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1. Full Text Functional role of β domain in the Thermoanaerobacter tengcongensis glucoamylase
by Li, Zilong and Wei, Pingying and Cheng, Hairong and He, Peng and Wang, Qinhong and Jiang, Ning
Applied Microbiology and Biotechnology, ISSN 0175-7598, 3/2014, Volume 98, Issue 5, pp. 2091 - 2099
Thermoanaerobacter tengcongensis MB4 glucoamylase (TteGA) contains a catalytic domain (CD), which is structurally similar to eukaryotic GA, and a β domain (BD)... 
Life Sciences | Thermostability | Biotechnology | Prokaryotic glucoamylase | β domain | Microbiology | Microbial Genetics and Genomics | Thermoanaerobacter tengcongensis glucoamylase | Activity | beta domain | THERMOACTIVE GLUCOAMYLASE | STARCH-BINDING DOMAIN | THERMOSTABLE GLUCOAMYLASE | EVOLUTION | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | X-RAY | MOLECULAR-CLONING | ASPERGILLUS-NIGER GLUCOAMYLASE | SACCHAROMYCOPSIS-FIBULIGERA | STRUCTURE PREDICTION | CLOSTRIDIUM | Protein Structure, Tertiary | Recombinant Proteins - metabolism | Glucan 1,4-alpha-Glucosidase - genetics | Temperature | Enzyme Stability | Starch - metabolism | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Protein Folding | Hydrolysis | Escherichia coli - genetics | Glucan 1,4-alpha-Glucosidase - chemistry | Thermoanaerobacter - enzymology | Glucan 1,4-alpha-Glucosidase - metabolism | Index Medicus
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2. Full Text Small intestine mucosal α-glucosidase: A missing feature of in vitro starch digestibility
by Lin, Amy Hui-Mei and Lee, Byung-Hoo and Chang, Wei-Jen
Food Hydrocolloids, ISSN 0268-005X, 02/2016, Volume 53, pp. 163 - 171
The quality of starch digestion related to the rate and extent of glucose release is associated with high glycemia-related health issues such as diabetes and... 
Glucoamylase | Maltase–glucoamylase | Starch digestion | Starch digestibility | Mucosal α-glucosidase | Sucrase–isomaltase | Maltase-glucoamylase | Sucrase-isomaltase | ENZYME-RESISTANT STARCH | FOOD SCIENCE & TECHNOLOGY | ILEAL BRAKE | SUCRASE-ISOMALTASE COMPLEX | DIGESTION | Mucosal alpha-glucosidase | DIETARY FIBER | AMYLASE | RAW STARCH | CHEMISTRY, APPLIED | BRUSH-BORDER MEMBRANE | ASPERGILLUS-NIGER GLUCOAMYLASE
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3. Full Text Bienzyme Magnetic Nanobiocatalyst with Fe3+–Tannic Acid Film for One-Pot Starch Hydrolysis
by Bian, Hongjie and Sun, Baoting and Cui, Jiandong and Ren, Sizhu and Lin, Tao and Feng, Yuxiao and Jia, Shiru
Journal of Agricultural and Food Chemistry, ISSN 0021-8561, 08/2018, Volume 66, Issue 33, pp. 8753 - 8760
In this study, a novel co-immobilization biocatalyst for one-pot starch hydrolysis was prepared through shielding enzymes on the Fe3O4/SiO2 core–shell... 
α-amylase and glucoamylase | starch hydrolysis | co-immobilization | TA film | Fe | COVALENT ATTACHMENT | alpha-amylase and glucoamylase | IMMOBILIZED ENZYME | FOOD SCIENCE & TECHNOLOGY | ORGANOSILICA LAYER | CHEMICAL-MODIFICATION | CHITOSAN BEADS | GLUTARALDEHYDE | GLUCOAMYLASE | NANOPARTICLES | Fe3+ - TA film | AGRICULTURE, MULTIDISCIPLINARY | BIOCATALYST | CHEMISTRY, APPLIED | ALPHA-AMYLASE
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4. Full Text Purification and biochemical characterization of a novel mesophilic glucoamylase from Aspergillus tritici WZ99
by Xian, Liang and Feng, Jia-Xun
International Journal of Biological Macromolecules, ISSN 0141-8130, 02/2018, Volume 107, Issue Pt A, pp. 1122 - 1130
Glucoamylase, cleaving the nonreducing end of starch releasing glucose, is an important enzyme in starch processing. The optimal temperature for industrial... 
