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Volumn 1764, Issue 4, 2006, Pages 671-676

Identification and characterization of glucoamylase from the fungus Thermomyces lanuginosus

Author keywords

Cloning; Enzyme; Glucoamylase; Thermomyces lanuginosus; Thermostability

Indexed keywords

COMPLEMENTARY DNA; FUNGAL DNA; GLUCAN 1,4 ALPHA GLUCOSIDASE;

EID: 33646097700     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2006.01.009     Document Type: Article
Times cited : (49)

References (34)
  • 1
    • 0002339053 scopus 로고
    • The Amylase Research Society of Japan
    • Pergamon Press, Oxford, United Kingdom
    • The Amylase Research Society of Japan. Handbook of Amylases and Related Enzymes (1988), Pergamon Press, Oxford, United Kingdom
    • (1988) Handbook of Amylases and Related Enzymes
  • 2
    • 0024715519 scopus 로고
    • Kinetics, equilibria, and modeling of the formation of oligosaccharides from d-glucose with Aspergillus niger glucoamylases I and II
    • Nikolov Z.L., Meagher M.M., and Reilly P.J. Kinetics, equilibria, and modeling of the formation of oligosaccharides from d-glucose with Aspergillus niger glucoamylases I and II. Biotechnol. Bioeng. 34 (1989) 694-704
    • (1989) Biotechnol. Bioeng. , vol.34 , pp. 694-704
    • Nikolov, Z.L.1    Meagher, M.M.2    Reilly, P.J.3
  • 3
    • 0024715518 scopus 로고
    • Subsite mapping of Aspergillus niger glucoamylases I and II with malto- and isomaltoseoligosaccharides
    • Meagher M.M., Nikolov Z.L., and Reilly P.J. Subsite mapping of Aspergillus niger glucoamylases I and II with malto- and isomaltoseoligosaccharides. Biotechnol. Bioeng. 34 (1989) 681-688
    • (1989) Biotechnol. Bioeng. , vol.34 , pp. 681-688
    • Meagher, M.M.1    Nikolov, Z.L.2    Reilly, P.J.3
  • 4
    • 84989071169 scopus 로고
    • Glucoamylase research: an overview
    • Pandey A. Glucoamylase research: an overview. Starch 47 (1995) 439-445
    • (1995) Starch , vol.47 , pp. 439-445
    • Pandey, A.1
  • 6
    • 0030729996 scopus 로고    scopus 로고
    • Glucoamylase structural, functional, and evolutionary relationships
    • Coutinho P.M., and Reilly P.J. Glucoamylase structural, functional, and evolutionary relationships. Proteins Struct. Funct. Genet. 29 (1997) 334-347
    • (1997) Proteins Struct. Funct. Genet. , vol.29 , pp. 334-347
    • Coutinho, P.M.1    Reilly, P.J.2
  • 7
    • 0021430130 scopus 로고
    • Glucoamylases G1 and G2 from Aspergillus niger are synthesized from two different but closely related mRNAs
    • Boel E., Hjort I., Svensson B., Norris F., Norris K.E., and Fiil N.P. Glucoamylases G1 and G2 from Aspergillus niger are synthesized from two different but closely related mRNAs. EMBO J. 3 (1984) 1097-1102
    • (1984) EMBO J. , vol.3 , pp. 1097-1102
    • Boel, E.1    Hjort, I.2    Svensson, B.3    Norris, F.4    Norris, K.E.5    Fiil, N.P.6
  • 8
    • 0023040629 scopus 로고
    • Characterization of glucoamylase G2 from Aspergillus niger
    • Svensson B., Larsen K., and Gunnarsson A. Characterization of glucoamylase G2 from Aspergillus niger. Eur. J. Biochem. 154 (1986) 497-502
    • (1986) Eur. J. Biochem. , vol.154 , pp. 497-502
    • Svensson, B.1    Larsen, K.2    Gunnarsson, A.3
  • 9
    • 0029361087 scopus 로고
    • Enzyme and microbial systems involved in starch processing
    • Nigam P., and Singh D. Enzyme and microbial systems involved in starch processing. Enzyme Microb. Technol. 17 (1995) 770-778
    • (1995) Enzyme Microb. Technol. , vol.17 , pp. 770-778
    • Nigam, P.1    Singh, D.2
  • 10
    • 0035098779 scopus 로고    scopus 로고
    • Hyperthermophilic enzymes: sources, uses and molecular mechanisms for thermostability
    • Vieille C., and Zeikus G.J. Hyperthermophilic enzymes: sources, uses and molecular mechanisms for thermostability. Microbiol. Mol. Biol. Rev. 65 (2001) 1-43
    • (2001) Microbiol. Mol. Biol. Rev. , vol.65 , pp. 1-43
    • Vieille, C.1    Zeikus, G.J.2
  • 11
    • 0001736752 scopus 로고
    • Purification of extracellular amylotic enzymes from the thermophilic fungus Thermomyces lanuginosus
