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Volumn 118, Issue 2, 2005, Pages 167-176

Improving the amylolytic activity of Saccharomyces cerevisiae glucoamylase by the addition of a starch binding domain

Author keywords

Enzyme engineering; Ethanol; Family 15 glycosyl hydrolases; Fermentation; Hybrid protein

Indexed keywords

BIOTECHNOLOGY; FUNGI; GENES; HYDROLYSIS; STARCH; YEAST;

EID: 21244466379     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2005.03.019     Document Type: Article
Times cited : (35)

References (45)
  • 1
    • 1942476062 scopus 로고    scopus 로고
    • Structural analysis of glucoamylase encoded by the STA1 gene of Saccharomyces cerevisiae (var. diastaticus)
    • A.C. Adam, L. Latorre-García, and J. Polaina Structural analysis of glucoamylase encoded by the STA1 gene of Saccharomyces cerevisiae (var. diastaticus) Yeast 21 2004 379 388
    • (2004) Yeast , vol.21 , pp. 379-388
    • Adam, A.C.1    Latorre-García, L.2    Polaina, J.3
  • 2
    • 0026726797 scopus 로고
    • Crystal structure of glucoamylase from Aspergillus awamori var X100 to 2. 2-Å resolution
    • A. Aleshin, A. Golubev, L.M. Firsov, and R.B. Honzatko Crystal structure of glucoamylase from Aspergillus awamori var X100 to 2. 2-Å resolution J. Biol. Chem. 267 1992 19291 19298
    • (1992) J. Biol. Chem. , vol.267 , pp. 19291-19298
    • Aleshin, A.1    Golubev, A.2    Firsov, L.M.3    Honzatko, R.B.4
  • 3
    • 0037436378 scopus 로고    scopus 로고
    • Crystal structure and evolution of a prokaryotic glucoamylase
    • A. Aleshin, P-H. Feng, R.B. Honzatko, and P.J. Reilly Crystal structure and evolution of a prokaryotic glucoamylase J. Mol. Biol. 327 2003 61 73
    • (2003) J. Mol. Biol. , vol.327 , pp. 61-73
    • Aleshin, A.1    Feng, P.-H.2    Honzatko, R.B.3    Reilly, P.J.4
  • 4
    • 0034666315 scopus 로고    scopus 로고
    • Increased thermal resistance and modification of the catalytic properties of a ß-glucosidase by random mutagenesis and in vitro recombination
    • M.J. Arrizubieta, and J. Polaina Increased thermal resistance and modification of the catalytic properties of a ß-glucosidase by random mutagenesis and in vitro recombination J. Biol. Chem. 275 2000 28843 28848
    • (2000) J. Biol. Chem. , vol.275 , pp. 28843-28848
    • Arrizubieta, M.J.1    Polaina, J.2
  • 6
    • 0032102057 scopus 로고    scopus 로고
    • Ethanol production and fermentation characteristics of recombinant Saccharomyces cerevisiae strains grown on starch
    • G. Birol, I. Onsan, B. Kidar, and S.G. Oliver 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, I.2    Kidar, B.3    Oliver, S.G.4
  • 7
    • 0021430130 scopus 로고
    • Glucoamylases G1 and G2 from Aspergillus niger are synthesized from two different but closely related mRNAs
    • E. Boel, I. Hjort, B. Svensson, F. Norris, K.E. Norris, and N.P. Fiil 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
  • 9
    • 0000615498 scopus 로고
    • Plasmid vector carrying the replication origin of filamentous single-stranded phages
    • J.K. Setlow Plenum Press New York, USA
    • G. Cesareni, and A.H. Murray Plasmid vector carrying the replication origin of filamentous single-stranded phages J.K. Setlow Genetic Engineering vol. 9 1987 Plenum Press New York, USA 135 154
    • (1987) Genetic Engineering , vol.9 , pp. 135-154
