Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Sun, Y.; Duan, X.; Wang, L.; Wu, J.
    Enhanced maltose production through mutagenesis of acceptor binding subsite +2 in Bacillus stearothermophilus maltogenic amylase (2016), J. Biotechnol., 217, 53-61 .
    View publication on PubMed

Application

EC Number Application Comment Organism
3.2.1.133 food industry maltogenic amylases are used to decrease the maltotriose content of high maltose syrups. However, due to the interplay between the hydrolysis and transglycosylation activities of maltogenic amylases, the maltotriose contents of these syrups are still greater than that necessary for pure maltose preparation. Mutant enzyme W177S, shows decreased transglycosylation activity and enhanced maltose production. It will deliver performance superior to that of the wild-type under industrial conditions Geobacillus stearothermophilus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.133 expression in Escherichia coli strains BL21(DE3) Geobacillus stearothermophilus

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.133 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 Geobacillus stearothermophilus
3.2.1.133 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 Geobacillus stearothermophilus
3.2.1.133 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 Geobacillus stearothermophilus
3.2.1.133 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 Geobacillus stearothermophilus
3.2.1.133 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 Geobacillus stearothermophilus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.133 12.3
-
 maltotriose pH 5.5, 60°C, wild-type enzyme Geobacillus stearothermophilus
3.2.1.133 16.4
-
 maltotriose pH 5.5, 60°C, mutant enzyme W177F Geobacillus stearothermophilus
3.2.1.133 22
-
 maltotriose pH 5.5, 60°C, mutant enzyme W177Y Geobacillus stearothermophilus
3.2.1.133 28
-
 maltotriose pH 5.5, 60°C, mutant enzyme W177L Geobacillus stearothermophilus
3.2.1.133 31.7
-
 maltotriose pH 5.5, 60°C, mutant enzyme W177N Geobacillus stearothermophilus
3.2.1.133 35.3
-
 maltotriose pH 5.5, 60°C, mutant enzyme W177S Geobacillus stearothermophilus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.133 69000
-
 SDS-PAGE Geobacillus stearothermophilus

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.133 Geobacillus stearothermophilus P19531
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.133
-
 Geobacillus stearothermophilus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.133 maltotriose + H2O
-
 Geobacillus stearothermophilus alpha-maltose + glucose
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.133 ? x * 69000, SDS-PAGE Geobacillus stearothermophilus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.133 50
-
 hydrolysis of maltotriose, mutant enzyme W177Y Geobacillus stearothermophilus
3.2.1.133 60
-
 hydrolysis of maltotriose, wild-type enzyme and mutant enzymes W177F, W177L, W177N, and W177S Geobacillus stearothermophilus

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.2.1.133 30 70 30°C: about 40% of maximal activity, 70°C: about 65% of maximal activity, hydrolysis of maltotriose, mutant enzyme W177Y Geobacillus stearothermophilus
3.2.1.133 50 80 50°C: about 70% of maximal activity, 80°C: about 40% of maximal activity, hydrolysis of maltotriose, wild-type enzyme Geobacillus stearothermophilus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.133 60
-
 half-life: 325 h (wild-type enzyme), 95 h (mutant enzyme W177F), 250 h (mutant enzyme W177Y), 200 h (mutant enzyme W177L), 150 h (mutant enzyme W177N), 192 h (mutant enzyme W177S) Geobacillus stearothermophilus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.2.1.133 70.97
-
 maltotriose pH 5.5, 60°C, mutant enzyme W177F Geobacillus stearothermophilus
3.2.1.133 108.25
-
 maltotriose pH 5.5, 60°C, mutant enzyme W177Y Geobacillus stearothermophilus
3.2.1.133 126.2
-
 maltotriose pH 5.5, 60°C, mutant enzyme W177L Geobacillus stearothermophilus
3.2.1.133 137.2
-
 maltotriose pH 5.5, 60°C, wild-type enzyme Geobacillus stearothermophilus
3.2.1.133 150.98
-
 maltotriose pH 5.5, 60°C, mutant enzyme W177N Geobacillus stearothermophilus
3.2.1.133 182.82
-
 maltotriose pH 5.5, 60°C, mutant enzyme W177S Geobacillus stearothermophilus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.133 5.5
-
 hydrolysis of maltotriose, wild-type enzyme and mutant enzymes W177F, W177L, W177N, W177Y and W177S Geobacillus stearothermophilus

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.2.1.133 4 6.5 pH 4.0: about 65% of maximal activity, pH 6.5: about 60% of maximal activity, hydrolysis of maltotriose, wild-type enzyme Geobacillus stearothermophilus

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.2.1.133 261.3
-
 maltotriose pH 5.5, 60°C, mutant enzyme W177F Geobacillus stearothermophilus
3.2.1.133 270.4
-
 maltotriose pH 5.5, 60°C, mutant enzyme W177L Geobacillus stearothermophilus
3.2.1.133 285.8
-
 maltotriose pH 5.5, 60°C, mutant enzyme W177N Geobacillus stearothermophilus
3.2.1.133 295.2
-
 maltotriose pH 5.5, 60°C, mutant enzyme W177Y Geobacillus stearothermophilus
3.2.1.133 310.7
-
 maltotriose pH 5.5, 60°C, mutant enzyme W177S Geobacillus stearothermophilus
3.2.1.133 669.2
-
 maltotriose pH 5.5, 60°C, wild-type enzyme Geobacillus stearothermophilus