메뉴 건너뛰기




Volumn 21, Issue 3, 1997, Pages 182-190

Purification and characterization of an extracellular β-glucosidase from the filamentous fungus Acremonium persicinum and its probable role in β-glucan degradation

Author keywords

glucan hydrolysis; glucosidase; Acremonium persicinum

Indexed keywords

AMINO ACIDS; BIODEGRADATION; CELL CULTURE; CHARACTERIZATION; CHROMATOGRAPHIC ANALYSIS; ENZYME INHIBITION; FUNGI; HYDROLYSIS; ION EXCHANGE; PH EFFECTS; PRECIPITATION (CHEMICAL); PURIFICATION;

EID: 0343052683     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0141-0229(96)00263-3     Document Type: Article
Times cited : (51)

References (57)
  • 2
    • 0020099053 scopus 로고
    • Fungal and other β-D-glucosidases: Their properties and applications
    • Woodward, J. and Wiseman, A. Fungal and other β-D-glucosidases: Their properties and applications. Enzyme Microb. Technol. 1984, 4, 73-79
    • (1984) Enzyme Microb. Technol. , vol.4 , pp. 73-79
    • Woodward, J.1    Wiseman, A.2
  • 3
    • 0020010564 scopus 로고
    • β-Glucosidase: Its role in cellulase synthesis and hydrolysis of cellulose
    • Shewale, J. G. β-Glucosidase: Its role in cellulase synthesis and hydrolysis of cellulose. Int. J. Biochem. 1982, 14, 435-443
    • (1982) Int. J. Biochem. , vol.14 , pp. 435-443
    • Shewale, J.G.1
  • 4
    • 0040542896 scopus 로고
    • Fungal cellulases. VI. Substrate and inhibitor specificity of the β-glucosidase of Stachybotrys atra
    • Jermyn, M. A. Fungal cellulases. VI. Substrate and inhibitor specificity of the β-glucosidase of Stachybotrys atra. Aust. J. Biol. Sci. 1955, 8, 577-602
    • (1955) Aust. J. Biol. Sci. , vol.8 , pp. 577-602
    • Jermyn, M.A.1
  • 6
    • 0006894477 scopus 로고
    • The aglycone specificity of plant glycosidases
    • Hösel, W. and Conn, E. E. The aglycone specificity of plant glycosidases. Trends Biochem. Sci. 1982, 7, 219-221
    • (1982) Trends Biochem. Sci. , vol.7 , pp. 219-221
    • Hösel, W.1    Conn, E.E.2
  • 7
    • 0014466894 scopus 로고
    • Extracellular enzyme system utilized by the rot fungus Stereum sanguinoletum for the breakdown of cellulose. IV. Separation of cellobiase and aryl-β-glucosidase activities
    • Bucht, B. and Eriksson, K. E. Extracellular enzyme system utilized by the rot fungus Stereum sanguinoletum for the breakdown of cellulose. IV. Separation of cellobiase and aryl-β-glucosidase activities. Arch. Biochem. Biophys. 1969, 129, 416-420
    • (1969) Arch. Biochem. Biophys. , vol.129 , pp. 416-420
    • Bucht, B.1    Eriksson, K.E.2
  • 9
    • 0028786543 scopus 로고
    • Purification and characterization of an intracellular β-glucosidase from Botrytis cinerea
    • Gueguen, Y., Chemardin, P., Arnaud, A., and Galzy, P. Purification and characterization of an intracellular β-glucosidase from Botrytis cinerea. Enzyme Microb. Technol. 1995, 17, 900-906
    • (1995) Enzyme Microb. Technol. , vol.17 , pp. 900-906
    • Gueguen, Y.1    Chemardin, P.2    Arnaud, A.3    Galzy, P.4
  • 10
    • 0017618890 scopus 로고
    • β-Glucosidase: Microbial production and effect on enzymatic hydrolysis of cellulose
