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Literature summary for 3.2.1.41 extracted from

  • Li, L.; Dong, F.; Lin, L.; He, D.; Wei, W.; Wei, D.
    N-Terminal domain truncation and domain insertion-based engineering of a novel thermostable type I pullulanase from Geobacillus thermocatenulatus (2018), J. Agric. Food Chem., 66, 10788-10798 .
    View publication on PubMed
Search for more literature for 3.2.1.41

Activating Compound

Activating Compound Comment Organism Structure
dithiothreitol 10 mM, 2.4fold activation Geobacillus thermocatenulatus
Triton X-100 0.1%, 1.2fold activation. 1%, 1.3fold activation Geobacillus thermocatenulatus

Application

Application Comment Organism
food industry the enzyme can be used directly for maize starch saccharification without adjusting the pH, which reduces cost and improves efficiency Geobacillus thermocatenulatus

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli BL21 (DE3) Geobacillus thermocatenulatus

Protein Variants

Protein Variants Comment Organism
additional information different N-terminally domain truncated (730T) or spliced (730T-U1 and 730T-U2) mutants are constructed. Truncating the N-terminal 85 amino acids decreases the Km value and does not change its optimum pH. Wild-type enzyme can exhibit almost entirely soluble expression, but inclusion bodies are formed after truncating 85 amino acids from its N-terminus. This indicates that the N-terminal 85 amino acids of PulGT are responsible for ensuring secretory protein folding and maintaining its stability Geobacillus thermocatenulatus

Inhibitors

Inhibitors Comment Organism Structure
alpha-cyclodextrin 1%, 99% inhibition Geobacillus thermocatenulatus
CaCl2 1 mM, 1.8fold activation. 5 mM, 66% loss of activity. 10 mM, 97% loss of activity Geobacillus thermocatenulatus
CoCl2 1 mM, 97% inhibition Geobacillus thermocatenulatus
CuCl2 1 mM, complete inhibition Geobacillus thermocatenulatus
EDTA 5 mM, complete inhibition Geobacillus thermocatenulatus
Urea 2 M, complete inhibition Geobacillus thermocatenulatus
ZnSO4 1 mM, complete inhibition Geobacillus thermocatenulatus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 pullulan pH 6.5, 70°C Geobacillus thermocatenulatus

Metals/Ions

Metals/Ions Comment Organism Structure
CaCl2 1 mM, 1.8fold activation. 5 mM, 66% loss of activity. 10 mM, 97% loss of activity Geobacillus thermocatenulatus
MgCl2 1 mM, 1.5fold activation. 5 mM, 1.8fold activation. 10 mM, 1.1fold activation Geobacillus thermocatenulatus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
80000
-
 SDS-PAGE Geobacillus thermocatenulatus
80370
-
 calculated from sequence Geobacillus thermocatenulatus

Organism

Organism UniProt Comment Textmining
Geobacillus thermocatenulatus A0A1V0FWX7
-
-
Geobacillus thermocatenulatus DSMZ730 A0A1V0FWX7
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
192.56
-
 Km-value: 22.4 mg/ml, 70 °C, pH 6.5, recombinant wild-type enzyme Geobacillus thermocatenulatus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
amylopectin + H2O the enzyme specifically attacks alpha-1,6-linkages of branched oligosaccharides Geobacillus thermocatenulatus ?
-
 ?
amylopectin + H2O the enzyme specifically attacks alpha-1,6-linkages of branched oligosaccharides Geobacillus thermocatenulatus DSMZ730 ?
-
 ?
additional information the enzyme has no activity toward alpha-1,4-glycosidic linkages Geobacillus thermocatenulatus ?
-
 ?
additional information the enzyme has no activity toward alpha-1,4-glycosidic linkages Geobacillus thermocatenulatus DSMZ730 ?
-
 ?
pullulan + H2O
-
 Geobacillus thermocatenulatus maltotriose + ?
-
 ?
pullulan + H2O
-
 Geobacillus thermocatenulatus DSMZ730 maltotriose + ?
-
 ?
soluble starch + H2O the enzyme specifically attacks alpha-1,6-linkages of branched oligosaccharides Geobacillus thermocatenulatus ?
-
 ?
soluble starch + H2O the enzyme specifically attacks alpha-1,6-linkages of branched oligosaccharides Geobacillus thermocatenulatus DSMZ730 ?
-
 ?

Synonyms

Synonyms Comment Organism
pulGT
-
 Geobacillus thermocatenulatus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
70
-
 wild-type enzyme Geobacillus thermocatenulatus

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
50 80 50°C: about 60% of maximal activity, 80°C: about 30% of maximal activity, wild-type enzyme Geobacillus thermocatenulatus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
60
-
 3 h, about 45% loss of activity. 1 h, about 20% loss of activity, wild-type enzyme Geobacillus thermocatenulatus
70
-
 3 h, about 75% loss of activity. 1 h, about 20% loss of activity, wild-type enzyme Geobacillus thermocatenulatus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5
-
 sodium phosphate buffer, wild-type enzyme Geobacillus thermocatenulatus

pH Range

pH Minimum pH Maximum Comment Organism
5 9 pH 5.0: about 80% of maximal activity, pH 9.0: about 35% of maximal activity, wild-type enzyme Geobacillus thermocatenulatus

pH Stability

pH Stability pH Stability Maximum Comment Organism
5
-
 4°C, 60 min, 75% residual activity, wild-type enzyme Geobacillus thermocatenulatus
6
-
 4°C, 60 min, 90% residual activity, wild-type enzyme Geobacillus thermocatenulatus
7
-
 4°C, 60 min, 85% residual activity, wild-type enzyme Geobacillus thermocatenulatus
8
-
 4°C, 60 min, 70% residual activity, wild-type enzyme Geobacillus thermocatenulatus
9
-
 4°C, 60 min, 55% residual activity, wild-type enzyme Geobacillus thermocatenulatus

pI Value

Organism Comment pI Value Maximum pI Value
Geobacillus thermocatenulatus calculated from sequence
-
 5.53