    • Jensen B., Olsen J., and Allermann K. Purification of extracellular amylotic enzymes from the thermophilic fungus Thermomyces lanuginosus. Can. J. Microbiol. 34 (1988) 218-222
    • (1988) Can. J. Microbiol. , vol.34 , pp. 218-222
    • Jensen, B.1    Olsen, J.2    Allermann, K.3
  • 12
    • 85180973336 scopus 로고
    • A thermostable glucoamylase from the thermophilic fungus Thermomyces lanuginosus
    • Rao V.B., Maheshwari R., Sastry N.V.S., and Rao P.V.S. A thermostable glucoamylase from the thermophilic fungus Thermomyces lanuginosus. Curr. Sci. 48 (1979) 113-115
    • (1979) Curr. Sci. , vol.48 , pp. 113-115
    • Rao, V.B.1    Maheshwari, R.2    Sastry, N.V.S.3    Rao, P.V.S.4
  • 13
    • 0001051874 scopus 로고    scopus 로고
    • Amylases of the thermophilic fungus Thermomyces lanuginosus: their purification, properties, action on starch and response to heat
    • Mishra R.S., and Maheshwari R. Amylases of the thermophilic fungus Thermomyces lanuginosus: their purification, properties, action on starch and response to heat. J. Biosci. 21 (1996) 653-672
    • (1996) J. Biosci. , vol.21 , pp. 653-672
    • Mishra, R.S.1    Maheshwari, R.2
  • 14
    • 0025981348 scopus 로고
    • Growth and glucoamylase production by the thermophilic fungus Thermomyces lanuginosus in a synthetic medium
    • Haasum I., Eriksen S.H., Jensen B., and Olsen J. Growth and glucoamylase production by the thermophilic fungus Thermomyces lanuginosus in a synthetic medium. Appl. Microbiol. Biotechnol. 34 (1991) 656-660
    • (1991) Appl. Microbiol. Biotechnol. , vol.34 , pp. 656-660
    • Haasum, I.1    Eriksen, S.H.2    Jensen, B.3    Olsen, J.4
  • 15
    • 0031864133 scopus 로고    scopus 로고
    • Purification and characterization of extracellular glucoamylase from the thermophilic Thermomyces lanuginosus
    • Li D.-C., Yang Y.-J., Peng Y.-L., and Shen C.-Y. Purification and characterization of extracellular glucoamylase from the thermophilic Thermomyces lanuginosus. Mycol. Res. 102 (1998) 568-572
    • (1998) Mycol. Res. , vol.102 , pp. 568-572
    • Li, D.-C.1    Yang, Y.-J.2    Peng, Y.-L.3    Shen, C.-Y.4
  • 16
    • 0037008421 scopus 로고    scopus 로고
    • Purification and characterisation of amylolytic enzymes from thermophilic fungus Thermomyces lanuginosus strain ATCC 34626
    • Nguyen Q.D., Rezessy-Szabo J.M., Claeyssens M., Stals I., and Hoschke A. Purification and characterisation of amylolytic enzymes from thermophilic fungus Thermomyces lanuginosus strain ATCC 34626. Enzyme Microb. Technol. 31 (2002) 345-352
    • (2002) Enzyme Microb. Technol. , vol.31 , pp. 345-352
    • Nguyen, Q.D.1    Rezessy-Szabo, J.M.2    Claeyssens, M.3    Stals, I.4    Hoschke, A.5
  • 18
    • 0019482653 scopus 로고
    • Purification and characterization of a thermostable glucoamylase from the thermophilic fungus Thermomyces lanuginosus
    • Rao V.B., Sastri N.V.S., and Rao P.V.S. Purification and characterization of a thermostable glucoamylase from the thermophilic fungus Thermomyces lanuginosus. Biochem. J. 193 (1981) 379-387
    • (1981) Biochem. J. , vol.193 , pp. 379-387
    • Rao, V.B.1    Sastri, N.V.S.2    Rao, P.V.S.3
  • 19
    • 0000102131 scopus 로고
    • Some properties of a glucoamylase produced by the thermophilic fungus Humicola lanuginose
    • Taylor P.M., Napier E.J., and Fleming I.D. Some properties of a glucoamylase produced by the thermophilic fungus Humicola lanuginose. Carbohydr. Res. 61 (1978) 301-308
    • (1978) Carbohydr. Res. , vol.61 , pp. 301-308
    • Taylor, P.M.1    Napier, E.J.2    Fleming, I.D.3
  • 20
    • 0000966280 scopus 로고
    • Distribution of lysine pathways among fungi: evolutionary implications
    • Vogel H.J. Distribution of lysine pathways among fungi: evolutionary implications. Am. Nat. 903 (1964) 435-446
    • (1964) Am. Nat. , vol.903 , pp. 435-446
    • Vogel, H.J.1
  • 21
    • 0035145071 scopus 로고    scopus 로고
    • Calreticulin is an interleukin-3-sensitive calcium-binding protein in human basophil leukocytes