    • Sternberg, D., Vijayakumar, P., and Reese, E. T. β-Glucosidase: Microbial production and effect on enzymatic hydrolysis of cellulose. Can. J. Microbiol. 1977, 23, 139-147
    • (1977) Can. J. Microbiol. , vol.23 , pp. 139-147
    • Sternberg, D.1    Vijayakumar, P.2    Reese, E.T.3
  • 11
    • 0020400010 scopus 로고
    • Purification and properties of the extracellular β-D-glucosidase of the cellulolytic fungus Trichoderma koningii
    • Wood, T. M. and McCrae, S. I. Purification and properties of the extracellular β-D-glucosidase of the cellulolytic fungus Trichoderma koningii. J. Gen. Microbiol. 1982, 128, 2973-2982
    • (1982) J. Gen. Microbiol. , vol.128 , pp. 2973-2982
    • Wood, T.M.1    McCrae, S.I.2
  • 12
    • 84954917277 scopus 로고
    • Enzymic properties of three β-glucosidases from Aspergillus aculeatus No. F-50
    • Sakamoto, R., Arai, M., and Murao, S. Enzymic properties of three β-glucosidases from Aspergillus aculeatus No. F-50. Agric. Biol. Chem. 1985, 49, 1283-1290
    • (1985) Agric. Biol. Chem. , vol.49 , pp. 1283-1290
    • Sakamoto, R.1    Arai, M.2    Murao, S.3
  • 13
    • 0024278187 scopus 로고
    • Synergism in cellulose hydrolysis by endoglucanases and exoglucanases purified from Trichoderma viride
    • Beldman, G., Voragen, A. G. J., Rombouts, F. M., and Pilnik, W. Synergism in cellulose hydrolysis by endoglucanases and exoglucanases purified from Trichoderma viride. Biotechnol. Bioeng. 1988, 31, 173-178
    • (1988) Biotechnol. Bioeng. , vol.31 , pp. 173-178
    • Beldman, G.1    Voragen, A.G.J.2    Rombouts, F.M.3    Pilnik, W.4
  • 14
    • 0026785486 scopus 로고
    • Degradation of extracellular β-(1,3)(1,6)-D-glucan by Botrytis cinerea
    • Stahmann, K.-P., Pielken, P., Schimz, K.-L., and Sahm, H. Degradation of extracellular β-(1,3)(1,6)-D-glucan by Botrytis cinerea. Appl. Environ. Microbiol. 1992, 58, 3347-3354
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 3347-3354
    • Stahmann, K.-P.1    Pielken, P.2    Schimz, K.-L.3    Sahm, H.4
  • 15
    • 0027332216 scopus 로고
    • Purification and characterisation of four extracellular 1,3-β-glucanases of Botrytis cinerea
    • Stahmann, K.-P., Schimz, K.-L., and Sahm, H. Purification and characterisation of four extracellular 1,3-β-glucanases of Botrytis cinerea. J. Gen. Microbiol 1993, 139, 2833-2840
    • (1993) J. Gen. Microbiol , vol.139 , pp. 2833-2840
    • Stahmann, K.-P.1    Schimz, K.-L.2    Sahm, H.3
  • 16
    • 0014745323 scopus 로고
    • Autolysis of extracellular glucans produced in vitro by a strain of Claviceps fusiformis
    • Dickerson, A. G., Mantle, P. G., and Szczyrbak, C. A. Autolysis of extracellular glucans produced in vitro by a strain of Claviceps fusiformis. J. Gen. Microbiol. 1970, 60, 403-415
    • (1970) J. Gen. Microbiol. , vol.60 , pp. 403-415
    • Dickerson, A.G.1    Mantle, P.G.2    Szczyrbak, C.A.3
  • 17
    • 0024428813 scopus 로고
    • 1,3-β-Glucanase, 1,6-β-glucanase, and β-glucosidase activities of Sclerotium glucanicum: Synthesis and properties
