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Literature summary for 3.2.1.23 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
Search for more literature for 3.2.1.23

Application

Application Comment Organism
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)

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

Protein Variants

Protein Variants Comment Organism
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
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

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

KM Value [mM]

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

Localization

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

Metals/Ions

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

Natural Substrates/ Products (Substrates)

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

Organism

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

Reaction

Reaction Comment Organism Reaction ID
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

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

Substrates and Products (Substrate)

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

Subunits

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

Temperature Optimum [°C]

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

Temperature Stability [°C]

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

pH Optimum

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