    • Cesareni, G.1    Murray, A.H.2
  • 10
    • 0030729996 scopus 로고    scopus 로고
    • Glucoamylase structural, functional, and evolutionary relationships
    • P.M. Coutinho, and P.J. Reilly Glucoamylase structural, functional, and evolutionary relationships Proteins 29 1997 334 347
    • (1997) Proteins , vol.29 , pp. 334-347
    • Coutinho, P.M.1    Reilly, P.J.2
  • 11
    • 0014011862 scopus 로고
    • The induction and repression of nitrate reductase in the fungus Aspergillus nidulans
    • D.J. Cove The induction and repression of nitrate reductase in the fungus Aspergillus nidulans Biochim. Biophys. Acta 113 1966 51 56
    • (1966) Biochim. Biophys. Acta , vol.113 , pp. 51-56
    • Cove, D.J.1
  • 13
    • 0037438660 scopus 로고    scopus 로고
    • Cloning and characterization of a second α-amylase gene (LKA2) from Lipomyces kononenkoae IGC4052B and its expression in Saccharomyces cerevisiae
    • J.M. Eksteen, A.J. Steyn, P. van Rensburg, R.R. Cordero-Otero, and I.S. Pretorius Cloning and characterization of a second α-amylase gene (LKA2) from Lipomyces kononenkoae IGC4052B and its expression in Saccharomyces cerevisiae Yeast 15 2003 69 78
    • (2003) Yeast , vol.15 , pp. 69-78
    • Eksteen, J.M.1    Steyn, A.J.2    Van Rensburg, P.3    Cordero-Otero, R.R.4    Pretorius, I.S.5
  • 14
    • 0026704344 scopus 로고
    • Comparison of the Coomassie brilliant blue, bicinchoninic acid and Lowry quantitation assays, using non-glycosylated and glycosylated proteins
    • M. Fountoulakis, J.F. Juranville, and M. Manneberg Comparison of the Coomassie brilliant blue, bicinchoninic acid and Lowry quantitation assays, using non-glycosylated and glycosylated proteins J. Biochem. Biophys. Methods 24 1992 265 274
    • (1992) J. Biochem. Biophys. Methods , vol.24 , pp. 265-274
    • Fountoulakis, M.1    Juranville, J.F.2    Manneberg, M.3
  • 16
    • 0030733350 scopus 로고    scopus 로고
    • Structural and sequence-based classification of glycoside hydrolases
    • B. Henrissat, and G. Davies Structural and sequence-based classification of glycoside hydrolases Curr. Opin. Struct. Biol. 7 1997 637 644
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 637-644
    • Henrissat, B.1    Davies, G.2
  • 17
    • 0042162837 scopus 로고    scopus 로고
    • Cloning and characterisation of a glucoamylase gene (GlaM) from the dimorphic zygomycete Mucor circinelloides
    • J. Houghton-Larsen, and P.A. Pedersen Cloning and characterisation of a glucoamylase gene (GlaM) from the dimorphic zygomycete Mucor circinelloides Appl. Microbiol. Biotechnol. 62 2003 210 217
    • (2003) Appl. Microbiol. Biotechnol. , vol.62 , pp. 210-217
    • Houghton-Larsen, J.1    Pedersen, P.A.2
  • 19
    • 0037356636 scopus 로고    scopus 로고
    • Microbial starch-binding domain as a tool for targeting proteins to granules during starch biosynthesis
    • Q. Ji, J.P. Vincken, L.C. Suurs, and R.G. Visser Microbial starch-binding domain as a tool for targeting proteins to granules during starch biosynthesis Plant. Mol. Biol. 51 2003 789 801
    • (2003) Plant. Mol. Biol. , vol.51 , pp. 789-801
    • Ji, Q.1    Vincken, J.P.2    Suurs, L.C.3    Visser, R.G.4
  • 20
    • 0023993036 scopus 로고
    • High-efficiency, one-step starch utilization by transformed Saccharomyces cells which secrete both yeast glucoamylase and mouse alpha-amylase
