Protein engineering of glucoamylase to improve industrial performance - A review

Starch/Staerke

Volumn 51, Issue 8-9, 1999, Pages 269-274

  Reilly, Peter J ^a  

^a Iowa State University of Science and Technology   (United States)

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EID: 0000120116     PISSN: 00389056     EISSN: None     Source Type: Journal    
DOI: 10.1002/(sici)1521-379x(199909)51:8/9<269::aid-star269>3.0.co;2-3     Document Type: Article

References (77)

1. B. Svensson, K. Larsen, I. Svendsen, and E, Boel: The complete amino acid sequence of the glycoprotein, glucoamylase GI, from Aspergillus niger. Carlsberg Res. Commun. 48 (1983), 529-544.
2. J. H. Nunberg, J. H. Meade, G. Cole, F. C. Lawyer, P. McCabe, V. Schweickart, R. Tal, V. P. Wittman, J. E. Flatgaard, and M. A. Innis: Molecular cloning and characterization of the glucoamylase gene of Aspergillus awamori. Mol. Cell. Biol. 4 (1984), 2306-2315.
3. I. Diagne, V. T. PechexOnov, S. A. Bulat, and L. M. Firsov: Gen-Bank Entry # U59303 (1996).
4. S. Hayashida, K. Kuroda, K. Ohta, S. Kuhara, K. Fukuda, and Y. Sakaki: Molecular cloning of the glucoamylase I gene of Aspergillus awamori var. kawachi for localization of raw-starch-affinity site. Agric. Biol. Chem. 54 (1989), 923-929.
5. Y. Hata, K. Kitamoto, K. Gomi, C. Kumagai, G, Tamura, and S. Hara: The glucoamylase cDNA from Aspergillus oryzae: Its cloning, nucleotide sequence, and expression in Saccharomyces cerevisiae. Agric. Biol. Chem. 55 (1991), 941-949.
6. Y. Hata, H. Ishida, E. Ichikawa, A. Kawato, K. Suginami, and S. Imayasu: Nucleotide sequence of an alternative glucoamylase-encoding gene (glaB) expressed in solid-state culture of Aspergillus oryzae. Gene 207 (1998), 127-134.
7. I. Shibuya, K. Gomi, Y. Iimura, K. Takahashi, G. Tamura, and S. Hara: Molecular cloning of the glucoamylase gene of Aspergillus shirousami and its expression in Aspergillus oryzae. Agric. Biol. Chem. 54 (1990), 1905-1914.
8. L. Ventura, L. González-Candelas, J. A. Pérez-González, and D. Ramón: Molecular cloning and transcriptional analysis of the Aspergillus terreus gla1 gene encoding a glucoamylase. Appl. Environ. Microbiol. 61 (1995), 399-402.
9. Y. Nagasaka, N. Muraki, A. Kimura, M. Suto, A. Yokota, and F. Tomita: Cloning of Corticium rolfsii glucoamylase cDNA and its expression in Saccharomyces cerevisiae. Appl. Microbiol. Biotechnol. 44 (1995), 451-458.
10. V. V. Joutsjoki, and T. K. Torkkeli: Glucoamylase P gene of Hormoconis resinae: Molecular cloning, sequencing and introduction in-to Trichoderma reesei. FEMS Microbiol. Lett. 99 (1992), 237-244.
11. A. M. Berka, M. W. Rey, S. A. Thompson, G. L. Gray, C. L. Carmona, and S. D. Power: GenBank Entry # M89475 (1993).
12. P. J. Stone, A. J. Makoff, J. H. Parish, and A. Radford: Cloning and sequence analysis of the glucoamylase gene of Neurospora crassa, Curr. Genet. 24 (1993), 205-211.
13. T. Ashikari, N. Nakamura, Y. Tanaka, N. Kiuchi, Y. Shibano, T. Tanaka, T, Amachi, and H. Yoshizumi: Rhizopus raw-starch-degrading glucoamylase: Its cloning and expression in yeast. Agric. Biol. Chein. 50 (1986), 957-964.