    • Rapp, P. 1,3-β-Glucanase, 1,6-β-glucanase, and β-glucosidase activities of Sclerotium glucanicum: Synthesis and properties. J. Gen. Microbiol. 1989, 135, 2847-2858
    • (1989) J. Gen. Microbiol. , vol.135 , pp. 2847-2858
    • Rapp, P.1
  • 18
    • 0026654729 scopus 로고
    • Formation, separation, and characterisation of three β-1,3-glucanases from Sclerotium glucanicum
    • Rapp, P. Formation, separation, and characterisation of three β-1,3-glucanases from Sclerotium glucanicum. Biochim. Biophys. Acta 1990, 1117, 7-14
    • (1990) Biochim. Biophys. Acta , vol.1117 , pp. 7-14
    • Rapp, P.1
  • 20
    • 0025994102 scopus 로고
    • Microbial β-glucanases different from cellulases
    • Bielecki, S. and Galas, E. Microbial β-glucanases different from cellulases. Crit. Rev. Biotechnol. 1991, 10, 275-304
    • (1991) Crit. Rev. Biotechnol. , vol.10 , pp. 275-304
    • Bielecki, S.1    Galas, E.2
  • 21
    • 0017813223 scopus 로고
    • Regulation of the 1,3-β-glucanase system in Penicillium italicum: Localization of the various enzymes and correlation with cell wall glucan mobilization and autolysis
    • Santos, T., Sanchez, M., Villanueva, J. R., and Nombela, C. Regulation of the 1,3-β-glucanase system in Penicillium italicum: Localization of the various enzymes and correlation with cell wall glucan mobilization and autolysis. J. Bacteriol. 1978, 133, 465-471
    • (1978) J. Bacteriol. , vol.133 , pp. 465-471
    • Santos, T.1    Sanchez, M.2    Villanueva, J.R.3    Nombela, C.4
  • 22
    • 0018409092 scopus 로고
    • The regulation of β-glucanase synthesis in fungi and yeast
    • Del Rey, F., García-Acha, I., and Nombela, C. The regulation of β-glucanase synthesis in fungi and yeast. J. Gen. Microbiol. 1979, 110, 83-89
    • (1979) J. Gen. Microbiol. , vol.110 , pp. 83-89
    • Del Rey, F.1    García-Acha, I.2    Nombela, C.3
  • 23
    • 84954970673 scopus 로고
    • Change of the structure of cell wall β-1,3-d-glucan with the growth of Neurospora crassa cells
    • Hiura, N., Honjyo, I., Nakajima, T., and Matsuda, K. Change of the structure of cell wall β-1,3-D-glucan with the growth of Neurospora crassa cells. Agric. Biol. Chem. 1984, 48, 1041-1047
    • (1984) Agric. Biol. Chem. , vol.48 , pp. 1041-1047
    • Hiura, N.1    Honjyo, I.2    Nakajima, T.3    Matsuda, K.4
  • 24
    • 0012005816 scopus 로고
    • Purification and some properties of two wall-associated (β1,3)glucanases from Neurospora crassa cells
    • Hiura, N., Kobayashi, M., Nakajima, T., and Matsuda, K. Purification and some properties of two wall-associated (β1,3)glucanases from Neurospora crassa cells. Agric. Biol. Chem. 1986, 50, 2461-2467
    • (1986) Agric. Biol. Chem. , vol.50 , pp. 2461-2467
    • Hiura, N.1    Kobayashi, M.2    Nakajima, T.3    Matsuda, K.4
  • 25
    • 85004579791 scopus 로고
    • Purification and some properties of an endo-β-1,6-glucanase from Neurospora crassa
    • Hiura, N., Nakajima, T., and Matsuda, K. Purification and some properties of an endo-β-1,6-glucanase from Neurospora crassa. Agric. Biol. Chem. 1987, 51, 3315-3321
    • (1987) Agric. Biol. Chem. , vol.51 , pp. 3315-3321
    • Hiura, N.1    Nakajima, T.2    Matsuda, K.3