    • K. Kim, C.S. Park, and J.R. Mattoon High-efficiency, one-step starch utilization by transformed Saccharomyces cells which secrete both yeast glucoamylase and mouse alpha-amylase Appl. Environ. Microbiol. 54 1988 966 971
    • (1988) Appl. Environ. Microbiol. , vol.54 , pp. 966-971
    • Kim, K.1    Park, C.S.2    Mattoon, J.R.3
  • 21
    • 0023800786 scopus 로고
    • Purification and properties of an extracellular glucoamylase from a diastatic strain of Saccharomyces cerevisiae
    • M.J. Kleinman, A.E. Wilkinson, I.P. Wright, I.H. Evans, and E.A. Bevan Purification and properties of an extracellular glucoamylase from a diastatic strain of Saccharomyces cerevisiae Biochem. J. 249 1988 163 170
    • (1988) Biochem. J. , vol.249 , pp. 163-170
    • Kleinman, M.J.1    Wilkinson, A.E.2    Wright, I.P.3    Evans, I.H.4    Bevan, E.A.5
  • 23
    • 0029737510 scopus 로고    scopus 로고
    • Muc1, a mucin-like protein that is regulated by Mss10, is critical for pseudohyphal differentiation in yeast
    • M.G. Lambrechts, F.F. Bauer, J. Marmur, and I.S. Pretorius Muc1, a mucin-like protein that is regulated by Mss10, is critical for pseudohyphal differentiation in yeast Proc. Natl. Acad. Sci. U.S.A. 93 1996 8419 8424
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 8419-8424
    • Lambrechts, M.G.1    Bauer, F.F.2    Marmur, J.3    Pretorius, I.S.4
  • 24
    • 0035917427 scopus 로고    scopus 로고
    • Addition of substrate-binding domains increases substrate-binding capacity and specific activity of a chitinase from Trichoderma harzianum
    • M.C. Limón, E. Margolles-Clark, T. Benitez, and M. Penttila Addition of substrate-binding domains increases substrate-binding capacity and specific activity of a chitinase from Trichoderma harzianum FEMS Microbiol. Lett. 198 2001 57 63
    • (2001) FEMS Microbiol. Lett. , vol.198 , pp. 57-63
    • Limón, M.C.1    Margolles-Clark, E.2    Benitez, T.3    Penttila, M.4
  • 25
    • 0030451075 scopus 로고    scopus 로고
    • FLO11, a yeast gene related to the STA genes, encodes a novel cell surface flocculin
    • W-S. Lo, and A.M. Dranginis FLO11, a yeast gene related to the STA genes, encodes a novel cell surface flocculin J. Bacteriol. 178 1996 7144 7151
    • (1996) J. Bacteriol. , vol.178 , pp. 7144-7151
    • Lo, W.-S.1    Dranginis, A.M.2
  • 26
    • 0028865920 scopus 로고
    • Development of yeast strains for the efficient utilisation of starch: Evaluation of constructs that express α-amylase and glucoamylase separately or as bifunctional fusion proteins
    • L.M. de Moraes, S. Astolfi-Filho, and S.G. Oliver Development of yeast strains for the efficient utilisation of starch: evaluation of constructs that express α-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 Moraes, L.M.1    Astolfi-Filho, S.2    Oliver, S.G.3
  • 27
    • 0026041607 scopus 로고
    • Structural and functional similarities suggest that intestinal sucrase-isomaltase, human lysosomal alpha-glucosidase and Schwanniomyces occidentalis glucoamylase are derived from a common ancestral gene
    • H.Y. Naim, T. Niermann, U. Kleinhans, C.P. Hollenberg, and A.W. Strasser Structural and functional similarities suggest that intestinal sucrase-isomaltase, human lysosomal alpha-glucosidase and Schwanniomyces occidentalis glucoamylase are derived from a common ancestral gene FEBS Lett. 294 1991 109 112