14. D. M. Bui, I. Kunze, S. Förster, T. Wartmann, C. Horstmann, R. Manteuffel, and G. Kunze: Cloning and expression of an Arxula adeninivorans glucoamylase gene in Saccharomyces cerevisiae. Appl. Microbiol. Biotechnol, 44 (1996), 610-619.
15. I. Yamashita, M. Nakamura, and S. Fukui: Gene fusion is a possible mechanism underlying the evolution of STA 1. J. Bacteriol. 169 (1987), 2142-2149.
16. I. Yamashita, K, Suzuki, and S. Fukui: Nucleotide sequence of the extracellular glucoamylase gene STA1 in the yeast Saccharomyces diastaticus. J. Bacteriol. 161 (1985), 567-573.
17. M. G. Lambrechts, I. S. Pretorius, P. Sollitti, and J. Marmur: Primary structure and regulation of a glucoamylase-encoding gene (STA2) in Saccharomyces diastaticus. Gene 100 (1991), 95-103.
18. T. Itoh, I. Ohtsuki, I. Yamashita, and S. Fukui: Nucleotide sequence of the glucoamylase gene GLU1 in the yeast Saccharomycopsis fibuligera. J. Bacteriol. 169 (1987), 4171-4176.
19. E. Hostinová, J. Balanová, and J. Gaŝperík: The nucleotide sequence of the glucoamylase gene GLA1 from Saccharomycopsis fibuligera KZ. FEMS Microb. Lett. 83 (1991), 103-108.
20. H. Ohnishi, H. Kitamura, T. Minowa, H. Sakai, and T. Ohta: Molecular cloning of a glucoamylase gene from a thermophilic Clostridium and kinetics of the cloned enzyme. Eur. J. Biochem. 207 (1992), 413-418.
21. A. Ducki, O. Grundmann, L. Konermann, F. Mayer, and M. Hoppert: Glucoamylase from Thermoanaerobacterium thermosaccharolyticum. GenBank Entry # AF071548 (1998).
22. C. J. Bult, O. White, G. J. Olsen et al.: Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii. Science 273 (1996), 1058-1073.
23. P. M. Coutinho, and B. Henrissat: CAZy: Carbohydrate-Active enZYmes. http://afmb.cnrs-mrs.fr/-pedro (1999).
24. 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.
25. E. M. S. Harris, A. E. Aleshin, L. M. Firsov, and R. B. Honzatko: Refined structure for the complex of l-deoxynojirimycin with glucoamylase from Aspergillus awamori var. X100 to 2.4-Å resolution. Biochemistry 32 (1993), 1618-1626.
26. A. E. Aleshin, C. Hoffman, L. M. Firsov, and R. B. Honzatko: Refined crystal structures of glucoamylase from Aspergillus awamori var. X100. J. Mol. Biol. 238 (1994), 575-591.
27. A. E. Aleshin, L. M. Firsov, and R. B. Honzatko: Refined structure for the complex of acarbose with glucoamylase from Aspergillus awamori var. X100 to 2.4-Å resolution. J. Biol. Chem. 269 (1994), 15631-15639.
28. B. Stoffer, A. E. Aleshin, L. M. Firsov, B. Svensson, and R. B. Honzatko: Refined structure of the complex of D-gluco-dihydroacarbose with glucoamylase from Aspergillus awamori var. X100 to 2.2 Å resolution. Dual conformations for extended inhibitors bound to the active site of glucoamylase. FEBS Lett. 358 (1995), 57-61.
29. J. Ševčik, A. Solovicová, E. Hostinová, J. Gašpeík, K. S. Wilson, and Z. Dauter: Structure of glucoamylase from Saccharomycopsis fibuligera at 1.7 Å resolution. Acta Crystallogr. D54 (1998), 854-866.
30. G. F. H. Kramer, A. P. Gunning, V. J. Morris, N. J. Belshaw, and C. Williamson: Scanning tunnelling microscopy of Aspergillus niger glucoamylase. J. Chem. Soc. Faraday Trans. 89 (1993), 2595-2602.