  • 26
    • 85005633655 scopus 로고
    • Exopolysaccharide formation by isolates of Cephalosporium and Acremonium
    • Stasinopoulos, S. J. and Seviour, R. J. Exopolysaccharide formation by isolates of Cephalosporium and Acremonium. Mycol. Res. 1989, 92, 55-60
    • (1989) Mycol. Res. , vol.92 , pp. 55-60
    • Stasinopoulos, S.J.1    Seviour, R.J.2
  • 27
    • 0000948022 scopus 로고
    • Production and regulation of β-glucanases in Acremonium and Cephalosporium isolates
    • Pitson, S., Seviour, R. J., Bott, J., and Stasinopoulos, S. J. Production and regulation of β-glucanases in Acremonium and Cephalosporium isolates. Mycol. Res. 1991, 95, 352-356
    • (1991) Mycol. Res. , vol.95 , pp. 352-356
    • Pitson, S.1    Seviour, R.J.2    Bott, J.3    Stasinopoulos, S.J.4
  • 29
    • 0029054781 scopus 로고
    • Purification and characterization of three extracellular (1 → 3)-β-D-glucan glucanohydrolases from the filamentous fungus Acremonium persicinum
    • Pitson, S. M., Seviour, R. J., McDougall, B. M., Woodward, J. R., and Stone, B. A. Purification and characterization of three extracellular (1 → 3)-β-D-glucan glucanohydrolases from the filamentous fungus Acremonium persicinum. Biochem. J. 1995, 308, 733-741
    • (1995) Biochem. J. , vol.308 , pp. 733-741
    • Pitson, S.M.1    Seviour, R.J.2    McDougall, B.M.3    Woodward, J.R.4    Stone, B.A.5
  • 30
    • 0029844533 scopus 로고    scopus 로고
    • Purification and characterization of an extracellular (1 → 6)-β-glucanase from the filamentous fungus Acremonium persicinum
    • Pitson, S. M., Seviour, R. J., McDougall, B. M., Stone, B. A., and Sadek, M. Purification and characterization of an extracellular (1 → 6)-β-glucanase from the filamentous fungus Acremonium persicinum. Biochem. J. 1996, 316, 841-846
    • (1996) Biochem. J. , vol.316 , pp. 841-846
    • Pitson, S.M.1    Seviour, R.J.2    McDougall, B.M.3    Stone, B.A.4    Sadek, M.5
  • 31
    • 0027439791 scopus 로고
    • Purification and properties of three (1 → 3)-β-D-glucanase isoenzymes from young leaves of barley (Hordeum vulgare)
    • Hrmova, M. and Fincher, G. B. Purification and properties of three (1 → 3)-β-D-glucanase isoenzymes from young leaves of barley (Hordeum vulgare). Biochem. J. 1993, 289, 453-461
    • (1993) Biochem. J. , vol.289 , pp. 453-461
    • Hrmova, M.1    Fincher, G.B.2
  • 32
    • 0015830586 scopus 로고
    • The mechanism of enzymatic cellulose degradation. Characterization and enzymatic properties of a β-1,4-glucan cellobiohydrolase from Trichoderma viride
    • Berghem, L. E. R. and Petterson, L. G. The mechanism of enzymatic cellulose degradation. Characterization and enzymatic properties of a β-1,4-glucan cellobiohydrolase from Trichoderma viride. Eur. J. Biochem. 1973, 37, 21-30
    • (1973) Eur. J. Biochem. , vol.37 , pp. 21-30
    • Berghem, L.E.R.1    Petterson, L.G.2
  • 33
    • 0000674033 scopus 로고
    • A photometric adaptation of the somogyi method for the determination of glucose
    • Nelson, N. A photometric adaptation of the Somogyi method for the determination of glucose. J. Biol. Chem. 1944, 153, 375-380
