3.2.1.133: glucan 1,4-alpha-maltohydrolase
This is an abbreviated version!
For detailed information about glucan 1,4-alpha-maltohydrolase, go to the full flat file.
Word Map on EC 3.2.1.133
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3.2.1.133
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amylases
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baking
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bake
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food industry
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synthesis
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cgtases
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maltooligosaccharide
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amylopectin
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enzyme-total
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alpha-amylases
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novozymes
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staling
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beta-cds
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crumb
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stale
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antistaling
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nutrition
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biotechnology
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medicine
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degradation
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pharmacology
- 3.2.1.133
- amylases
-
baking
-
bake
- food industry
- synthesis
- cgtases
- maltooligosaccharide
- amylopectin
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enzyme-total
- alpha-amylases
-
novozymes
-
staling
- beta-cds
-
crumb
-
stale
-
antistaling
- nutrition
- biotechnology
- medicine
- degradation
- pharmacology
Reaction
Synonyms
alpha-amylase, AmyB, BbmA, BSMA, BSTA, BTMA, CAZy-GH13, glucan 1,4-alpha-maltohydrolase, glucan-1,4-alpha-maltohydrolase, Gt-MamyIII, LGMA, MAase, MABS, MAG1, maltogenase L, maltogenic alpha-amylase, maltogenic amylase, maltose-forming alpha-amylase, MAmy, MAUS149, More, NM319, NM326, NM398, NM404, NM447, Novamyl, PSMA, Smar_0613, SMMA, TCMA, Thermus maltogenic amylase, ThMA, TK4MA
ECTree
3.2.1.133 glucan 1,4-alpha-maltohydrolaseAdvanced search results
results (
results (Engineering
Engineering on EC 3.2.1.133 - glucan 1,4-alpha-maltohydrolase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D30A/K40R/D261G
D46G
the mutant behaves similar to the wild type enzyme regarding thermoactivity, thermostability and pH profile. The Km values of the mutant for all substrates are strongly increased compared to the wild type enzyme
D46N
the mutant behaves similar to the wild type enzyme regarding kinetic parameters, thermoactivity, thermostability and pH profile
D46V
the mutant behaves similar to the wild type enzyme regarding thermoactivity, thermostability and pH profile. The affinity and catalytic efficiency of the mutant toward beta-cyclodextrin are increased 5fold as compared with the wild type enzyme
D46V/P78L/V145A/K548E
the half-life times for the mutant at 50°C and 55°C are 70 min and 25 min, compared to 30 min and 13 min for the wild type, respectively
F188L/D261G/T288P
G312A
the mutant has an optimal temperature of 45°C instead of the 40°C for the wild type enzyme
G312A/K436R
the half-life time at 55°C increase from 15 to 25 min for the double mutant
K436R
the mutant has an optimal temperature of 45°C instead of the 40°C for the wild type enzyme
N115D/F188L
T142A
T142A/D261G/N327S/K425E/K520R/N5951
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variant NM404, medium thermotolerance due to D261G mutation
T142A/D261G/N327S/K425E/K520R/N595I
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Novamyl variant NM404, similar to wild-type at pH 4.0
F188L/D261G/T288P
T142A
D46G
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the mutant behaves similar to the wild type enzyme regarding thermoactivity, thermostability and pH profile. The Km values of the mutant for all substrates are strongly increased compared to the wild type enzyme
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D46N
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the mutant behaves similar to the wild type enzyme regarding kinetic parameters, thermoactivity, thermostability and pH profile
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D46V
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the mutant behaves similar to the wild type enzyme regarding thermoactivity, thermostability and pH profile. The affinity and catalytic efficiency of the mutant toward beta-cyclodextrin are increased 5fold as compared with the wild type enzyme
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D46V/P78L/V145A/K548E
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the half-life times for the mutant at 50°C and 55°C are 70 min and 25 min, compared to 30 min and 13 min for the wild type, respectively
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G312A
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the mutant has an optimal temperature of 45°C instead of the 40°C for the wild type enzyme
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G312A/K436R
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the half-life time at 55°C increase from 15 to 25 min for the double mutant
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K436R
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the mutant has an optimal temperature of 45°C instead of the 40°C for the wild type enzyme
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N147D/F195L/N263S/D311G/A344V/F397S/N508D
mutant III-1, seven mutations, generated by random mutagenesis after three rounds of DNA shuffling and recombination, lineage of shuffling mutants indicated
N147D/F195L/N263S/D311G/A344V/F397S/N508D/M375T
additional exchange M375T of mutant III-2 responsible for decreased specific activity, lineage of shuffling mutants shown
N147D/F195L/N263S/D311G/A344V/F397S/N508D
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mutant III-1, seven mutations, generated by random mutagenesis after three rounds of DNA shuffling and recombination, lineage of shuffling mutants indicated
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N147D/F195L/N263S/D311G/A344V/F397S/N508D/M375T
