EC Number   |
Application |
Reference |
|---|
    3.2.1.3 | analysis |
method for anchoring native acarbose to gold chip surfaces for surface plasmon resonance studies employing glucoamylase as analyte. The key method is the chemoselective and protecting group-free oxime functionalization of the pseudo-tetrasaccharide-based inhibitor acarbose. At pH 7.0 the association and dissociation rate constants for the acarbose-glucoamylase interaction are 10000 per M and s and 103 per s, respectively, and the conformational change to a tight enzyme-inhibitor complex affects the dissociation rate constant by a factor of 100 per s. The acarbose-presenting surface plason resonance surfaces can be used as a glucoamylase sensor that allows rapid, label-free affinity screening of small carbohydrate-based inhibitors in solution |
729537 |
| 3.2.1.3 | biofuel production |
the sake yeast strains constructed in this study are expected to produce bioethanol from starchy materials such as corn. Furthermore, to improve the efficiency of hydrolysis, a combination of sake yeast and various enzymes that cleave alpha-glucoside bonds shall be used |
691371 |
| 3.2.1.3 | biofuel production |
the secreted glucoamylase from Paenibacillus amylolyticus strain NEO03 possesses properties suitable for saccharification processes such as biofuel production |
-, 750990 |
| 3.2.1.3 | biotechnology |
enzyme immobilization on polyacrylamide gel results in an enzyme with increases thermostability for use in biocatalysis |
682713 |
| 3.2.1.3 | biotechnology |
immobilization of the enzyme on alginate beads for large-scale hydrolysis of starch in a fluidized bed of enzyme-alginate particles, method development, comparison to packed and batch mode, overview |
655380 |
| 3.2.1.3 | biotechnology |
improvement of the yeast enzyme for starch degradation in biotechnological applications by introduction of the starch binding domain from the glucoamylase of Aspergillus niger, chimeric enzyme in Saccharomyces cerevisiae strain Y428, overview |
665781 |
| 3.2.1.3 | biotechnology |
the enzyme from commercial preparation is immobilized by sorption on a carbon support Sibunit, starch and dextrin hydrolysis kinetic parameters of glucoamylase, including the rate constant of thermal inactivation, show that immobilization of the enzyme results in a 1000fold increase in enzyme stability in comparison to the dissolved enzyme, presence of the dextrin substrate has a stabilizing effect, increase in dextrin concentration to 53% increases the thermostability of the immobilized enzyme, the immobilized-enzyme biocatalyst for starch saccharification has a high operational stability, half-inactivation time at 60°C exceeds 30 days |
677647 |
| 3.2.1.3 | biotechnology |
the enzyme immobilized on foamed glass covered with the catalytic filament carbon layer is highly active and stable, the effect of the carbon layer synthesized on the surface of aluminum oxide on the properties of biocatalysts shows that the glucoamylase adsorbed on the carbon-containing mesoporous ny-aluminum oxide exhibits a greater activity than the glucoamylase adsorbed on the macroporous alpha-aluminum oxide, kinetics, overview |
677641 |
| 3.2.1.3 | biotechnology |
the enzyme is potentially useful in improvement of industrial starch processing by eliminating the need to adjust both pH and temperature |
663696 |
| 3.2.1.3 | biotechnology |
the enzyme might be useful in biotechnological processes |
665887 |
