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Literature summary for 3.2.1.23 extracted from

  • Landman, O.E.
    Properties and induction of beta-galactosidase in Bacillus megaterium (1957), Biochim. Biophys. Acta, 23, 558-569.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
D-fructose slightly stimulating Priestia megaterium
D-glucose slightly stimulating Priestia megaterium
maltose slightly stimulating Priestia megaterium
additional information no activation by melibiose and raffinose Priestia megaterium
sucrose slightly stimulating Priestia megaterium

General Stability

General Stability Organism
non-specific enzyme stabilization by amino acids, overview Priestia megaterium

Metals/Ions

Metals/Ions Comment Organism Structure
Cs+ stimulates Priestia megaterium
K+ stimulates Priestia megaterium
Li+ stimulates Priestia megaterium
Mn2+ stimulates Priestia megaterium
Na+ stimulates Priestia megaterium
NH4+ stimulates Priestia megaterium

Organism

Organism UniProt Comment Textmining
Priestia megaterium
-
inducible enzyme
-
Priestia megaterium KM / ATCC 13632
-
inducible enzyme
-

Purification (Commentary)

Purification (Comment) Organism
native enzyme by MnSO4 or streptomycin precipitation, ammonium sulfate fractionation, and starch column electrophoresis Priestia megaterium

Storage Stability

Storage Stability Organism
-20°C, crude enzyme extract, 24 h, fully stable, loss of 49% activity after 12 days, partially purified enzyme is stable for 60 days Priestia megaterium

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-nitrophenyl beta-D-galactopyranoside + H2O
-
Priestia megaterium 2-nitrophenol + beta-D-galactose
-
?
2-nitrophenyl beta-D-galactopyranoside + H2O
-
Priestia megaterium KM / ATCC 13632 2-nitrophenol + beta-D-galactose
-
?
lactose + H2O
-
Priestia megaterium beta-D-glucose + beta-D-galactose
-
?
lactose + H2O
-
Priestia megaterium KM / ATCC 13632 beta-D-glucose + beta-D-galactose
-
?
additional information the enzyme hydrolyzes methyl-, butyl-, and phenyl-beta-D-galactosides, no activity with thiomethyl-and thiophenyl-beta-D-galactosides or with methyl-beta-L-arabinoside Priestia megaterium ?
-
?
additional information the enzyme hydrolyzes methyl-, butyl-, and phenyl-beta-D-galactosides, no activity with thiomethyl-and thiophenyl-beta-D-galactosides or with methyl-beta-L-arabinoside Priestia megaterium KM / ATCC 13632 ?
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
40
-
assay at Priestia megaterium

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
55
-
5 min, loss of 42% activity in 0.5 M K2HPO4 buffer, no activity loss in 1.5 M K2HP04 Priestia megaterium

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.3 8
-
Priestia megaterium

pH Range

pH Minimum pH Maximum Comment Organism
6 9 pH profile Priestia megaterium