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Literature summary extracted from

  • Yang, S.; Yan, Q.; Bao, Q.; Liu, J.; Jiang, Z.
    Expression and biochemical characterization of a novel type I pullulanase from Bacillus megaterium (2017), Biotechnol. Lett., 39, 397-405 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.41 heterologously expressed in Escherichia coli Priestia megaterium

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.41 additional information
-
pullulan Km-value: 3.3 mg/ml, pH 6.5, 55°C Priestia megaterium
3.2.1.41 additional information
-
amylopectin Km-value: 3.6 mg/ml, pH 6.5, 55°C Priestia megaterium

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.41 106063
-
calculated from sequence Priestia megaterium
3.2.1.41 112000
-
SDS-PAGE Priestia megaterium

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.41 Priestia megaterium A0A173DUJ5
-
-
3.2.1.41 Priestia megaterium WW1210 A0A173DUJ5
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.41
-
Priestia megaterium

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.41 amylopectin + H2O 28% of the activity compared to pullulan, the enzyme hydrolyzes amylopectin to release mainly maltotriose, maltotetraose, maltopentaose and maltohexaose, and their contents reach to 0.0044, 0.0068, 0.0073, 0.025 and 0.035 mg/ml, respectively, after 2 h incubation Priestia megaterium maltotriose + maltotetraose + maltopentaose + maltohexaose
-
?
3.2.1.41 amylopectin + H2O 28% of the activity compared to pullulan, the enzyme hydrolyzes amylopectin to release mainly maltotriose, maltotetraose, maltopentaose and maltohexaose, and their contents reach to 0.0044, 0.0068, 0.0073, 0.025 and 0.035 mg/ml, respectively, after 2 h incubation Priestia megaterium WW1210 maltotriose + maltotetraose + maltopentaose + maltohexaose
-
?
3.2.1.41 additional information the enzyme does not show activity towards amylose, maltoheptaose, maltohexaose, maltopentaose and maltotetraose Priestia megaterium ?
-
?
3.2.1.41 additional information the enzyme does not show activity towards amylose, maltoheptaose, maltohexaose, maltopentaose and maltotetraose Priestia megaterium WW1210 ?
-
?
3.2.1.41 pullulan + H2O the enzyme hydrolyzes pullulan to yield mainly maltotriose, more than 95% Priestia megaterium maltotriose + ?
-
?
3.2.1.41 pullulan + H2O the enzyme hydrolyzes pullulan to yield mainly maltotriose, more than 95% Priestia megaterium WW1210 maltotriose + ?
-
?

Subunits

EC Number Subunits Comment Organism
3.2.1.41 ? x * 112000, SDS-PAGE Priestia megaterium
3.2.1.41 ? x * 106063, calculated from sequence Priestia megaterium

Synonyms

EC Number Synonyms Comment Organism
3.2.1.41 BmPul
-
Priestia megaterium

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.41 55
-
-
Priestia megaterium

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.2.1.41 40 60 40°C: about 35% of maximal activity, 60°C: about 25% of maximal activity Priestia megaterium

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.41 40
-
stable below Priestia megaterium

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.41 6.5
-
-
Priestia megaterium

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.2.1.41 6 9 pH 6.0: about 45% of maximal activity, pH 9.0: about 25% of maximal activity Priestia megaterium

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.2.1.41 6.5 8.5 30 min, enzyme retains more than 85% of its original activity Priestia megaterium

pI Value

EC Number Organism Comment pI Value Maximum pI Value
3.2.1.41 Priestia megaterium calculated from sequence
-
7.7