Bioethanol | Aspergillus tritici | Enzymatic characterization | Starch processing | Protein purification | Mesophilic glucoamylase | POLYMER SCIENCE | ACID | THERMOACTIVE GLUCOAMYLASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | IDENTIFICATION | THERMOSTABLE GLUCOAMYLASE | YEAST | CLONING | STARCH | ETHANOL | PENICILLIUM-OXALICUM | CHEMISTRY, APPLIED | ALPHA-AMYLASE
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5. Full Text Total Syntheses of Casuarine and Its 6‐O‐α‐Glucoside: Complementary Inhibition towards Glycoside Hydrolases of the GH31 and GH37 Families
by Cardona, Francesca and Parmeggiani, Camilla and Faggi, Enrico and Bonaccini, Claudia and Gratteri, Paola and Sim, Lyann and Gloster, Tracey M and Roberts, Shirley and Davies, Gideon J and Rose, David R and Goti, Andrea
Chemistry – A European Journal, ISSN 0947-6539, 02/2009, Volume 15, Issue 7, pp. 1627 - 1636
Selective glucosylation: Total synthesis of naturally occurring casuarine (1) and the first total synthesis of casuarine 6‐O‐α‐glucoside (2) were achieved... 
maltase glucoamylase | trehalase | natural products | total synthesis | enzyme structures | Enzyme structures | Maltase glucoamylase natural products | Trehalase | Total synthesis | ORGANIC-SYNTHESIS | ASYMMETRIC SYNTHESES | ENZYMATIC-SYNTHESIS | POLYHYDROXYLATED PYRROLIZIDINES | HYDROXY GROUP | CHEMISTRY, MULTIDISCIPLINARY | PHENYLDIMETHYLSILYL GROUP | SILAFUNCTIONAL COMPOUNDS | SUCRASE-ISOMALTASE | STEREOSELECTIVE-SYNTHESIS | INTESTINAL MALTASE-GLUCOAMYLASE | Pyrroles - metabolism | Catalytic Domain | Enzyme Inhibitors - metabolism | Alkaloids - chemical synthesis | Enzyme Inhibitors - chemical synthesis | Glucosides - metabolism | Trehalase - metabolism | Glucosides - chemical synthesis | Pyrroles - chemical synthesis | Hydrogen Bonding | Glucan 1,4-alpha-Glucosidase - metabolism | Alkaloids - metabolism | Glycoside Hydrolases - metabolism | Kinetics
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6. Full Text Selective purification of intestinal maltase complex by affinity chromatography employing an uncompetitive inhibitor as the ligand
by Kato, Eisuke and Tsuji, Hiroki and Kawabata, Jun
Tetrahedron, ISSN 0040-4020, 03/2015, Volume 71, Issue 9, pp. 1419 - 1424
Affinity chromatography of specific enzymes is limited by the presence of related enzymes and the limited selectivity of the affinity ligand. We synthesized... 
Uncompetitive inhibitor | Maltase-glucoamylase complex | Affinity chromatography | Intestinal glucosidase | Glucosidase inhibitor | 2-AMINORESORCINOL | CHEMISTRY, ORGANIC | IDENTIFICATION | GLUCOAMYLASE | Amylases | Chromatography
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7. Full Text α-Amylase, glucoamylase and isopullulanase determine molecular weight of pullulan produced by Aureobasidium melanogenum P16
by Liu, Nan-Nan and Liu, Guang-Lei and Chi, Zhe and Chi, Zhen-Ming and Chen, Tie-Jun and Jiang, Hong and Hu, Zhong
International Journal of Biological Macromolecules, ISSN 0141-8130, 10/2018, Volume 117, pp. 727 - 734
A high molecular weight (Mw) pullulan has many potential applications in various fields. α-Amylase, glucoamylase and pullulanase were thought to play an... 
Aureobasidium spp | Isopullulanase | α-Amylase, glucoamylase | High Mw pullulan | POLYMER SCIENCE | OLIGOSACCHARIDES | alpha-Amylase, glucoamylase | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | BIOSYNTHESIS | ENZYMES | OPTIMIZATION | CHEMISTRY, APPLIED | EXPRESSION | BINDING
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8. Full Text Pullulan-complexed α-amylase and glucosidase in alginate beads: Enhanced entrapment and stability
by Jadhav, Swati B and Singhal, Rekha S
Carbohydrate Polymers, ISSN 0144-8617, 05/2014, Volume 105, Issue 1, pp. 49 - 56
Enhanced entrapment of the enzymes, α-amylase and glucoamylase, was found in alginate beads on addition of pullulan in the enzyme mixture. Under optimized... 