31. M. R. Sierks, C. Ford, P. J. Reilly, and B. Svensson: Catalytic mechanism of fungal glucoamylase as defined by mutagenesis of Asp176, Glu179, and Glu180 in the enzyme from Aspergillus awamori. Protein Eng. 3 (1990), 193-198.
32. P. M. Coutinho, and P. J. Reilly: Structure-function relationships in the catalytic and starch-binding domains of glucoamylase. Protein Eng. 7 (1994), 393-400.
33. P. M. Coutinho, and P. J. Reilly: Structural similarities in glucoamylases by hydrophobic cluster analysis. Protein Eng. 7 (1994), 749-760.
34. B. Henrissat, P. M. Coutinho, and P. J. Reilly: Reading-frame shift in Saccharomyces glucoamylases restores catalytic base, extends sequence and improves alignment with other glucoamylases. Protein Eng. 7 (1994), 1281-1282.
35. P. M. Coutinho, and P. J. Reilly: Glucoamylase structural, functional, and evolutionary relationships. Proteins: Struct. Funct. Genet. 29 (1997), 334-347.
36. M. M. Meagher, and P. J. Reilly: Kinetics of the hydrolysis of diand trisaccharides by Aspergillus niger glucoamylases I and II. Biotechnol, Bioeng. 34 (1989), 689-693.
37. Z. L. Nikolov, M. M. Meagher, and P. J. Reilly: Kinetics, equilibria, and modeling of the formation of oligosaccharides from D-glucose by Aspergillus niger glucoamylases I and II. Biotechnol. Bioeng. 34 (1989), 694-704.
38. M. R. Sierks, C. Ford, P. J. Reilly, and B. Svensson: Site-directed mutagenesis at the active site Trp120 of Aspergillus awamori glucoamylase. Protein Eng. 2 (1989), 621-625.
39. M. R. Sierks, C. Ford, P. J. Reilly, and B. Svensson: Functional roles and subsite locations of Leu 177, Trp178, and Asn182 of Aspergillus awamori glucoamylase determined by site-directed mutagenesis. Protein Eng. 6 (1993), 75-79.
40. U. Bakir, P. M. Coutinho, P. A. Sullivan, C. Ford, and P. J. Reilly: Cassette mutagenesis of Aspergillus awamori glucoamylase near its general acid residue to probe its catalytic and pH properties. Protein Eng. 6 (1993), 939-946.
41. R. Evans, C. Ford, M. R. Sierks, Z. Nikolov, and B. Svensson: Activity and thermal stability of genetically truncated forms of Aspergillus glucoamylase. Gene 91 (1990), 131-134.
42. C. B. Libby, C. A. G. Cornett, P. J. Reilly, and C. Ford: Effect of amino acid deletions in the O-glycosylated region of Aspergillus awamori glucoamylase. Protein Eng. 7 (1994), 1109-1114.
43. L. Chen, P. M. Coutinho, Z. Nikolov, and C. Ford; Deletion analysis of the starch binding domain of Aspergillus glucoamylase. Protein Eng. 8 (1995), 1049-1055.
44. L. Chen, C. Ford, and Z. Nikolov: Adsorption to starch of a βgalactosidase fusion protein containing the starch-binding region of Aspergillus glucoamylase. Gene 99 (1991), 121-126.
45. L. Chen, C. Ford, A. Kusnadi, and Z. L. Nikolov: Improved adsorption to starch of a β-galactosidase fusion protein containing the starch-binding domain from Aspergillus glucoamylase. Biotechnol. Prog. 7 (1991), 225-229.
46. C. F. Ford, I. Suominen, and C. E. Glatz:: Fusion tails for the recovery and purification of recombinant proteins. Protein Express. Purif. 2 (1991), 95-107.
47. I. Suominen, C. Ford, D. Stachon, H. Heimo, M. Niederauer, H. Nurmela, and C. Glatz; Enhanced recovery and purification of Aspergillus glucoamylase from Saccharomyces cerevisiae by addition of poly(aspartic acid) tails. Enzyme Microb. Technol. 15 (1993), 593-600.
