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

BRENDA support

Literature summary extracted from

  • de Lima, E.A.; Machado, C.B.; Zanphorlin, L.M.; Ward, R.J.; Sato, H.H.; Ruller, R.
    GH53 endo-beta-1,4-galactanase from a newly isolated Bacillus licheniformis CBMAI 1609 as an enzymatic cocktail supplement for biomass saccharification (2016), Appl. Biochem. Biotechnol., 179, 415-426 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.89 expressed in Escherichia coli BL21(DE3) cells Bacillus licheniformis

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.89 Cu2+ about 5% residual activity at 5 mM Bacillus licheniformis
3.2.1.89 EDTA about 60% residual activity at 5 mM Bacillus licheniformis
3.2.1.89 EGTA about 80% residual activity at 5 mM Bacillus licheniformis
3.2.1.89 Fe3+ about 2% residual activity at 5 mM Bacillus licheniformis
3.2.1.89 Zn2+ about 5% residual activity at 5 mM Bacillus licheniformis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.2.1.89 Ca2+ about 110% activity at 5 mM Bacillus licheniformis
3.2.1.89 Co2+ about 130% activity at 5 mM Bacillus licheniformis
3.2.1.89 K+ about 128% activity at 5 mM Bacillus licheniformis
3.2.1.89 Li+ about 118% activity at 5 mM Bacillus licheniformis
3.2.1.89 Mg2+ about 103% activity at 5 mM Bacillus licheniformis
3.2.1.89 Mn2+ about 115% activity at 5 mM Bacillus licheniformis
3.2.1.89 Na+ about 138% activity at 5 mM Bacillus licheniformis
3.2.1.89 Ni2+ about 145% activity at 5 mM Bacillus licheniformis

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.89 Bacillus licheniformis
-
-
-
3.2.1.89 Bacillus licheniformis CBMAI 1609
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.89 Ni2+-chelating affinity column chromatography and Superdex G200 gel filtration Bacillus licheniformis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.89 citrus fruit pectin + H2O
-
 Bacillus licheniformis ?
-
 ?
3.2.1.89 citrus fruit pectin + H2O
-
 Bacillus licheniformis CBMAI 1609 ?
-
 ?
3.2.1.89 potato galactan + H2O
-
 Bacillus licheniformis galactotetraose
-
 ?
3.2.1.89 potato galactan + H2O
-
 Bacillus licheniformis CBMAI 1609 galactotetraose
-
 ?
3.2.1.89 sugarcane bagasse + H2O
-
 Bacillus licheniformis ?
-
 ?
3.2.1.89 sugarcane bagasse + H2O
-
 Bacillus licheniformis CBMAI 1609 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.89 ? x * 48300, calculated from amino acid sequence Bacillus licheniformis

Synonyms

EC Number Synonyms Comment Organism
3.2.1.89 GAL
-
 Bacillus licheniformis
3.2.1.89 GH53 endo-beta-1,4-galactanase
-
 Bacillus licheniformis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.89 40
-
-
 Bacillus licheniformis

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.2.1.89 20 45 about 20% activity at 20°C, about 50% activity at 30°C, 100% activity at 40°C, about 70% activity at 45°C, no activity at 50°C Bacillus licheniformis

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.89 25 45 the enzyme retains nearly 100% activity after 1 h at pH 7.0 at 25-45°C, The melting temperature is 52.9°C Bacillus licheniformis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.2.1.89 555.8
-
 potato galactan at pH 6.0 and 40°C Bacillus licheniformis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.89 6.5 8 the enzyme shows maximum activity (more than 90 %) in the pH range over 6.5 to 8.0 Bacillus licheniformis

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.2.1.89 6 9 the enzyme retains 75% activity at pH values 6.0 and 9.0 Bacillus licheniformis

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.2.1.89 4 10 the enzyme retains more than 75 % activity after 24 h at pH 4.0-10.0 Bacillus licheniformis

pI Value

EC Number Organism Comment pI Value Maximum pI Value
3.2.1.89 Bacillus licheniformis calculated from amino acid sequence
-
 5.9