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A276C/S347C
101% of wild-type kcat
A276C/S347C/S298C
107% of wild-type kcat
C320A
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barely improved thermostability or altered activity
D71N
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increase in thermosability at 65 and 75°C
DELTA439-441
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increase in thermosability at 65 and 75°C
E389M
104% of wild-type kcat
G127A/P128A
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site-directed mutagenesis, the mutation decreases the enzyme thermostability compared to the wild-type protein
G137A
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site-directed mutagenesis, the mutant has a strong additive thermostabilizing effect
G139A
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site-directed mutagenesis, the mutant has a strong additive thermostabilizing effect
G183K
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slight increase in activity as compared with the wild-type enzyme towards maltose. The mutation broadens the optimal pH range for activity towards acidic as well as alkaline conditions. Selectivity of the mutant for alpha-1,4-linked disaccharides over alpha-1,6-linked disaccharides is enhanced 2.3fold to 3.5fold
G396A
90% of wild-type kcat
G396A/G407A
92% of wild-type kcat
G407A
96% of wild-type kcat
G447S
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increase in thermosability at 65 and 75°C
H391M
89% of wild-type kcat
I136L
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site-directed mutagenesis, the mutant has a strong additive thermostabilizing effect
P128A
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site-directed mutagenesis, the mutant destabilizes the enzyme
P128A/G139A/I136L
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site-directed mutagenesis, mutations G139A and I136L, located in the center of alpha-helix, completely compensate for the destabilization caused by substitution P128A
P307A/T310V/Y312M/N313G
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up to 15fold decreased turnover-number for alpha-1,4-linked substrates. Up to 9fold increase in Km-value for alpha-1,6-linked substrates
Q409P
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increase in thermosability at 65 and 75°C
S119Y
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slight increase in activity as compared with the wild-type enzyme towards maltose. Selectivity of the mutant for alpha-1,4-linked disaccharides over alpha-1,6-linked disaccharides is enhanced 2.3fold to 3.5fold
S184H
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slight increase in activity as compared with the wild-type enzyme towards maltose. The mutation broadens the optimal pH range for activity towards acidic as well as alkaline conditions. Selectivity of the mutant for alpha-1,4-linked disaccharides over alpha-1,6-linked disaccharides is enhanced 2.3fold to 3.5fold
S298C/L354C
104% of wild-type kcat
S386L
103% of wild-type kcat
S411A
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54-74% of the catalytic efficiency of the wild type enzyme. Increased pH-optimum by 0.8 units for both maltose and maltoheptaose hydrolysis while maintaining a high level of activity and catalytic efficiency. In hydrolysis of 28% DE 10 maltodextrin, the mutant enzyme has a pH optimum of 7 compared with 5.6 for wild-type enzyme, and has higher initial rates of glucose production than wild-type enzyme at all pH values tested above pH 6.6
S411C
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54-74% of the catalytic efficiency of the wild type enzyme
S411D
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6-12% of the catalytic efficiency of the wild type enzyme
S411G
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catalytic efficiency like that of wild type enzyme for isomaltose, maltose and maltoheptaose hydrolysis at pH 4.4
S411H
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6-12% of the catalytic efficiency of the wild type enzyme
S418L
103% of wild-type kcat
S54P/T314A/H415Y
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the mutant enzyme is more thermostable compared to the wild-type enzyme at 70°C. The mutation does not affect the protein secretion nor the production of the enzyme
T390L
101% of wild-type kcat
T416L
101% of wild-type kcat
V181T/N182Y/G183A
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2fold increased Km-value for alpha-1,4-linked substrates: For alpha-1,6-linked substrates a 2fold increase in Km and a 3fold decrease in turnover-number
V181T/N182Y/G183A/P307A/T310V/Y312M/A313G
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remarkably low Km-value for isomaltotriose through isomaltoheptaose and elevated turnover-number on isomaltose, resulting in an approximately 2fold improved catalytic effeciency
S54P/T314A/H415Y
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the mutant enzyme is more thermostable compared to the wild-type enzyme at 70°C. The mutation does not affect the protein secretion nor the production of the enzyme
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A246C
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site-directed mutagenesis, the mutant has a strong additive thermostabilizing effect
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G137A
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site-directed mutagenesis, the mutant has a strong additive thermostabilizing effect
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G139A
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site-directed mutagenesis, the mutant has a strong additive thermostabilizing effect
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P128A
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site-directed mutagenesis, the mutant destabilizes the enzyme
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D20C/A27C/S30P/G137A
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site-directed mutagenesis, the mutant, designated THS8, is highly thermotolerant with increased stability at 80°C compared to the wild-type enzyme
H391Y