48. A. R. Kusnadi, C. Ford, and Z. L. Nikolov; Production of a functional starch-binding domain of Aspergillus glucoamylase I in Escherichia coli. Gene 127 (1993), 193-197.
49. T.-Y Fang, and C. Ford: Protein engineering of Aspergillus awamori glucoamylase to increase its pH optimum. Protein Eng. 11 (1998), 383-388.
50. T.-Y. Fang, P. M. Coutinho, P. J. Reilly, and C. Ford: Mutations to alter Aspergillus awamori glucoamylase selectivity. I. Tyr48Phe49 → Trp, Tyr116 → Trp, Tyr175 → Phe, Arg241 → Lys, Ser411 → Ala and Ser411 → Gly. Protein Eng. 11 (1998), 119-126.
51. T.-Y. Fang, R. B. Honzatko, P. J. Reilly, and C Ford: Mutations to alter Aspergillus awamori glucoamylase selectivity. II. Mutations at positions 119 and 121. Protein Eng. 11 (1998), 127-133.
52. H. -L. Liu, P. M. Coutinho, C. Ford, and P. J. Reilly: Mutations to alter Aspergillus awamori glucoamylase selectivity. III. Asn20 → Cys/Ala27 → Cys/Ala27 → Pro. Ser30 → Pro, Lys 108 → Arg, Lys 108 → Met, Gly 137 → Ala, 311-314 Loop, Tyr312 → Trp and Ser436 → Pro. Protein Eng. 11 (1998), 389-398.
53. H.-L. Liu, C. Ford, and P. J. Reilly: Mutations to alter Aspergillus awamori glucoamylase selectivity. IV. Combinatiorts of Asn20 → Cys/Ala27 → Cys, Ser30 → Pro, Gly 137 → Ala, 311-314 Loop, Ser411 → Ala and Ser436 → Pro. Protein Eng. 12 (1999), 163-172.
54. H. M. Chen, U. Bakir, P. J. Reilly, and C. Ford: Increased thermostability of Asn182 → Ala mutant Aspergillus awamori glucoamylase. Biotechnol. Bioeng. 43 (1994), 101-105.
55. H.-M. Chen, C. Ford, and P. J. Reilly: Substitution of aparagine residues in Aspergillus awamori glucoamylase by site-directed mutagenesis to eliminate N-glycosylation and inactivation by deamidation. Biochem. J. 301 (1994), 275-281.
56. N. Flory, M. Gorman, P. M. Coutinho, C. Ford, and P. J. Reilly: Thermosensitive mutants of Aspergillus awamori glucoamylase by random mutagenesis: Inactivation kinetics and structural interpretation. Protein Eng. 7 (1994), 1005-1012.
57. H.-M. Chen, C. Ford, and P. J. Reilly: Identification and elimination by site-directed mutagenesis of thermolabile aspartyl bonds in Aspergillus awamori glucoamylase. Protein Eng. 8 (1995), 575-582.
58. H.-M. Chen, Y. Li, T. Panda, F. U. Buehler, C. Ford, and P. J. Reilly: Effect of replacing helical glycine residues with alanines on reversible and irreversible stability and production of Aspergillus awamori glucoamylase. Protein Eng. 9 (1996), 499-505.
59. Y. Li, P. J. Reilly, and C. Ford: Effect of introducing proline residues on the stability of Aspergillus awamori glucoamylase. Protein Eng. 10(1997), 1199-1204.
60. Y. Li, P. M. Coutinho, and C. Ford: Effect on thermostability and catalytic activity of introducing disulfide bonds into Aspergillus awamori glucoamylase. Protein Eng. 11 (1998), 661-667.
61. M. J. Allen, P. M. Coutinho, and C. F. Ford: Stabilization Aspergillus awamori glucoamylase by proline substitution and combining stabilizing mutations. Protein Eng. 11 (1998), 783-788.
62. P. M. Coutinho, M. K. Dowd, and P. J. Reilly: Automated docking of monosaccharide substrates and analogues and methyl α-acarviosinide in the glucoamylase active site. Proteins: Struct. Funct. Genet. 27 (1997), 235-248.
