Access the full text.
Sign up today, get DeepDyve free for 14 days.
R. Uotsu-Tomita, T. Tonozuka, H. Sakai, Y. Sakano (2001)
Novel glucoamylase-type enzymes from Thermoactinomyces vulgaris and Methanococcus jannaschii whose genes are found in the flanking region of the α-amylase genesApplied Microbiology and Biotechnology, 56
Jung-Yu Tung, M. Chang, Wei-I Chou, Yen-Yi Liu, Y. Yeh, Fan-Yu Chang, Shu-Chuan Lin, Zhen-Liang Qiu, Yuh-Ju Sun (2008)
Crystal structures of the starch-binding domain from Rhizopus oryzae glucoamylase reveal a polysaccharide-binding path.The Biochemical journal, 416 1
Hsuan-Liang Liu, Wen-Chi Wang (2003)
Protein engineering to improve the thermostability of glucoamylase from Aspergillus awamori based on molecular dynamics simulations.Protein engineering, 16 1
Yue Wang, E. Fuchs, R. Silva, Allison McDaniel, J. Seibel, C. Ford (2006)
Improvement of Aspergillus niger Glucoamylase Thermostability by Directed EvolutionStarch-starke, 58
Pardeep Kumar, T. Satyanarayana (2009)
Microbial glucoamylases: characteristics and applicationsCritical Reviews in Biotechnology, 29
A. Adam, Lorena Latorre-García, J. Polaina (2004)
Structural analysis of glucoamylase encoded by the STA1 gene of Saccharomyces cerevisiae (var. diastaticus)Yeast, 21
Shu-Chuan Lin, Wei-Ting Liu, Shi-Hwei Liu, Wei-I Chou, Bor-Kai Hsiung, I. Lin, Chia-chin Sheu, Margaret Chang (2007)
Role of the linker region in the expression of Rhizopus oryzae glucoamylaseBMC Biochemistry, 8
Alexander Aleshin, Chad Hoffman, L. Firsov, R. Honzatko (1994)
Refined crystal structures of glucoamylase from Aspergillus awamori var. X100.Journal of molecular biology, 238 4
B. Svensson, K. Larsen, I. Svendsen, E. Boel (1983)
The complete amino acid sequence of the glycoprotein, glucoamylase G1, from Aspergillus nigerCarlsberg Research Communications, 48
R. Rodríguez-Sanoja, N. Oviedo, S. Sánchez (2005)
Microbial starch-binding domain.Current opinion in microbiology, 8 3
C. Christiansen, M. Hachem, Š. Janeček, A. Viksø‐Nielsen, A. Blennow, B. Svensson (2009)
The carbohydrate‐binding module family 20 – diversity, structure, and functionThe FEBS Journal, 276
B. Svensson, H. Jespersen, M. Sierks, E. Macgregor (1989)
Sequence homology between putative raw-starch binding domains from different starch-degrading enzymes.The Biochemical journal, 264 1
A. Aleshin, P. Feng, R. Honzatko, P. Reilly (2003)
Crystal structure and evolution of a prokaryotic glucoamylase.Journal of molecular biology, 327 1
Yuxing Li, Pedro Coutinho, C. Ford (1998)
Effect on thermostability and catalytic activity of introducing disulfide bonds into Aspergillus awamori glucoamylase.Protein engineering, 11 8
C. Rodgers, C. Blanford, S. Giddens, Pari Skamnioti, F. Armstrong, S. Gurr (2010)
Designer laccases: a vogue for high-potential fungal enzymes?Trends in biotechnology, 28 2
M. Machovič, Š. Janeček (2006)
Starch-binding domains in the post-genome eraCellular and Molecular Life Sciences CMLS, 63
Jozef Ševčík, A. Solovicová, E. Hostinová, J. Gašperík, Keith Wilson, Z. Dauter (1998)
Structure of glucoamylase from Saccharomycopsis fibuligera at 1.7 A resolution.Acta crystallographica. Section D, Biological crystallography, 54 Pt 5
H. Fierobe, B. Stoffer, T. Frandsen, Birte Svensson (1996)
Mutational modulation of substrate bond-type specificity and thermostability of glucoamylase from Aspergillus awamori by replacement with short homologue active site sequences and thiol/disulfide engineering.Biochemistry, 35 26
B. Cantarel, P. Coutinho, C. Rancurel, T. Bernard, V. Lombard, B. Henrissat (2008)
The Carbohydrate-Active EnZymes database (CAZy): an expert resource for GlycogenomicsNucleic Acids Research, 37
K. Sorimachi, K. Sorimachi, A. Jacks, A. Jacks, Marie‐Francoise Gal‐Coëffet, Marie‐Francoise Gal‐Coëffet, Gary Williamson, Gary Williamson, David Archer, David Archer, Michael Williamson, Michael Williamson (1996)
