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Literature summary for 3.2.1.23 extracted from

  • Jurado, E.; Camacho, F.; Luzon, G.; Vicaria, J.M.
    Kinetic models of activity for b-galactosidases: influence of pH, ionic concentration and temperature (2004), Enzyme Microb. Technol., 34, 33-40.
No PubMed abstract available
Search for more literature for 3.2.1.23

Organism

Organism UniProt Comment Textmining
Kluyveromyces lactis
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Kluyveromyces marxianus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
o-nitrophenyl-beta-D-galactoside + H2O
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 Kluyveromyces marxianus o-nitrophenol + beta-D-galactose
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 ?
o-nitrophenyl-beta-D-galactoside + H2O
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 Kluyveromyces lactis o-nitrophenol + beta-D-galactose
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 ?

Synonyms

Synonyms Comment Organism
Lactozym 3000L
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 Kluyveromyces marxianus
Maxilact-L/2000
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 Kluyveromyces lactis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
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 thermal deactivation is fit to a kinetic model Kluyveromyces marxianus
additional information
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 thermal deactivation is fit to a kinetic model Kluyveromyces lactis

pH Stability

pH Stability pH Stability Maximum Comment Organism
additional information
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 proposal of two kinetic models to explain the behaviour of the enzymatic activity versus pH, implying the dissociation of one or two protons of the enzyme Kluyveromyces marxianus
additional information
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 proposal of two kinetic models to explain the behaviour of the enzymatic activity versus pH, implying the dissociation of one or two protons of the enzyme Kluyveromyces lactis