    • (1944) J. Biol. Chem. , vol.153 , pp. 375-380
    • Nelson, N.1
  • 34
    • 33750423631 scopus 로고
    • Notes of sugar determination
    • Somogyi, M. Notes of sugar determination. J. Biol. Chem. 1952, 195, 19-23
    • (1952) J. Biol. Chem. , vol.195 , pp. 19-23
    • Somogyi, M.1
  • 35
    • 0343968421 scopus 로고
    • Elsevier-Biosoft, Cambridge
    • Williams, P. A. Enzpack. Elsevier-Biosoft, Cambridge, 1985
    • (1985) Enzpack
    • Williams, P.A.1
  • 37
    • 14744272350 scopus 로고
    • Cloning and amplification of the gene encoding an extracellular β-glucosidase from Trichoderma reesei: Evidence for improved rates of saccharification of cellulosic substrates
    • Barnett, C. C., Berka, R. M., and Fowler, T. Cloning and amplification of the gene encoding an extracellular β-glucosidase from Trichoderma reesei: Evidence for improved rates of saccharification of cellulosic substrates. Biotechnology 1991, 9, 562-567
    • (1991) Biotechnology , vol.9 , pp. 562-567
    • Barnett, C.C.1    Berka, R.M.2    Fowler, T.3
  • 38
    • 0030590353 scopus 로고    scopus 로고
    • Cloning and sequencing of the cDNA encoding β-glucosidase 1 from Aspergillus aculeatus
    • Kawaguchi, T., Enoki, T., Tsurumaki, S., Sumitani, J., Ueda, M., Ooi, T., and Arai, M. Cloning and sequencing of the cDNA encoding β-glucosidase 1 from Aspergillus aculeatus. Gene 1996, 173, 287-288
    • (1996) Gene , vol.173 , pp. 287-288
    • Kawaguchi, T.1    Enoki, T.2    Tsurumaki, S.3    Sumitani, J.4    Ueda, M.5    Ooi, T.6    Arai, M.7
  • 39
    • 0024254393 scopus 로고
    • Nucleotide sequences of Saccharomycopsis fibuligera genes for extracellular β-glucosidases as expressed in Saccharomyces cerevisiae
    • Machida, M., Ohtsuki, I., Fukui, S., and Yamashita, I. Nucleotide sequences of Saccharomycopsis fibuligera genes for extracellular β-glucosidases as expressed in Saccharomyces cerevisiae. Appl. Environ. Microbiol. 1988, 54, 3147-3155
    • (1988) Appl. Environ. Microbiol. , vol.54 , pp. 3147-3155
    • Machida, M.1    Ohtsuki, I.2    Fukui, S.3    Yamashita, I.4
  • 40
    • 0022423552 scopus 로고
    • Nucleotide sequence of Candida pelliculosa β-glucosidase gene
    • Kohchi, C. and Toh-e, A. Nucleotide sequence of Candida pelliculosa β-glucosidase gene. Nucl. Acid Res. 1985, 13, 6273-6282
    • (1985) Nucl. Acid Res. , vol.13 , pp. 6273-6282
    • Kohchi, C.1    Toh-E, A.2
  • 41
    • 11944256494 scopus 로고
    • Catalytic mechanisms of enzymic glycosyl transfer
    • Sinnott, M.L. Catalytic mechanisms of enzymic glycosyl transfer. Chem. Rev. 1990, 90, 1171-1202
    • (1990) Chem. Rev. , vol.90 , pp. 1171-1202
    • Sinnott, M.L.1
  • 42
    • 0017815423 scopus 로고
    • Studies on cellulases from a phytopathogenic fungus, Pyricularia oryzae, carvara. II. Purification and properties of a β-glucosidase
    • Hirayama, T., Horie, S., Nagayama, H., and Matsuda, K. J. Studies on cellulases from a phytopathogenic fungus, Pyricularia oryzae, Carvara. II. Purification and properties of a β-glucosidase. Biochemistry 1978, 84, 27-37
    • (1978) Biochemistry , vol.84 , pp. 27-37