63. P.-M. Coutinho, M. K. Dowd, and P. J. Reilly: Automated docking of isomaltose analogues in the glucoamylase active site. Carbohydr. Res. 297 (1997), 309-324.
64. P. M. Coutinho, M. K. Dowd, and P. J. Reilly: Automated docking of glucosyl disaccharides in the glucoamylase active site. Proteins: Struct. Funct. Genet. 28 (1997), 162-173.
65. P. M. Coutinho, M. K. Dowd, and P. J. Reilly: Automated docking of α-(1,4)-and α-(1,6)-linked glucosyl trisaccharides in the glucoamylase active site. Ind. Eng. Chem. Res. 37 (1998), 2148-2157.
66. B. Svensson, and M. R. Sierks: Roles of aromatic side chains in the binding of substrates, inhibitors and cyclomalto-oligosaccharides to glucoamylase from Aspergillus niger probed by perturbation difference spectroscopy, chemical modification and mutagenesis. Carbohydr. Res. 227 (1992), 29-44.
67. M. R. Sierks, and B. Svensson: Functional roles of the invariant aspartic acid 55, tyrosine 306, and aspartic acid 309 in glucoamylase from Aspergillus niger studied by mutagenesis. Biochemistry 32 (1993), 1113-1117.
68. T. P. Frandsen, C. Dupont, J. Lehmberk, B. Stoffer, M. R. Sierks, R. B. Honzatko, and B. Svensson: Site-directed mutagenesis of the catalytic base glutamic acid 400 in glucoamylase from Aspergillus niger and of tyrosine 48 and glutamine 401, both hydrogen-bonded to the α-carboxylate group of glutamic acid 400. Biochemistry 33 (1994), 13808-13816.
69. T. P. Frandsen, T. Christensen, B. Stoffer, J. Lehmbeck, C. Dupont, R. B. Honzatko, and B. Svensson: Mutational analysis of the roles in catalysis and substrate recognition of arginines 54 and 305, aspartic acid 309, and tryptophan 317 located at subsites 1 and 2 in glucoamylase from Aspergillus niger. Biochemistry 34 (1995), 10162-10169.
70. M. R. Sierks, and B. Svensson: Catalytic mechanism of glucoamylase probed by mutagenesis in conjunction with hydrolysis of α-D-glucopyranosyl fluoride and maltooligodextrins. Biochemistry 35 (1996), 1865-1871.
71. M. R. Sierks, and B. Svensson: Protein engineering of the relative specificity of glucoamylase from Aspergillus awamori based on sequence similarities between starch-degrading enzymes. Protein Eng. 7(1994), 1479-1484.
72. H.-P. Fierobe, B. B. Stoffer T. P. Frandsen, and B. Svensson: Mutational modulation of substrate bond-type specificity and thermostability of glucoamylase from Aspergillus awamori by replacement with short homologue sequences and thiol/disulfide engineering. Biochemistry 35 (1996), 8696-8704.
73. B. B. Stoffer, C. Dupont, T. P. Frandsen, J. Lehmbeck, and B. Svensson: Glucoamylase mutants in the conserved active-site segment Trp170-Tyr175 located at a distance from the site of catalysis. Protein Eng. 10 (1997) 81-89.
74. T. P. Frandson, B. B. Stoffer, M. M. Palcic, S. Hof, and B. Svensson: Structure and energetics of the glucoamylase-isomaltose transition-state complex probed by using modeling and deoxygenated substrates coupled with site-directed mutagenesis. J. Mol. Biol. 263 (1996), 79-89.
75. D. S. Goodsell, and A. J. Olson: Automated docking of substrates to proteins by simulated annealing. Proteins: Struct. Funct. Genet. 8 (1990), 195-202.
76. D. S. Goodsell, H. Lauble, C. S. Stout, and A. J. Olson: Automated docking in crystallography: Analysis of the substrates of aconitase. Proteins: Struct. Funct. Genet. 17 (1993), 1-10.
77. D. S. Goodsell, G. M. Morris, and A. J. Olson: Docking of flexible ligands. Applications of AutoDock. J. Mol. Recognit. 9 (1996), 1-5.