Entrapment | Pullulan | Reusability | Stability | α-Amylase and glucoamylase | Starch hydrolysis | POLYMER SCIENCE | DEXTRAN | HYDROLYSIS | CHEMISTRY, ORGANIC | IMMOBILIZATION | GLUCOAMYLASE | GEL | CONJUGATION | TEMPERATURE | STARCH | OPTIMIZATION | LIPASE | alpha-Amylase and glucoamylase | CHEMISTRY, APPLIED | Drug Carriers - metabolism | Glucosidases - metabolism | Drug Stability | Glucuronic Acid - metabolism | alpha-Amylases - metabolism | Hexuronic Acids - chemistry | Alginates - metabolism | Drug Carriers - chemistry | Glucosidases - chemistry | alpha-Amylases - chemistry | Alginates - chemistry | Glucans - chemistry | Glucans - metabolism | Glucuronic Acid - chemistry | Enzyme Activation - physiology | Hexuronic Acids - metabolism
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9. Full Text Genome Mining for New α-Amylase and Glucoamylase Encoding Sequences and High Level Expression of a Glucoamylase from Talaromyces stipitatus for Potential Raw Starch Hydrolysis
by Xiao, Zhizhuang and Wu, Meiqun and Grosse, Stephan and Beauchemin, Manon and Lévesque, Michelle and Lau, Peter C. K
Applied Biochemistry and Biotechnology, ISSN 0273-2289, 1/2014, Volume 172, Issue 1, pp. 73 - 86
Mining fungal genomes for glucoamylase and α-amylase encoding sequences led to the selection of 23 candidates, two of which (designated TSgam-2 and NFamy-2)... 
Biochemistry, general | Biotechnology | Amylase | Triticale | Pichia pastoris | Biocatalysts | Cold starch hydrolysis | Chemistry | Fungal genomes | Glucoamylase | Biorefinery | Potato Starch | Genome mining | ASPERGILLUS-NIGER | BIOCHEMISTRY & MOLECULAR BIOLOGY | ETHANOL-PRODUCTION | SACCHAROMYCES-CEREVISIAE | SUBMERGED FERMENTATION | THERMOSTABLE GLUCOAMYLASE | DIGESTING GLUCOAMYLASE | YEAST-STRAIN | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | NEUTRAL GLUCOAMYLASE | THERMOMUCOR-INDICAE-SEUDATICAE | PICHIA-PASTORIS | Gene Expression Regulation, Fungal | Glucan 1,4-alpha-Glucosidase - genetics | Starch - metabolism | Data Mining | Talaromyces - enzymology | alpha-Amylases - metabolism | Glucan 1,4-alpha-Glucosidase - isolation & purification | alpha-Amylases - genetics | Hydrolysis | Talaromyces - genetics | Adsorption | Genome, Fungal - genetics | Escherichia coli - genetics | alpha-Amylases - isolation & purification | Pichia - genetics | Glucan 1,4-alpha-Glucosidase - metabolism | Kinetics | Sequence Analysis | Metals - pharmacology
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10. Full Text Posttranslational Processing and Function of Mucosal Maltases
by Amiri, Mahdi and Naim, Hassan Y
Journal of Pediatric Gastroenterology and Nutrition, ISSN 0277-2116, 06/2018, Volume 66 Suppl 3, pp. S18 - S23
ABSTRACTThe final step of carbohydrate digestion in the intestine is performed by 2 major α-glucosidases of the intestinal mucosa, sucrase-isomaltase (SI) and... 
PROTEIN | SUCRASE-ISOMALTASE DEFICIENCY | GLYCOSYLATION | IDENTIFICATION | GLUCOAMYLASE | sucrase-isomaltase | SUBSTRATE-SPECIFICITY | TRANSPORT | NUTRITION & DIETETICS | malabsorption | PEDIATRICS | ENZYME COMPLEX | MUTATIONS | GASTROENTEROLOGY & HEPATOLOGY | STARCH DIGESTION | maltase-glucoamylase | Glucosidases | Research | Intestine, Small | Health aspects
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11. Purification and characterization of thermostable glucoamylase from Rhizopus oligosporus SK5 mutant obtained through UV radiation and chemical mutagenesis
by Kareem, Sarafadeen and Akpan, Inyang and Popoola, Temitope and Lateef, Sanni
04/2014
Thermostable glucoamylase from Rhizopus oligosporus SK5 mutant was purified in a 3-step purification using Imarsil, activated charcoal and Sephadex-G-100 to... 
Enzyme purification | thermostability | Rhizopus oligosporus | glucoamylase
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12. Full Text The genomic signature of dog domestication reveals adaptation to a starch-rich diet
by Axelsson, Erik and Ratnakumar, Abhirami and Arendt, Maja-Louise and Maqbool, Khurram and Webster, Matthew T and Perloski, Michele and Liberg, Olof and Arnemo, Jon M and Hedhammar, Åke and Lindblad-Toh, Kerstin and Medicinska fakulteten and Science for Life Laboratory, SciLifeLab and Medicinska och farmaceutiska vetenskapsområdet and Institutionen för medicinsk biokemi och mikrobiologi and Uppsala universitet
Nature, ISSN 0028-0836, 03/2013, Volume 495, Issue 7441, pp. 360 - 364
The domestication of dogs. was an important episode in the development of human civilization. The precise timing and location of this event is debated(1-5) and... 