Solution structure of the granular starch binding domain of glucoamylase from Aspergillus niger by nuclear magnetic resonance spectroscopy.Journal of molecular biology, 259 5
Syun-ichi Yamakawa, Ryosuke Yamada, Tsutomu Tanaka, C. Ogino, A. Kondo (2010)
Repeated batch fermentation from raw starch using a maltose transporter and amylase expressing diploid yeast strainApplied Microbiology and Biotechnology, 87
K. Sorimachi, Marie‐Francoise Gal‐Coëffet, Gary Williamson, David Archer, Michael Williamson, Researc Article (1997)
Solution structure of the granular starch binding domain of Aspergillus niger glucoamylase bound to beta-cyclodextrin.Structure, 5 5
J. Polaina, A. Maccabe (2010)
Industrial Enzymes: Structure, Function and Applications
Yu-Nan Liu, Y. Lai, Wei-I Chou, M. Chang, P. Lyu (2007)
Solution structure of family 21 carbohydrate-binding module from Rhizopus oryzae glucoamylase.The Biochemical journal, 403 1
A. Boraston, D. Bolam, H. Gilbert, G. Davies (2004)
Carbohydrate-binding modules: fine-tuning polysaccharide recognition.The Biochemical journal, 382 Pt 3
H. Ohnishi, H. Kitamura, T. Minowa, H. Sakai, T. Ohta (1992)
Molecular cloning of a glucoamylase gene from a thermophilic Clostridium and kinetics of the cloned enzyme.European journal of biochemistry, 207 2
B. Svensson, K. Larsen, A. Gunnarsson (1986)
Characterization of a glucoamylase G2 from Aspergillus niger.European journal of biochemistry, 154 3
Yingying Zheng, Yanfen Xue, Yueling Zhang, Cheng Zhou, U. Schwaneberg, Yanhe Ma (2010)
Cloning, expression, and characterization of a thermostable glucoamylase from Thermoanaerobacter tengcongensis MB4Applied Microbiology and Biotechnology, 87
J. Ševčík, E. Hostinová, A. Solovicová, J. Gašperík, Z. Dauter, K. Wilson (2006)
Structure of the complex of a yeast glucoamylase with acarbose reveals the presence of a raw starch binding site on the catalytic domainThe FEBS Journal, 273
A. Voronovsky, Olha Rohulya, C. Abbas, A. Sibirny (2009)
Development of strains of the thermotolerant yeast Hansenula polymorpha capable of alcoholic fermentation of starch and xylan.Metabolic engineering, 11 4-5
E. Hostinová, J. Gašperík (2010)
Yeast glucoamylases: molecular-genetic and structural characterizationBiologia, 65
Ji-hye Kim, Ha-Ram Kim, M. Lim, H. Ko, Jong-eon Chin, Hwanghee-Blaise Lee, I. Kim, S. Bai (2010)
Construction of a direct starch-fermenting industrial strain of Saccharomyces cerevisiae producing glucoamylase, α-amylase and debranching enzymeBiotechnology Letters, 32
A. Aleshin, A. Golubev, L. Firsov, R. Honzatko (1994)
Crystal structure of glucoamylase from Aspergillus awamori var. X100 to 2.2-A resolution.The Journal of biological chemistry, 267 27
Synowiecki Jozef (2007)
The Use of Starch Processing Enzymes in the Food Industry
R. Fagerström (1994)
Purification and specificity of recombinant Hormoconis resinae glucoamylase P and endogenous glucoamylase from Trichoderma reesei.Enzyme and microbial technology, 16 1
Hsuan-Liang Liu, Yann Doleyres, Pedro Coutinho, C. Ford, Peter Reilly (2000)
Replacement and deletion mutations in the catalytic domain and belt region of Aspergillus awamori glucoamylase to enhance thermostability.Protein engineering, 13 9
Martin Allen, Pedro Coutinho, C. Ford (1998)
Stabilization of Aspergillus awamori glucoamylase by proline substitution and combining stabilizing mutations.Protein engineering, 11 9
C. Dock, M. Hess, G. Antranikian (2008)
A thermoactive glucoamylase with biotechnological relevance from the thermoacidophilic Euryarchaeon Thermoplasma acidophilumApplied Microbiology and Biotechnology, 78
M. Machovič, Š. Janeček (2006)
The evolution of putative starch‐binding domainsFEBS Letters, 580