    • (1991) FEBS Lett. , vol.294 , pp. 109-112
    • Naim, H.Y.1    Niermann, T.2    Kleinhans, U.3    Hollenberg, C.P.4    Strasser, A.W.5
  • 28
    • 0032579520 scopus 로고    scopus 로고
    • Human small intestinal maltase-glucoamylase cDNA cloning homology to sucrase-isomaltase
    • B.L. Nichols, J. Eldering, S. Avery, D. Hahn, A. Quaroni, and E. Sterchi Human small intestinal maltase-glucoamylase cDNA cloning homology to sucrase-isomaltase J. Biol. Chem. 273 1998 3076 3081
    • (1998) J. Biol. Chem. , vol.273 , pp. 3076-3081
    • Nichols, B.L.1    Eldering, J.2    Avery, S.3    Hahn, D.4    Quaroni, A.5    Sterchi, E.6
  • 29
    • 0037417990 scopus 로고    scopus 로고
    • The maltase-glucoamylase gene: Common ancestry to sucrase-isomaltase with complementary starch digestion activities
    • B.L. Nichols, S. Avery, P. Sen, D.M. Swallow, D. Hahn, and E. Sterchi The maltase-glucoamylase gene: common ancestry to sucrase-isomaltase with complementary starch digestion activities Proc. Natl. Acad. Sci. U.S.A. 100 2003 1432 1437
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 1432-1437
    • Nichols, B.L.1    Avery, S.2    Sen, P.3    Swallow, D.M.4    Hahn, D.5    Sterchi, E.6
  • 30
    • 0033916432 scopus 로고    scopus 로고
    • Introduction of raw starch-binding domain into Bacillus subtillis α-amylase by fusion with the starch-binding domain of Bacillus cyclomaltodextrin glucanotransferase
    • K. Ohdam, T. Kuriki, H. Takata, H. Kaneko, and S. Okada Introduction of raw starch-binding domain into Bacillus subtillis α-amylase by fusion with the starch-binding domain of Bacillus cyclomaltodextrin glucanotransferase Appl. Environ. Microbiol. 66 2000 3058 3064
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 3058-3064
    • Ohdam, K.1    Kuriki, T.2    Takata, H.3    Kaneko, H.4    Okada, S.5
  • 31
    • 0026637695 scopus 로고
    • Molecular cloning of a glucoamylase from a thermophilic Clostridium and kinetics of the cloned enzyme
    • H. Ohnishi, H. Kitamura, T. Minowa, H. Sakai, and T. Ohta Molecular cloning of a glucoamylase from a thermophilic Clostridium and kinetics of the cloned enzyme Eur. J. Biochem. 207 1992 413 418
    • (1992) Eur. J. Biochem. , vol.207 , pp. 413-418
    • Ohnishi, H.1    Kitamura, H.2    Minowa, T.3    Sakai, H.4    Ohta, T.5
  • 32
    • 0001945222 scopus 로고
    • STA10: A gene involved in the control of starch utilization by Saccharomyces
    • J. Polaina, and M.Y. Wiggs STA10: A gene involved in the control of starch utilization by Saccharomyces Curr. Genet. 7 1983 108 112
    • (1983) Curr. Genet. , vol.7 , pp. 108-112
    • Polaina, J.1    Wiggs, M.Y.2
  • 34
    • 0034736420 scopus 로고    scopus 로고
    • Lactose utilization by Saccharomyces cerevisiae strains expressing Kluyveromyces lactis LAC genes
    • M. Rubio-Texeira, M. Arévalo-Rodriguez, J.L. Lequeríca, and J. Polaina Lactose utilization by Saccharomyces cerevisiae strains expressing Kluyveromyces lactis LAC genes J. Biotechnol. 84 2000 97 106
    • (2000) J. Biotechnol. , vol.84 , pp. 97-106
    • Rubio-Texeira, M.1    Arévalo-Rodriguez, M.2    Lequeríca, J.L.3    Polaina, J.4
  • 37
    • 0036275447 scopus 로고    scopus 로고
    • Getting started with yeast
    • F. Sherman Getting started with yeast Methods Enzymol. 350 2002 3 41