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random mutagenesis, the mutant shows increased thermotolerance compared to the wild-type enzyme
R54L
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active site mutant. For inhibitor acarbose, a rapid binding event is apparently intersected by a slower secondary binding event. Mutant shows a dramatically higher Kd value for acarbose
T290A
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random mutagenesis, the mutant shows increased thermotolerance compared to the wild-type enzyme
T62A
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random mutagenesis, the mutant shows increased thermotolerance compared to the wild-type enzyme
W120F
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mutant of G1, 3% of wild-type kcat for maltose, 2% of kcat for maltotriose
W317F
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mutant of G1, 90% of wild-type kcat for maltose, 97% of kcat for maltotriose
W52F
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mutant of G2, almost no activity with maltose and maltotriose
Y175F
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mutation in subsite +3. Mutant displays only minor differences to wild-type in affinities to inhibitors acarbose and an acarbose conjugate
I339G
about 10% of wild-type specific activity
T47A
about 50% of wild-type specific activity
T47A/W48A
about 25% of wild-type specific activity
W48A
about 55% of wild-type specific activity
I339G
-
about 10% of wild-type specific activity
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T47A
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about 50% of wild-type specific activity
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T47A/W48A
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about 25% of wild-type specific activity
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W48A
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about 55% of wild-type specific activity
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W47A
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site-directed mutagenesis, the mutant shows altered kinetics and starch binding compared to the wild-type enzyme
Y32A
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site-directed mutagenesis, the mutant shows altered kinetics and starch binding compared to the wild-type enzyme
Y32A/Y47A
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site-directed mutagenesis, the mutant shows altered kinetics and starch binding compared to the wild-type enzyme
H447A
site-directed mutagenesis, structure analysis compared to the wild-type, crystal structure
H447A/D450A
site-directed mutagenesis, structure analysis compared to the wild-type, crystal structure
R15A
site-directed mutagenesis, structure analysis compared to the wild-type, crystal structure
T462A
site-directed mutagenesis, structure analysis compared to the wild-type, crystal structure
H447A
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site-directed mutagenesis, structure analysis compared to the wild-type, crystal structure
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H447A/D450A
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site-directed mutagenesis, structure analysis compared to the wild-type, crystal structure
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R15A
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site-directed mutagenesis, structure analysis compared to the wild-type, crystal structure
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T462A
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site-directed mutagenesis, structure analysis compared to the wild-type, crystal structure
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H447A
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site-directed mutagenesis, structure analysis compared to the wild-type, crystal structure
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H447A/D450A
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site-directed mutagenesis, structure analysis compared to the wild-type, crystal structure
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R15A
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site-directed mutagenesis, structure analysis compared to the wild-type, crystal structure
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T462A
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site-directed mutagenesis, structure analysis compared to the wild-type, crystal structure
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W622C
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site-directed mutagenesis, the mutant enzyme shows slightly altered pH optimum and 87% reduced activity compared to the wild-type enzyme
W622D
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site-directed mutagenesis, the mutant enzyme shows slightly altered pH optimum and 95% reduced activity compared to the wild-type enzyme
W622G
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site-directed mutagenesis, the mutant enzyme shows slightly altered pH optimum and 95.7% reduced activity compared to the wild-type enzyme
W622H
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site-directed mutagenesis, the mutant enzyme shows slightly altered pH optimum and 48% reduced activity compared to the wild-type enzyme
W622S
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site-directed mutagenesis, the mutant enzyme shows slightly altered pH optimum and 83% reduced activity compared to the wild-type enzyme
W622C
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site-directed mutagenesis, the mutant enzyme shows slightly altered pH optimum and 87% reduced activity compared to the wild-type enzyme
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W622D
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site-directed mutagenesis, the mutant enzyme shows slightly altered pH optimum and 95% reduced activity compared to the wild-type enzyme
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W622G
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site-directed mutagenesis, the mutant enzyme shows slightly altered pH optimum and 95.7% reduced activity compared to the wild-type enzyme
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W622H
