochim. Biophys. Acta 1156:167-172.
    • (1993) Biochim. Biophys. Acta , vol.1156 , pp. 167-172
    • Ruttersmith, L.D.1    Daniel, R.M.2
  • 43
    • 0025870894 scopus 로고
    • An extremely thermostable xylanase from the thermophilic eubacteria Thermotoga
    • Simpson, H. D., U. R. Haufler, and R. M. Daniel. 1991. An extremely thermostable xylanase from the thermophilic eubacteria Thermotoga. Biochem. J. 277:413-417.
    • (1991) Biochem. J. , vol.277 , pp. 413-417
    • Simpson, H.D.1    Haufler, U.R.2    Daniel, R.M.3
  • 45
    • 0025002095 scopus 로고
    • Purification and characterization of thermostable β-mannanase and α-galactosidase from Bacillus stearothermophilus
    • Talbot, G., and J. Sygusch. 1990. Purification and characterization of thermostable β-mannanase and α-galactosidase from Bacillus stearothermophilus. Appl. Environ. Microbiol. 56:3505-3510.
    • (1990) Appl. Environ. Microbiol. , vol.56 , pp. 3505-3510
    • Talbot, G.1    Sygusch, J.2
  • 46
    • 0029018981 scopus 로고
    • xylA cloning and sequencing and biochemical characterization of xylose isomerase from Thermotoga neapolitana 5068
    • Vielle, C., J. M. Hess, R. M. Kelly, and J. G. Zeikus. 1995. xylA cloning and sequencing and biochemical characterization of xylose isomerase from Thermotoga neapolitana 5068. Appl. Environ. Microbiol. 61:1867-1875.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 1867-1875
    • Vielle, C.1    Hess, J.M.2    Kelly, R.M.3    Zeikus, J.G.4
  • 47
    • 0029008857 scopus 로고
    • Two extremely thermostable xylanases of the hyperthermophilic bacterium Thermotoga maritima MSB8
    • Winterhalter, C., and W. Liebl. 1995. Two extremely thermostable xylanases of the hyperthermophilic bacterium Thermotoga maritima MSB8. Appl. Environ. Microbiol. 61:1810-1815.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 1810-1815
    • Winterhalter, C.1    Liebl, W.2
  • 48
    • 0003034798 scopus 로고
    • Applications of hemicellulases in the food, feed mid pulp and paper industries
    • M. P. Coughlan and G. P. Hazlewood (ed.), Portland Press Research Monograph. Portland Press Ltd., Chapel Hill, N.C.
    • Wong, K. Y., and J. N. Saddler. 1993. Applications of hemicellulases in the food, feed mid pulp and paper industries, p. 127-143. In M. P. Coughlan and G. P. Hazlewood (ed.), Hemicellulose and hemicellulases. Portland Press Research Monograph. Portland Press Ltd., Chapel Hill, N.C.
    • (1993) Hemicellulose and Hemicellulases , pp. 127-143
    • Wong, K.Y.1    Saddler, J.N.2
  • 49
    • 0025672650 scopus 로고
    • Extracellular α-galactosidase (E.C.3.2.1.22) from Aspergillus ficuum NRRL 3135, purification and characterization
    • Zapater, I. G., A. H. Ullah, and R. J. Wodzinski. 1990. Extracellular α-galactosidase (E.C.3.2.1.22) from Aspergillus ficuum NRRL 3135, purification and characterization. Prep. Biochem. 20:263-296.
    • (1990) Prep. Biochem. , vol.20 , pp. 263-296
    • Zapater, I.G.1    Ullah, A.H.2    Wodzinski, R.J.3
  • 50
    • 0027287853 scopus 로고
    • Conditions of formation, purification, and characterization of an α-galactosidase of Trichoderma reesei RUT C-30
    • Zeilinger, S., A.-A. I. Kristufek, D. Hodits, and A. P. Kubicek. 1993. Conditions of formation, purification, and characterization of an α-galactosidase of Trichoderma reesei RUT C-30. Appl. Environ. Microbiol. 59:1347-1353.
    • (1993) Appl. Environ. Microbiol. , vol.59 , pp. 1347-1353
    • Zeilinger, S.1    Kristufek, A.-A.I.2    Hodits, D.3    Kubicek, A.P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.