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BRENDA support

Literature summary extracted from

  • Rasouli, N.; Sohrabi, N.; Zamani, M.
    Influence of a novel magnetic recoverable support on kinetic, stability and activity of beta-amylase enzyme (2016), Phys. Chem. Res., 4, 271-283 .
No PubMed abstract available

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.2 additional information covalent immobilization of beta-amylase enzyme on the surface of modified magnetic nanoparticles (ZnFe2O4-SiO2-NH2). The magnetic nanoparticles of ZnFe2O4 are synthesized by chemical co-precipitation method, and then tetraethyl orthosilicate (TEOS) and 3-aminopropyltriethoxy silane (APTES) are used for modification of ZnFe2O4 nanoparticles with silica and amine groups (ZnFe2O4-SiO2-NH2, classical Stoeber method). The aminated surface of ZnFe2O4 nanoparticles is exposed to beta-amylase immobilization using trichlorotriazine (TCT) as covalent agent. The immobilized beta-amylase enzyme is characterized by techniques such as Fourier transform infrared (FT-IR), scanning electron microscopy (SEM), powder X-ray diffraction (XRD) and energy dispersive X-ray analysis (EDAX). The immobilized enzyme shows increased catalytic activity and efficiency, as well as thermal stability compared to free enzyme. Highest activity at pH 7.0 and 40°C. Method evaluation and kinetics, overview Ipomoea batatas

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.2 additional information
-
 additional information Michaelis-Menten kinetics, modelling Ipomoea batatas
3.2.1.2 5.64
-
 starch immobilized enzyme, pH 7.0, 40°C Ipomoea batatas
3.2.1.2 7.49
-
 starch free enzyme, pH 7.0, 40°C Ipomoea batatas

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.2 Ipomoea batatas P10537
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.2.1.2 commercial preparation
-
 Ipomoea batatas
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.2 starch + H2O soluble starch Ipomoea batatas ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.2.1.2 1,4-alpha-D-glucan maltohydrolase UniProt Ipomoea batatas
3.2.1.2 beta amylase
-
 Ipomoea batatas
3.2.1.2 Bmy1
-
 Ipomoea batatas

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.2 40
-
 free and immobilized enzyme Ipomoea batatas

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.2.1.2 30 60 the immobilized enzyme shows over 70% of maximal activity within this range, while the free enzyme only shows over 50% of maximal activity within this range Ipomoea batatas

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.2 7
-
 free and immobilized enzyme Ipomoea batatas

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.2.1.2 4 8 immobilized enzyme, over 50% of maximal activity within this range Ipomoea batatas
3.2.1.2 5 7.5 free enzyme, over 50% of maximal activity within this range Ipomoea batatas