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Literature summary extracted from

  • Niu, C.; Zhu, L.; Wang, J.; Li, Q.
    Simultaneous enhanced catalytic activity and thermostability of a 1,3-1,4-beta-glucanase from Bacillus amyloliqueformis by chemical modification of lysine residues (2014), Biotechnol. Lett., 36, 2453-2460.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.73 recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) Bacillus amyloliquefaciens

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.73 additional information modifying five (out of 12) epsilon-amino groups in lysine residues with nitrous acid improves thermostablility and enzymatic activity of the enzyme, optimizing the condition of chemical modification, overview. Compared to the wild-type enzyme, the optimally-modified enzyme has higher specific activity and T50 value, which are 3370 U/mg and 70°C, respectively. Its half-life values at 50 and 60°C are extended and reach 58.5 and 49.5 min, respectively Bacillus amyloliquefaciens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.73 additional information
-
 additional information 7.9 mg/ml for recombinant wild-type enzyme, 7.2 mg/ml for recombinant optimally-modified enzyme, with AZO blue beta-glucan at pH 6.5, 40°C Bacillus amyloliquefaciens

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.73 Bacillus amyloliquefaciens
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.73 recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration Bacillus amyloliquefaciens

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.2.1.73 2717
-
 recombinant wild-type enzyme, pH 6.5, 40°C, substrate AZO blue beta-glucan Bacillus amyloliquefaciens
3.2.1.73 3370
-
 recombinant optimally-modified enzyme, pH 6.5, 40°C, substrate AZO blue beta-glucan Bacillus amyloliquefaciens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.73 AZO blue beta-glucan + H2O
-
 Bacillus amyloliquefaciens ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.2.1.73 1,3-1,4-beta-glucanase
-
 Bacillus amyloliquefaciens
3.2.1.73 BglA
-
 Bacillus amyloliquefaciens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.73 55
-
-
 Bacillus amyloliquefaciens

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.2.1.73 35 65 activity range, wild-type and optimally-modified enzymes, overview Bacillus amyloliquefaciens

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.73 60 70 purified recombinant enzyme, the wild-type enzymes activity decline rapidly above 60°C, while the optimally-modified enzyme is more stable and shows activity up to 70°C Bacillus amyloliquefaciens

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.2.1.73 109
-
 AZO blue beta-glucan recombinant wild-type enzyme, pH 6.5, 40°C Bacillus amyloliquefaciens
3.2.1.73 267
-
 AZO blue beta-glucan recombinant optimally-modified enzyme, pH 6.5, 40°C Bacillus amyloliquefaciens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.73 6.5
-
-
 Bacillus amyloliquefaciens

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.2.1.73 4.5 8 activity range, wild-type and optimally-modified enzymes, overview Bacillus amyloliquefaciens

General Information

EC Number General Information Comment Organism
3.2.1.73 additional information three-dimensional structure modelling Bacillus amyloliquefaciens