Lorena Latorre-García, A. Adam, P. Manzanares, J. Polaina (2005)
Improving the amylolytic activity of Saccharomyces cerevisiae glucoamylase by the addition of a starch binding domain.Journal of biotechnology, 118 2
J. Marín-Navarro, Leontina Gurgu, S. Alamar, J. Polaina (2010)
Structural and functional analysis of hybrid enzymes generated by domain shuffling between Saccharomyces cerevisiae (var. diastaticus) Sta1 glucoamylase and Saccharomycopsis fibuligera Bgl1 β-glucosidaseApplied Microbiology and Biotechnology, 89
Ryosuke Yamada, Tsutomu Tanaka, C. Ogino, H. Fukuda, A. Kondo (2010)
Novel strategy for yeast construction using δ-integration and cell fusion to efficiently produce ethanol from raw starchApplied Microbiology and Biotechnology, 85
A. Jørgensen, J. Nøhr, J. Kastrup, M. Gajhede, B. Sigurskjold, J. Sauer, D. Svergun, B. Svensson, B. Vestergaard (2008)
Small Angle X-ray Studies Reveal That Aspergillus niger Glucoamylase Has a Defined Extended Conformation and Can Form Dimers in Solution*Journal of Biological Chemistry, 283
J. Sauer, B. Sigurskjold, U. Christensen, T. Frandsen, E. Mirgorodskaya, Matt Harrison, P. Roepstorff, B. Svensson (2000)
Glucoamylase: structure/function relationships, and protein engineering.Biochimica et biophysica acta, 1543 2
P. Coutinho, P. Reilly (1997)
Glucoamylase structural, functional, and evolutionary relationshipsProteins: Structure, 29
Mi‐Sun Kim, Jong-Tae Park, Young-Wan Kim, Heeseob Lee, Rose Nyawira, H. Shin, Cheon-Seok Park, S. Yoo, Yong-Ro Kim, T. Moon, Kwan‐Hwa Park (2004)
Properties of a Novel Thermostable Glucoamylase from the Hyperthermophilic Archaeon Sulfolobus solfataricus in Relation to Starch ProcessingApplied and Environmental Microbiology, 70
H. Leemhuis, R. Kelly, L. Dijkhuizen (2009)
Engineering of cyclodextrin glucanotransferases and the impact for biotechnological applicationsApplied Microbiology and Biotechnology, 85
J. McCarter, G. Withers (1994)
Mechanisms of enzymatic glycoside hydrolysis.Current opinion in structural biology, 4 6
R. Bott, M. Saldajeno, W. Cuevas, D. Ward, M. Scheffers, W. Aehle, S. Karkehabadi, M. Sandgren, H. Hansson (2008)
Three-dimensional structure of an intact glycoside hydrolase family 15 glucoamylase from Hypocrea jecorina.Biochemistry, 47 21
Glucoamylases, one of the main types of enzymes involved in starch hydrolysis, are exo-acting enzymes that release consecutive glucose units from the non-reducing ends of starch molecules. Glucoamylases are microbial enzymes, present in bacteria, archaea, and fungi but not in plants and animals. Structurally, they are classified in family 15 of glycoside hydrolases and characterised by the invariable presence of a catalytic domain with (α/α)6-fold, often bound to a non-catalytic domain of diverse origin and function. Fungal glucoamylases are biotechnologically very important as they are used industrially in large amounts and have been extensively studied during the past 30 years. Prokaryotic glucoamylases are of biotechnological relevance for being generally thermophilic enzymes, active at elevated temperatures.
Applied Microbiology and Biotechnology – Springer Journals
Published: Dec 9, 2010
Read and print from thousands of top scholarly journals.
Already have an account? Log in
Bookmark this article. You can see your Bookmarks on your DeepDyve Library.
To save an article, log in first, or sign up for a DeepDyve account if you don’t already have one.
Copy and paste the desired citation format or use the link below to download a file formatted for EndNote
Access the full text.
Sign up today, get DeepDyve free for 14 days.
All DeepDyve websites use cookies to improve your online experience. They were placed on your computer when you launched this website. You can change your cookie settings through your browser.