    • Hirayama, T.1    Horie, S.2    Nagayama, H.3    Matsuda, K.J.4
  • 43
    • 0027332218 scopus 로고
    • Purification and characterisation of an extracellular β-glucosidase from the thermophylic fungus Sporotrichum thermophile and its influence on cellulase activity
    • Bhat, K. M., Gaikwad, J. S., and Maheshwari, R. Purification and characterisation of an extracellular β-glucosidase from the thermophylic fungus Sporotrichum thermophile and its influence on cellulase activity. J. Gen. Microbiol. 1993, 139, 2825-2832
    • (1993) J. Gen. Microbiol. , vol.139 , pp. 2825-2832
    • Bhat, K.M.1    Gaikwad, J.S.2    Maheshwari, R.3
  • 44
    • 0027565969 scopus 로고
    • Isolation and characterization of two forms of β-D-glucosidase from Aspergillus niger
    • Himmel, M. E., Adney, W. S., Fox, J. W., Mitchell, D. J., and Baker, J. O. Isolation and characterization of two forms of β-D-glucosidase from Aspergillus niger. Appl. Biochem. Biotechnol. 1993, 39/40, 213-225
    • (1993) Appl. Biochem. Biotechnol. , vol.39-40 , pp. 213-225
    • Himmel, M.E.1    Adney, W.S.2    Fox, J.W.3    Mitchell, D.J.4    Baker, J.O.5
  • 45
    • 0026055308 scopus 로고
    • A classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat, B. A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 1991, 280, 309-316
    • (1991) Biochem. J. , vol.280 , pp. 309-316
    • Henrissat, B.1
  • 46
    • 0027225980 scopus 로고
    • New families in the classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat, B. and Bairoch, A. New families in the classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 1993, 293, 781-788
    • (1993) Biochem. J. , vol.293 , pp. 781-788
    • Henrissat, B.1    Bairoch, A.2
  • 47
    • 85007860310 scopus 로고
    • High recovery purification and some properties of a β-glucosidase from Aspergillus niger
    • Unno, T., Ide, K., Yazaki, T., Tanaka, Y., Nakakuki, T., and Okada, G. High recovery purification and some properties of a β-glucosidase from Aspergillus niger. Biosci. Biotechnol. Biochem. 1993, 57, 2172-2173
    • (1993) Biosci. Biotechnol. Biochem. , vol.57 , pp. 2172-2173
    • Unno, T.1    Ide, K.2    Yazaki, T.3    Tanaka, Y.4    Nakakuki, T.5    Okada, G.6
  • 48
    • 0037814138 scopus 로고
    • β-D-glucosidases of Sclerotium rolfsii. Substrate specificity and mode of action
    • Sadana, J. C., Shewale, J. G., and Patil, R. V. β-D-Glucosidases of Sclerotium rolfsii. Substrate specificity and mode of action. Carbohydr. Res. 1983, 118, 205-214
    • (1983) Carbohydr. Res. , vol.118 , pp. 205-214
    • Sadana, J.C.1    Shewale, J.G.2    Patil, R.V.3
  • 49
    • 0343968420 scopus 로고
    • (1 → 2)-β-D-Glucan-hydrolysing enzymes in Cytophaga arvensicola: Partial purification and some properties of endo-(1 → 2)-β-D-glucanase and β-D-glucosidase specific for (1 → 2)-and (1 → 3)-linkages
    • Mendoza, N. S. and Amemura, A. (1 → 2)-β-D-Glucan-hydrolysing enzymes in Cytophaga arvensicola: Partial purification and some properties of endo-(1 → 2)-β-D-glucanase and β-D-glucosidase specific for (1 → 2)-and (1 → 3)-linkages. J. Ferment. Technol. 1983, 61, 473-481