SPERM | TRANSPORTERS | GLUCOSE | MULTIDISCIPLINARY SCIENCES | SELECTION | MALTASE-GLUCOAMYLASE GENE | HISTORY | alpha-Glucosidases - genetics | Amylases - genetics | Animals | Animals, Domestic - genetics | Starch | Genome - genetics | Wolves - genetics | Glycogen Storage Disease Type II | Dogs - genetics | Mutation | Diet - veterinary | Genetic aspects | Research | Food and nutrition | High-carbohydrate diet | Health aspects | Dogs | Genetics | Standard deviation | Genomes | Glucose | Wolves | Naturvetenskap | Natural Sciences
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13. Full Text Identification of an essential regulator controlling the production of raw-starch-digesting glucoamylase in Penicillium oxalicum 06 Biological Sciences 0604 Genetics 06 Biological Sciences 0601 Biochemistry and Cell Biology
by Zhang, Mei-Yuan and Zhao, Shuai and Ning, Yuan-Ni and Fu, Li-Hao and Li, Cheng-Xi and Wang, Qi and You, Ran and Wang, Chen-Ying and Xu, Han-Nan and Luo, Xue-Mei and Feng, Jia-Xun
Biotechnology for Biofuels, ISSN 1754-6834, 01/2019, Volume 12, Issue 1
Raw-starch-digesting glucoamylase | Penicillium oxalicum | Amylase | Transcription regulation
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14. Full Text Selection of the best source of carbon for production of recombinants enzymes in liquid fermentation
by Jóse, Bárbara Garcia São and Pavezzi, Fabiana Carina and Frando, Cèlia Maria Landi and Gomes, Eleni and da Silva, Roberto
Journal of Biotechnology, ISSN 0168-1656, 2010, Volume 150, pp. 419 - 419
Glucoamylase | Enzyme | Starch | Production
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15. Full Text Identification of genetic alterations in the glucoamylase Aspergillus awamori gene
by Pavezzi, Fabiana Carina and Alves-Prado, Heloiza Ferreira and Ferreira, Henrique and Martins, Paula M.M and Gomes, Eleni and da Silva, Roberto
Journal of Biotechnology, ISSN 0168-1656, 2010, Volume 150, pp. 529 - 529
recombinant | hydrolyzes | thermostable | glucoamylase
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16. Full Text The carbohydrate‐binding module family 20 – diversity, structure, and function
by Christiansen, Camilla and Abou Hachem, Maher and Janeček, Štefan and Viksø‐Nielsen, Anders and Blennow, Andreas and Svensson, Birte
The FEBS Journal, ISSN 1742-464X, 09/2009, Volume 276, Issue 18, pp. 5006 - 5029
Starch‐active enzymes often possess starch‐binding domains (SBDs) mediating attachment to starch granules and other high molecular weight substrates. SBDs are... 
α‐glucan | starch‐binding domain | amylolytic enzymes | molecular recognition | glucan | starch metabolism | water dikinase | Glucan | Starch metabolism | Amylolytic enzymes | α-glucan | Starch-binding domain | Water dikinase | Molecular recognition | alpha-glucan | BACILLUS-CIRCULANS STRAIN-251 | PROGRESSIVE MYOCLONUS EPILEPSY | BARLEY ALPHA-AMYLASE | CEREUS VAR. MYCOIDES | BIOCHEMISTRY & MOLECULAR BIOLOGY | THERMOSTABLE CYCLODEXTRIN GLYCOSYLTRANSFERASE | THERMOANAEROBACTERIUM-THERMOSULFURIGENES EM1 | RAW-STARCH-BINDING | RHIZOPUS-ORYZAE GLUCOAMYLASE | starch-binding domain | RHODOTHERMUS-MARINUS XYLANASE | ASPERGILLUS-NIGER GLUCOAMYLASE | Catalytic Domain | Glycoside Hydrolases - physiology | Starch - metabolism | beta-Amylase - chemistry | Starch - chemistry | Thermodynamics | Glycogen - metabolism | alpha-Amylases - chemistry | Glycogen - chemistry | Glucosyltransferases - chemistry | Protein Engineering | Glycoside Hydrolases - chemistry | Ligands | Glucans - metabolism | Catalysis | Binding Sites | Arabidopsis thaliana | Glucose metabolism | Amylases | Phosphatases | Glycogen | Physiological aspects | Carbohydrate metabolism | Cyclodextrins | Universities and colleges | Carbohydrates | Enzymes | Biochemistry | Metabolism | Substrates
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