    • (2002) Methods Enzymol. , vol.350 , pp. 3-41
    • Sherman, F.1
  • 38
    • 0031570348 scopus 로고    scopus 로고
    • Solution structure of the granular starch binding domain of Aspergillus niger glucoamylase bound to beta-cyclodextrin
    • K. Sorimachi, M.F. Le Gal-Coeffet, G. Williamson, D.B. Archer, and M.P. Williamson Solution structure of the granular starch binding domain of Aspergillus niger glucoamylase bound to beta-cyclodextrin Structure 5 1997 647 661
    • (1997) Structure , vol.5 , pp. 647-661
    • Sorimachi, K.1    Le Gal-Coeffet, M.F.2    Williamson, G.3    Archer, D.B.4    Williamson, M.P.5
  • 40
    • 0032823710 scopus 로고    scopus 로고
    • Identification and cloning of GCA1, a gene that encodes a cell surface glucoamylase from Candida albicans
    • J. Sturtevant, F. Dixon, E. Wadsworth, J.P. Latge, X.J. Zhao, and R. Calderone Identification and cloning of GCA1, a gene that encodes a cell surface glucoamylase from Candida albicans Med. Mycol. 37 1999 357 366
    • (1999) Med. Mycol. , vol.37 , pp. 357-366
    • Sturtevant, J.1    Dixon, F.2    Wadsworth, E.3    Latge, J.P.4    Zhao, X.J.5    Calderone, R.6
  • 41
    • 0021485787 scopus 로고
    • Optimizing hydrolysis of N-linked high-manose oligosaccharides by endo-β-N-acetylglucosaminidase H
    • R.B. Trimble, and F. Maley Optimizing hydrolysis of N-linked high-manose oligosaccharides by endo-β-N-acetylglucosaminidase H Anal. Biochem. 141 1984 515 522
    • (1984) Anal. Biochem. , vol.141 , pp. 515-522
    • Trimble, R.B.1    Maley, F.2
  • 42
    • 0008141184 scopus 로고
    • Mouse α-amylase synthesized by Saccharomyces cerevisiae is released into the culture medium
    • K.K. Thomsen Mouse α-amylase synthesized by Saccharomyces cerevisiae is released into the culture medium Carlsberg Res. Commun. 48 1983 545 555
    • (1983) Carlsberg Res. Commun. , vol.48 , pp. 545-555
    • Thomsen, K.K.1
  • 43
    • 0030698386 scopus 로고    scopus 로고
    • Corregulation of starch degradation and dimorphism in the yeast Saccharomyces cerevisiae
    • M.A. Vivier, M.G. Lambrechts, and I.S. Pretorius Corregulation of starch degradation and dimorphism in the yeast Saccharomyces cerevisiae Crit. Rev. Biochem. Mol. Biol. 32 1997 405 435
    • (1997) Crit. Rev. Biochem. Mol. Biol. , vol.32 , pp. 405-435
    • Vivier, M.A.1    Lambrechts, M.G.2    Pretorius, I.S.3
  • 44
    • 0035489760 scopus 로고    scopus 로고
    • Generation of metal-binding staphylococci through surface display of combinatorially engineered cellulose-binding domains
    • H. Wernereus, J. Lehtio, T. Teeri, P.A. Nygren, and S. Stahal Generation of metal-binding staphylococci through surface display of combinatorially engineered cellulose-binding domains Appl. Environ. Microbiol. 67 2001 4678 4684
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 4678-4684
    • Wernereus, H.1    Lehtio, J.2    Teeri, T.3    Nygren, P.A.4    Stahal, S.5
  • 45
    • 0023185280 scopus 로고
    • Gene fusion is a possible mechanism underlying the evolution of STA1
    • I. Yamashita, M. Nakamura, and S. Fukui Gene fusion is a possible mechanism underlying the evolution of STA1 J. Bacteriol. 169 1987 2142 2149
    • (1987) J. Bacteriol. , vol.169 , pp. 2142-2149
    • Yamashita, I.1    Nakamura, M.2    Fukui, S.3


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