    • (1983) J. Ferment. Technol. , vol.61 , pp. 473-481
    • Mendoza, N.S.1    Amemura, A.2
  • 50
    • 85004571031 scopus 로고
    • Cyclic (1 → 2)-β-D-glucan-hydrolysing enzymes from Acremonium sp. 15: Purification and some properties of endo-(1 → 2)-β-D-glucanase and β-D-glucosidase
    • Kitahata, S. and Edagawa, S. Cyclic (1 → 2)-β-D-glucan-hydrolysing enzymes from Acremonium sp. 15: Purification and some properties of endo-(1 → 2)-β-D-glucanase and β-D-glucosidase. Agric. Biol. Chem. 1987, 51, 2701-2708
    • (1987) Agric. Biol. Chem. , vol.51 , pp. 2701-2708
    • Kitahata, S.1    Edagawa, S.2
  • 51
    • 0028084345 scopus 로고
    • Isolation and properties of an extracellular β-glucosidase from the polycentric rumen fungus Orpinomyces sp. strain PC-2
    • Chen, H., Li, X., and Ljungdahl, L. G. Isolation and properties of an extracellular β-glucosidase from the polycentric rumen fungus Orpinomyces sp. strain PC-2. Appl. Environ. Microbiol. 1994, 60, 64-70
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 64-70
    • Chen, H.1    Li, X.2    Ljungdahl, L.G.3
  • 52
    • 0019494972 scopus 로고
    • Separation and some properties of two intracellular β-glucosidases of Sporotrichum (Chrysosporium) thermophile
    • Meyer, H.-P. and Canevascini, G. Separation and some properties of two intracellular β-glucosidases of Sporotrichum (Chrysosporium) thermophile. Appl. Environ. Microbiol. 1981, 41, 924-931
    • (1981) Appl. Environ. Microbiol. , vol.41 , pp. 924-931
    • Meyer, H.-P.1    Canevascini, G.2
  • 53
    • 0017882608 scopus 로고
    • Purification and characterisation of an extracellular β-glucosidase from Lenzites tabea
    • Herr, D., Baumer, F., and Dellweg. H. Purification and characterisation of an extracellular β-glucosidase from Lenzites tabea. Eur. J. Appl. Microbiol. Biotechnol. 1978, 5, 29-36
    • (1978) Eur. J. Appl. Microbiol. Biotechnol. , vol.5 , pp. 29-36
    • Herr, D.1    Baumer, F.2    Dellweg, H.3
  • 54
    • 0017816271 scopus 로고
    • Purification and properties of an induced β-glucosidase from Stachybotrys atra
    • Gussem, R. L. D., Aerts, G. M., Claeyssens, M., and Debruyne, C. K. Purification and properties of an induced β-glucosidase from Stachybotrys atra. Biochim. Biophys. Acta 1978, 525, 142-153
    • (1978) Biochim. Biophys. Acta , vol.525 , pp. 142-153
    • Gussem, R.L.D.1    Aerts, G.M.2    Claeyssens, M.3    Debruyne, C.K.4
  • 55
    • 0344783011 scopus 로고
    • Determination of essential residues in enzymes by chemical modification
    • Freedman, R. B. Determination of essential residues in enzymes by chemical modification. Tech. Protein Enzyme Biotechnol. 1978, B117, 229-235
    • (1978) Tech. Protein Enzyme Biotechnol. , vol.B117 , pp. 229-235
    • Freedman, R.B.1
  • 57
    • 0025754017 scopus 로고
    • Characteristics of fungal cellulases
    • Goyal, A., Ghosh, B., and Eveleigh, D. Characteristics of fungal cellulases. Biores. Technol. 1991, 36, 37-50
    • (1991) Biores. Technol. , vol.36 , pp. 37-50
    • Goyal, A.1    Ghosh, B.2    Eveleigh, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.