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additional exchange M375T of mutant III-2 responsible for decreased specific activity, lineage of shuffling mutants shown
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W177F
transglycosylation activities of the mutant enzyme decreases by 18% as the hydrophilicity of the residue at position 177 increases. The mutant enzyme exhibits notable enhancements in maltose production. The maltotriose content is substantially lower than that of the syrup produced using the wild-type enzyme
W177L
transglycosylation activities of the mutant enzyme decreases by 37% as the hydrophilicity of the residue at position 177 increases. The mutant enzyme exhibits notable enhancements in maltose production. The maltotriose content is substantially lower than that of the syrup produced using the wild-type enzyme
W177N
transglycosylation activities of the mutant enzyme decreases by 45% as the hydrophilicity of the residue at position 177 increases. The mutant enzyme exhibits notable enhancements in maltose production. The maltotriose content is substantially lower than that of the syrup produced using the wild-type enzyme
W177S
transglycosylation activities of the mutant enzyme decreases by 52% as the hydrophilicity of the residue at position 177 increases. The mutant enzyme exhibits notable enhancements in maltose production. The maltotriose content is substantially lower than that of the syrup produced using the wild-type enzyme
W177Y
transglycosylation activities of the mutant enzyme decreases by 20% as the hydrophilicity of the residue at position 177 increases. The mutant enzyme exhibits notable enhancements in maltose production. The maltotriose content is substantially lower than that of the syrup produced using the wild-type enzyme
D109A
the mutant shows increased affinity towards amylose, amylopectin and starch, and a decreased affinity towards alpha- and beta-cyclodextrin
D109E
the mutant does not show any effect on the binding affinity and substrate hydrolytic efficiency towards alpha- and beta-cyclodextrin but a strong decline in the affinity and substrate hydrolytic efficiency of the mutant enzyme towards amylopectin
F218A
the mutant shows wild type activity with alpha-1,6-glycosidic bond hydrolysis and about 4fold increased activity with alpha-1,4-glycosidic bond hydrolysis compared to the wild type enzyme
F218A
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the mutant shows wild type activity with alpha-1,6-glycosidic bond hydrolysis and about 4fold increased activity with alpha-1,4-glycosidic bond hydrolysis compared to the wild type enzyme
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A290I
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mutant enzyme A290I produces mostly maltose from maltotetraose, while wild-type enzyme produces glucose as well as maltose. kcat/KM of mutant enzyme 290I for maltose is 48times less than that of wild-type enzyme. kcat/Km for maltotriose is 18.5fold lower than wild-type enzyme. kcat/Km for maltotetraose is 2.9fold lower than wild-type enzyme. kcat/Km for maltopentaose is 2.5fold lower than wild-type enzyme. kcat/Km for maltohexaose is 1.9fold lower than wild-type enzyme. kcat/Km for maltoheptaose is 4.7fold lower than wild-type enzyme
A330G/N331C/E332C
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F-18, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type
A330G/N331G/E332C
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C-20, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type
A330G/N331G/E332G
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G-91, strong reduction of all substrate hydrolyzing activities, higher relative specificity to beta-cyclodextrin than to starch compared to wild-type, lower relative specificity to maltotriose than to acarbose compared to wild-type, transglycosylation: high amount of branched tetraose and pentaose
A330G/N331G/E332S
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G-22, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type
A330G/N331P/E332G
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C-43, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type
A330G/N331V/E332G
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G-90, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type
A330M/N331G/E332C
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B-96, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type
A330S/N331A
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F-80, strong reduction of all substrate hydrolyzing activities, higher relative specificity to beta-cyclodextrin and pullulan than to starch compared to wild-type, lower relative specificity to maltotriose than to acarbose compared to wild-type, transglycosylation: high amount of branched tetraose and pentaose
A330S/N331G/E332T
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K-37, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodexxtrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type
E332D
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site-directed mutagenesis, significantly decreased transglycosylation activity
E332H
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site-directed mutagenesis, replacing Glu 332 with histidine reduces transglycosylation activity significantly, but enhances hydrolysis activity on alpha-(1,3)-, alpha-(1,4)- and alpha-(1,6) glycosidic bonds relative to the wild-type
G50I/D109E
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double mutation, two main residues of the catalytic binding pocket, site-directed mutagenesis
G50I/D109E/V431I
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triple mutation of three main residues of the catalytic binding pocket, site-directed mutagenesis
N331S/E332G
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I-69, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type
R26Q/I152N/S153N/S169N/I333V/A398V/Q411L/P453L
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mutant enzyme shows highly improved thermostability and catalytic activity in presence of Ca2+
V329A/A330C/N331G/E332V
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A-39, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type
V329A/A330G/N331V/E332A
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G-13, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type
