Results 161 to 170 of about 9,014 (216)
Forkhead Box S1 Inhibits the Progression of Hepatocellular Carcinoma [Retraction]. [PDF]
Onco Targets Thereuropepmc +1 more source
The small GTPases FoRab5, FoRab7, and FoRab8 regulate vesicle transport to modulate vegetative development and pathogenicity in Fusarium oxysporum f. sp. conglutinans. [PDF]
Front MicrobiolTan X, Chen L, Chen Y, Li Y, Lu L, Li E.
europepmc +1 more source
Luminal starch substrate "brake" on maltase-glucoamylase activity is located within the glucoamylase subunit. [PDF]
The Journal of nutrition, 2008 The detailed mechanistic aspects for the final starch digestion process leading to effective alpha-glucogenesis by the 2 mucosal alpha-glucosidases, human sucrase-isomaltase complex (SI) and human maltase-glucoamylase (MGAM), are poorly understood. This is due to the structural complexity and vast variety of starches and their intermediate digestion ...
Quezada-Calvillo, Roberto +9 more
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International Journal of Biological Macromolecules, 2017
The self-assembled glucoamylase metal-organic framework (glucoamylase-MOF) was synthesized by facile one-step method within 20min by simply mixing aqueous solution of 2-methylimidazole (160mM), glucoamylase (5mg/mL) and zinc acetate (40mM) at room temperature (28±2°C).
Shamraja S Nadar, Virendra K Rathod
exaly +3 more sources
The self-assembled glucoamylase metal-organic framework (glucoamylase-MOF) was synthesized by facile one-step method within 20min by simply mixing aqueous solution of 2-methylimidazole (160mM), glucoamylase (5mg/mL) and zinc acetate (40mM) at room temperature (28±2°C).
Shamraja S Nadar, Virendra K Rathod
exaly +3 more sources
Strain selection and medium optimization for glucoamylase production from industrial potato waste by Aspergillus niger [PDF]
Journal of the Science of Food and Agriculture, 2016 BACKGROUND: Glucoamylase is one of the most common enzymes used in the food industry to break down starch into its monomers. Glucoamylase production and its activity are highly dependent on medium composition.
Gulten Izmirlioglu, Ali Demirci
exaly +2 more sources
Identification and characterization of glucoamylase from the fungus Thermomyces lanuginosus [PDF]
Biochimica Et Biophysica Acta - Proteins and Proteomics, 2006 Udgivelsesdato: April 2006The glucoamylase from the thermophilic fungus Thermomyces lanuginosus has a molecular weight of 66 kDa and was characterized with isoelectric point, pH and temperature optimum of 3.8-4.0, 5.0 and 70 °C, respectively.
Thor S Thorsen +2 more
exaly +2 more sources
Biotechnology Advances, 2006
Fungi are employed to produce industrially important glucoamylases. Most glucoamylases are glycosylated. Glycosylation enhances the enzyme stability. Glucoamylases contain both starch binding and catalytic binding domains, the former being responsible for activity on raw (insoluble) starch.
Dariush, Norouzian +3 more
openaire +2 more sources
Fungi are employed to produce industrially important glucoamylases. Most glucoamylases are glycosylated. Glycosylation enhances the enzyme stability. Glucoamylases contain both starch binding and catalytic binding domains, the former being responsible for activity on raw (insoluble) starch.
Dariush, Norouzian +3 more
openaire +2 more sources
Glucoamylases: structural and biotechnological aspects
Applied Microbiology and Biotechnology, 2010Glucoamylases, 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.
Julia, Marín-Navarro, Julio, Polaina
openaire +2 more sources