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Literature summary extracted from

  • Rodriguez, A.P.; Leiro, R.F.; Trillo, M.C.; Cerdan, M.E.; Siso, M.I.; Becerra, M.
    Secretion and properties of a hybrid Kluyveromyces lactis-Aspergillus niger beta-galactosidase (2006), Microb. Cell Fact., 5, 41.
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
3.2.1.23 industry the beta-galactosidase from Kluyveromyces lactis is a protein of outstanding biotechnological interest in the food industry and milk whey reutilization, optimization of extraction and downstream processing of the intracellular enzyme for reduction of costs in industrial production by genetic modification, overview Kluyveromyces lactis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.23 expression of wild-type and recombinant hybrid mutant enzymes in Escherichia coli strain DH5alpha Aspergillus niger
3.2.1.23 expression of wild-type and recombinant hybrid mutant enzymes in Escherichia coli strain DH5alpha Kluyveromyces lactis

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.23 additional information construction of a hybrid mutant enzyme exchanging domains from Kluyveromyces lactis and Aspergillus niger enzymes, addition of a secretory signal in the N-terminus of the recombinant protein, enzyme optimization for industrial productions by fusion with extracellular and more stable enzyme from Aspergillus niger, overview, kinetics of growth and secretion Kluyveromyces lactis
3.2.1.23 additional information construction of a hybrid mutant enzyme exchanging domains from Kluyveromyces lactis and Aspergillus niger enzymes, addition of a secretory signal in the N-terminus of the recombinant protein, Kluyveromyces lactis enzyme optimization for industrial productions by fusion with extracellular and more stable enzyme from Aspergillus niger, overview, kinetics of growth and secretion Aspergillus niger

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.23 Ca2+ slight inhibition of both the wild-type Kluyveromyces lactis enzyme and the recombinant hybrid enzyme Kluyveromyces lactis
3.2.1.23 Mn2+ activates the recombinant hybrid enzyme, but inhibits the wild-type Kluyveromyces lactis enzyme Kluyveromyces lactis
3.2.1.23 Ni2+ activates the recombinant hybrid enzyme, but inhibits the wild-type Kluyveromyces lactis enzyme Kluyveromyces lactis
3.2.1.23 Zn2+ slightly inhibits the recombinant hybrid enzyme Aspergillus niger
3.2.1.23 Zn2+ slightly activates the wild-type Kluyveromyces lactis enzyme, but slightly inhibits the recombinant hybrid enzyme Kluyveromyces lactis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.23 additional information
-
 additional information kinetics Aspergillus niger
3.2.1.23 additional information
-
 additional information kinetics Kluyveromyces lactis
3.2.1.23 0.8
-
 2-nitrophenyl-beta-D-galactopyranoside pH 6.5, 40°C, recombinant hybrid enzyme Aspergillus niger
3.2.1.23 0.8
-
 2-nitrophenyl-beta-D-galactopyranoside pH 6.5, 40°C, recombinant hybrid enzyme Kluyveromyces lactis
3.2.1.23 1.5
-
 2-nitrophenyl-beta-D-galactopyranoside pH 6.5, 40°C, wild-type enzyme Kluyveromyces lactis
3.2.1.23 8.7
-
 lactose pH 6.5, 40°C, recombinant hybrid enzyme Aspergillus niger
3.2.1.23 8.7
-
 lactose pH 6.5, 40°C, recombinant hybrid enzyme Kluyveromyces lactis
3.2.1.23 21
-
 lactose pH 6.5, 40°C, wild-type enzyme Kluyveromyces lactis