V329A/N331L
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B-4, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch compared to wild-type
V329C/N331H/E332R
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D-3, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type
V329F/A330T/N331G/E332W
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I-70, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type
V329G/A330L/N331V/E332Y
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H-16, slightly higher activity with cyclodextrin, pullulan, and starch, reduced activities with maltotriose, and acarbose, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type, similar transglysocylation pattern as wild-type
V329I/A330G/N331W
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C-56, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type
V329S/A330C/N331S/E332P
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A-18, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type
V329S/A330G/N331D
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K-33, strong reduction of all substrate hydrolyzing activities, products of acarbose hydrolization are glucose, maltose, and acarviosine instead of only glucose and carviosine-glucose as in the wild-type reaction, higher relative specificity to beta-cyclodextrin than to starch compared to wild-type, lower relative specificity to maltotriose than to acarbose compared to wild-type, transglycosylation: very little amount of transfer products, with acarbose significant amount of acarviosine and maltose
V329S/A330G/N331G/E332V
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E-74, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type
V329T/A330C/N331T/E332V
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E-50, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type
additional information
D30A/K40R/D261G
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Novamyl variant NM398, similar to wild-type at pH 4.0
D30A/K40R/D261G
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variant NM398, medium thermotolerance due to D261G mutation
F188L/D261G/T288P
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Novamyl variant NM447, outperform wild-type Novamyl in bread at pH 4.3. Wild-type Novamyl requires a nearly 30fold protein dosage increase over NM447 to obtain anti-staling bread properties. NM447 appears to have a broad pH functionality profile and performs better than wild-type Novamyl in standard bread to pH 5.9. It seems to be be generally tehrmally stabilized, both at pH 4.0 and 5.0.
F188L/D261G/T288P
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variant NM447, most thermotolerant, probably due to F188L mutation, but reduced activity, medium thermotolerance due to D261G mutation, improved anti-staling performance in application test, about 70% activity retained after incubation at 80°C at pH 4.3 for 25 min
N115D/F188L
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Novamyl variant NM319, similar to wild-type at pH 4.0, at pH 5.5 the variant outperform wild-type Novamyl, significantly more thermally stable that wild-type
N115D/F188L
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variant NM319, most thermotolerant, probably due to F188L mutation, but reduced activity, improved anti-staling performance in application test, about 40% activity retained after incubation at 80°C at pH 4.3 for 25 min
T142A
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variant NM326, inducing 20% activity increase and 50% thermal stability increase
F188L/D261G/T288P
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Novamyl variant NM447, outperform wild-type Novamyl in bread at pH 4.3. Wild-type Novamyl requires a nearly 30fold protein dosage increase over NM447 to obtain anti-staling bread properties. NM447 appears to have a broad pH functionality profile and performs better than wild-type Novamyl in standard bread to pH 5.9. It seems to be be generally tehrmally stabilized, both at pH 4.0 and 5.0.
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F188L/D261G/T288P
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variant NM447, most thermotolerant, probably due to F188L mutation, but reduced activity, medium thermotolerance due to D261G mutation, improved anti-staling performance in application test, about 70% activity retained after incubation at 80°C at pH 4.3 for 25 min
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T142A
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variant NM326, inducing 20% activity increase and 50% thermal stability increase
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additional information
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mutagenesis is induced by error-prone PCR, mutagenic fragments screened for thermostable variants (80°C) at low pH 4.3, most thermostable variants show a decreased activity to the wild-type enzyme
additional information
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mutagenesis is induced by error-prone PCR, mutagenic fragments screened for thermostable variants (80°C) at low pH 4.3, most thermostable variants show a decreased activity to the wild-type enzyme
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additional information
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tapioca starch is modified using branching enzyme, BE, isolated from, Bacillus subtilis strain 168, and Bacillus stearothermophilus maltogenic amylase, BSMA. BE cleaves alpha-1,4 linkages of amylose and amylopectin, and moiety of glycosyl residues are transferred to another amylose and amylopectin to produce branched glucan and branching enzyme-treated tapioca starch by forming alpha-1,6 branch linkages. The product is further modified with BSMA to produce highly-branched tapioca starch with 9.7% of extra branch points, overview
additional information
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Random substitutions of amino acid residues Val329, Ala330, Asn331, and Glu332 that are forming an extra sugar-binding space with combinatorial saturation mutagenesis technique: substrate specificity, hydrolysis pattern, and transglycosylation activity of ThMA are modulated by these mutations. Activity assays with substrates: soluble starch, pullulan, beta-cyclodextrin, maltotriose, and acarbose at 60°C, pH 6.0 sodium-acetate buffer