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site-directed mutagenesis, the mutant enzyme shows slightly altered pH optimum and 48% reduced activity compared to the wild-type enzyme
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W622S
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site-directed mutagenesis, the mutant enzyme shows slightly altered pH optimum and 83% reduced activity compared to the wild-type enzyme
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A246C
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the T50-value is enhanced by 4°C to 73°C. Compared to wild-type enzyme, the mutant is twice as active at 66°C but half as active at 45°C
A246C
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site-directed mutagenesis, the mutant has a strong additive thermostabilizing effect
E400C
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cysteinesulfinic acid derivative of C320A/E400C-SO2H has a 700times higher turnover number towards maltose relative to C320A/E400C, while the Km-value is unchanged. Compared to wild-type enzyme, the C400-SO2H derivative has a turnover number of 150-190% and 85-320% on maltooliogosaccharides and isomaltooligosaccharides respectively, while Km-values are similar to that of wild-type for disaccharides and 3.5-5.5fold and 1.8-2.5fold higher for the longer maltooligosaccharides and isomaltooligosaccharides. The inhibition constant of cysteinesulfinic acid derivative of C320A/E400C-SO2H for acarbose increases more than 10000-fold
E400C
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further oxidation of Cys thiol group to sulfinic acid, up to 300% higher kcat and decreased Km compared to wild-type, depending on substrate
E180Q
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mutant of G1, 48% of wild-type kcat for maltose, 88% of kcat for maltotriose
E180Q
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active site mutant. For inhibitor acarbose, a rapid binding event is apparently intersected by a slower secondary binding event. Mutant shows a dramatically higher Kd value for acarbose
additional information
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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, method optimization, overview
additional information
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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
additional information
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molecular construction, molecular modeling and molecular dynamics of engineered enzyme with higher thermostability through optimized intrinsic interactions within alpha-helix D, overview
additional information
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molecular construction, molecular modeling and molecular dynamics of engineered enzyme with higher thermostability through optimized intrinsic interactions within alpha-helix D, overview
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additional information
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immobilization of the enzyme on polyaniline polymer results in improved catalytic performance with decreased temperature optimum, and increased thermal stability and catalytic efficiency with increased Vmax and reduced Km, overview
additional information
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improvement of enzyme for inductrial applications
additional information
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entrapment of amyloglucosidase into dipalmitoylphosphatidylcholine multilamellar vesicles and large unilamellar vesicles, vesicle formation, method optimization, enzyme activity is very stable during the first three batch runs, overview
additional information
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random mutagenesis and mutant screening by plate thermostability assay for increased thermotolerance at 65-80°C, overview
additional information
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engineered low-glycosylated variant of glucoamylase 1 with a short linker, low-glycosylated GA1 (dgGA). Low-glycosylated linker variant of GA1; GA1:L0 and dgGA:L0
additional information
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disulfide-deficient mutant of the starch-binding domain of glucoamylase
additional information
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improvement of enzyme for inductrial applications
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additional information
presence of the beta domain is essential for catalytic activity of the enzyme. The catalytic domain alone is not able to hydrolyze soluble starch while starch hydrolysis activity is restored in the catalytic domain in the presence of the beta domain. The catalytic domain displays lower thermostability compared with the intact wild-type and exhibits enhanced thermostability in the presence of the beta domain in vitro. Truncation of the wild-type enzyme or mutagenesis of the residues that participate in the interdomain interaction at its beta domain also lead to the reduced thermostability of the enzyme
additional information
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presence of the beta domain is essential for catalytic activity of the enzyme. The catalytic domain alone is not able to hydrolyze soluble starch while starch hydrolysis activity is restored in the catalytic domain in the presence of the beta domain. The catalytic domain displays lower thermostability compared with the intact wild-type and exhibits enhanced thermostability in the presence of the beta domain in vitro. Truncation of the wild-type enzyme or mutagenesis of the residues that participate in the interdomain interaction at its beta domain also lead to the reduced thermostability of the enzyme
additional information
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presence of the beta domain is essential for catalytic activity of the enzyme. The catalytic domain alone is not able to hydrolyze soluble starch while starch hydrolysis activity is restored in the catalytic domain in the presence of the beta domain. The catalytic domain displays lower thermostability compared with the intact wild-type and exhibits enhanced thermostability in the presence of the beta domain in vitro. Truncation of the wild-type enzyme or mutagenesis of the residues that participate in the interdomain interaction at its beta domain also lead to the reduced thermostability of the enzyme