    • Lyngholm J.M., Nielsen H.V., Holm M., Schiotz P.O., and Johnsen A.H. Calreticulin is an interleukin-3-sensitive calcium-binding protein in human basophil leukocytes. Allergy 56 (2001) 21-28
    • (2001) Allergy , vol.56 , pp. 21-28
    • Lyngholm, J.M.1    Nielsen, H.V.2    Holm, M.3    Schiotz, P.O.4    Johnsen, A.H.5
  • 23
    • 33646083874 scopus 로고    scopus 로고
    • Perrin D.D., Dempsey B., 1974. Buffers for pH and metal ion control. Boyd Dempsey science paperbacks.
  • 25
    • 0031105124 scopus 로고    scopus 로고
    • Overexpression and characterization of Aspergillus awamori wild-type and mutant glucoamylase secreted by the methylotrophic yeast Pichia pastoris: comparison with wild-type recombinant glucoamylase produced using Saccharomyces cerevisiae and Aspergillus niger as hosts
    • Fierobe H.P., Mirgorodskaya E., Frandsen T.P., Roepstorff P., and Svensson B. Overexpression and characterization of Aspergillus awamori wild-type and mutant glucoamylase secreted by the methylotrophic yeast Pichia pastoris: comparison with wild-type recombinant glucoamylase produced using Saccharomyces cerevisiae and Aspergillus niger as hosts. Protein Expr. Purif. 9 (1997) 159-170
    • (1997) Protein Expr. Purif. , vol.9 , pp. 159-170
    • Fierobe, H.P.1    Mirgorodskaya, E.2    Frandsen, T.P.3    Roepstorff, P.4    Svensson, B.5
  • 26
    • 0032143360 scopus 로고    scopus 로고
    • Increased production of α-amylase from Thermomyces lanuginosus by the addition of Tween 80
    • Arnesen S., Eriksen S.H., Olsen J., and Jensen B. Increased production of α-amylase from Thermomyces lanuginosus by the addition of Tween 80. Enzyme Microb. Technol. 23 (1998) 249-252
    • (1998) Enzyme Microb. Technol. , vol.23 , pp. 249-252
    • Arnesen, S.1    Eriksen, S.H.2    Olsen, J.3    Jensen, B.4
  • 28
    • 0043073112 scopus 로고    scopus 로고
    • Prolyl peptidases: a serine protease subfamily with high potential for drug discovery
    • Rosenblum J.S., and Kozarich J.W. Prolyl peptidases: a serine protease subfamily with high potential for drug discovery. Curr. Opin. Chem. Biol. 7 (2003) 496-504
    • (2003) Curr. Opin. Chem. Biol. , vol.7 , pp. 496-504
    • Rosenblum, J.S.1    Kozarich, J.W.2
  • 29
    • 0036422274 scopus 로고    scopus 로고
    • Cloning, heterologous expression, and enzymatic characterization of a thermostable glucoamylase from Talaromyces emersonii
    • Nielsen B.R., Lehmbeck J., and Frandsen T.P. Cloning, heterologous expression, and enzymatic characterization of a thermostable glucoamylase from Talaromyces emersonii. Protein Expr. Purif. 26 (2002) 1-8
    • (2002) Protein Expr. Purif. , vol.26 , pp. 1-8
    • Nielsen, B.R.1    Lehmbeck, J.2    Frandsen, T.P.3
  • 31
    • 0032910571 scopus 로고    scopus 로고
    • The function of CreA, the carbon catabolite repressor of Aspergillus nidulans, is regulated at the transcriptional and post-transcriptional level
    • Strauss J., Horvath H.K., Abdallah B.M., Kindermann J., Mach R.L., and Kubicek C.P. The function of CreA, the carbon catabolite repressor of Aspergillus nidulans, is regulated at the transcriptional and post-transcriptional level. Mol. Microbiol. 32 (1999) 169-178
    • (1999) Mol. Microbiol. , vol.32 , pp. 169-178
    • Strauss, J.1    Horvath, H.K.2    Abdallah, B.M.3    Kindermann, J.4    Mach, R.L.5    Kubicek, C.P.6
  • 32
    • 0030794656 scopus 로고    scopus 로고
    • Genetic regulation of nitrogen metabolism in the fungi
    • Marzluf G.A. Genetic regulation of nitrogen metabolism in the fungi. Microbiol. Mol. Biol. Rev. 61 (1997) 17-32
    • (1997) Microbiol. Mol. Biol. Rev. , vol.61 , pp. 17-32
    • Marzluf, G.A.1
  • 34
    • 0028153702 scopus 로고
    • DNA sequence requirements for transcriptional initiator activity in mammalian cells
    • Javahery R., Khachi A., Lo K., Zenzie-Gregory B., and Smale S.T. DNA sequence requirements for transcriptional initiator activity in mammalian cells. Mol. Cell. Biol. 14 (1994) 116-127
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 116-127
    • Javahery, R.1    Khachi, A.2    Lo, K.3    Zenzie-Gregory, B.4    Smale, S.T.5


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