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.2.1.23 extracellular
-
 Aspergillus niger
-
-
3.2.1.23 intracellular
-
 Kluyveromyces lactis 5622
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.2.1.23 Mg2+ activation of both the wild-type Kluyveromyces lactis enzyme and the recombinant hybrid enzyme Kluyveromyces lactis
3.2.1.23 Mg2+ activation of the recombinant hybrid enzyme Aspergillus niger
3.2.1.23 Mn2+ activates the recombinant hybrid enzyme Aspergillus niger
3.2.1.23 Mn2+ activates the recombinant hybrid enzyme, but inhibits the wild-type Kluyveromyces lactis enzyme Kluyveromyces lactis
3.2.1.23 Ni2+ activates the recombinant hybrid enzyme Aspergillus niger
3.2.1.23 Ni2+ activates the recombinant hybrid enzyme, but inhibits the wild-type Kluyveromyces lactis enzyme Kluyveromyces lactis
3.2.1.23 Zn2+ slightly activates the wild-type Kluyveromyces lactis enzyme, but slightly inhibits the recombinant hybrid enzyme Kluyveromyces lactis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.1.23 lactose + H2O Aspergillus niger
-
 D-glucose + D-galactose
-
 ?
3.2.1.23 lactose + H2O Kluyveromyces lactis
-
 D-glucose + D-galactose
-
 ?
3.2.1.23 lactose + H2O Kluyveromyces lactis MW 190-9B
-
 D-glucose + D-galactose
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.23 Aspergillus niger
-
-
-
3.2.1.23 Kluyveromyces lactis
-
-
-
3.2.1.23 Kluyveromyces lactis MW 190-9B
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
3.2.1.23 beta-D-galactopyranosyl-(1-4)-beta-D-galactopyranosyl-(1-6)-beta-D-galactopyranosyl-(1-3)-beta-D-galactopyranose + 3 H2O = 4 beta-D-galactopyranose the conserved residues E482, M522, Y523 and E551 are important in catalysis Kluyveromyces lactis
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.2.1.23 additional information kinetics of growth and secretion Aspergillus niger
-
3.2.1.23 additional information liquid batch cultures, kinetics of growth and secretion Kluyveromyces lactis
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.23 2-nitrophenyl beta-D-galactopyranoside + H2O
-
 Aspergillus niger 2-nitrophenol + beta-D-galactose
-
 ?
3.2.1.23 2-nitrophenyl beta-D-galactopyranoside + H2O
-
 Kluyveromyces lactis 2-nitrophenol + beta-D-galactose
-
 ?
3.2.1.23 2-nitrophenyl beta-D-galactopyranoside + H2O
-
 Kluyveromyces lactis MW 190-9B 2-nitrophenol + beta-D-galactose
-
 ?
3.2.1.23 lactose + H2O
-
 Aspergillus niger D-glucose + D-galactose
-
 ?
3.2.1.23 lactose + H2O
-
 Kluyveromyces lactis D-glucose + D-galactose
-
 ?
3.2.1.23 lactose + H2O
-
 Kluyveromyces lactis MW 190-9B D-glucose + D-galactose
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.23 More tertiary structure of the beta-galactosidase of Kluyveromyces lactis and the recombinant hybrid enzyme, protein structure homology-modelling, overview Kluyveromyces lactis
3.2.1.23 More tertiary structure of the recombinant hybrid enzyme, protein structure homology-modelling, overview Aspergillus niger

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.23 35
-
 wild-type enzyme Kluyveromyces lactis
3.2.1.23 40
-
 recombinant mutant hybrid enzyme Aspergillus niger
3.2.1.23 40
-
 recombinant mutant hybrid enzyme Kluyveromyces lactis

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.23 30
-
 30 min, recombinant hybrid enzyme, stable Aspergillus niger
3.2.1.23 30
-
 30 min, recombinant hybrid enzyme, stable, the wild-type enzyme loses 45% activity within 60 min Kluyveromyces lactis
3.2.1.23 40
-
 15 min, recombinant hybrid enzyme, stable Aspergillus niger
3.2.1.23 40
-
 15 min, recombinant hybrid enzyme, stable, the wild-type enzyme loses 10% activity within 10 min Kluyveromyces lactis
3.2.1.23 50
-
 15 min, recombinant hybrid enzyme, loss of 40% activity Aspergillus niger
3.2.1.23 50
-
 15 min, recombinant hybrid enzyme, loss of 40% activity, the wild-type enzyme loses 60% activity Kluyveromyces lactis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.23 6.5
-
 recombinant mutant hybrid enzyme Aspergillus niger
3.2.1.23 6.5
-
 recombinant mutant hybrid enzyme Kluyveromyces lactis
3.2.1.23 7
-
 wild-type enzyme Kluyveromyces lactis