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additional information
CauloGA gene product that is expressed in Escherichia coli is prone to forming inclusion bodies. Most of the gene product is expressed in a soluble and active form when it was expressed as a fusion protein with Staphylococcus Protein A
additional information
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CauloGA gene product that is expressed in Escherichia coli is prone to forming inclusion bodies. Most of the gene product is expressed in a soluble and active form when it was expressed as a fusion protein with Staphylococcus Protein A
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additional information
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purified glucoamylase is chemically modified by cross-linking with aniline hydrochloride in the presence of 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide for 1, 7, or 13 min, resulting in aniline-coupled glucoamylase-1/ACG-1, aniline-coupled glucoamylase-7/ACG-7, and 13 min aniline-coupled glucoamylase-13/ACG-13, the aniline coupling of GA has profound enhancing effects on temperature, pH optima, and pKas of active site residues, overview
additional information
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enzyme immobilization on polyacrylamide gel highly decreases the entropy and enthalpy of thermal enzyme deactivation
additional information
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co-expressed recombinant barley alpha-amylase 1 mutant and recombinant GLA synergistically enhanced the rate of hydrolysis by about 3fold for corn and wheat starch granules, compared to the sum of the individual activities, exo-endo synergism, reaction ratios, overview
additional information
effective hydrolysis of raw starch flour by the recombinant rPoGA15A preparation and alpha-amylase. Deletion of the starch-binding domain for raw starch-digesting glucoamylase rPoGA15A leads to reduced activity of the truncated enzyme with raw starches
additional information
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effective hydrolysis of raw starch flour by the recombinant rPoGA15A preparation and alpha-amylase. Deletion of the starch-binding domain for raw starch-digesting glucoamylase rPoGA15A leads to reduced activity of the truncated enzyme with raw starches
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additional information
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preparation of Ca-alginate gel beads, activation by p-benzoquinoone, and immobilization of purified enzyme, method, development, comparison of catalytic activities of free and immobilized enzyme, overview. Km values of free and entrapped glucoamylase are almost identical, while the covalently immobilized enzyme shows the lowest affinity for substrate. The covalently immobilized enzyme retains its activity over 36 days of shelf storage and after 30 repeated use runs
additional information
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sga1delta, significant reduction in conidiation
additional information
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improvement of enzyme for inductrial applications
additional information
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use of cell surface engineering to display Rhizopus oryzae glucoamylase on the cell surface of yeast Saccharomyces cerevisiae, improvement in enzymatic desizing of starched cotton cloth using yeast codisplaying glucoamylase and cellulose-binding domain, overview
additional information
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improvement of enzyme for industrial applications
additional information
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immobilization of the enzyme onto chemically synthesized poly(o-toluidine) salt and base powders using adsorption and covalent crosslinking with glutaraldehyde, overview, The immobilized enzyme has a better thermal stability than the free enzyme
additional information
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construction of a series of hybrid enzymes by interchanging domains of glucoamylase Sta1 from Saccharomyces cerevisiae and beta-glucosidase Bgl1 from Saccharomycopsis fibuligera strain ATCC 9947 based on the homology-based structural models of the two proteins. The replacement of native Bgl1 signal peptide by that of Sta1, SPS-Bgl1, increases the production of the enzyme by about threefold without affecting the ratio between the values of activity associated to cells and free in the medium
additional information
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construction of a mutant enzymes with improved catalytic activity with substrate starch by introduction of the starch binding domain from the glucoamylase of Aspergillus niger, overview
additional information
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construction of a series of hybrid enzymes by interchanging domains of glucoamylase Sta1 from Saccharomyces cerevisiae and beta-glucosidase Bgl1 from Saccharomycopsis fibuligera strain ATCC 9947 based on the homology-based structural models of the two proteins. The replacement of native Bgl1 signal peptide by that of Sta1, SPS-Bgl1, increases the production of the enzyme by about threefold without affecting the ratio between the values of activity associated to cells and free in the medium
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additional information
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enzyme is mutagenised using nitrous acid and gamma (60Co) irradiation in a sequential manner to isolate deregulated mutants for enhanced production of glucoamylase
additional information
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enzyme is mutagenised using nitrous acid and gamma (60Co) irradiation in a sequential manner to isolate deregulated mutants for enhanced production of glucoamylase
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