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Literature summary for 3.2.1.23 extracted from

  • Otieno, D.O.; Shah, N.P.
    Endogenous beta-glucosidase and beta-galactosidase activities from selected probiotic micro-organisms and their role in isoflavone biotransformation in soymilk (2007), J. Appl. Microbiol., 103, 910-917.
    View publication on PubMed
Search for more literature for 3.2.1.23

Application

Application Comment Organism
nutrition the enzyme is important in hydrolysis of the predominant isoflavone glycosides into isoflavone aglycones in order to improve biological activity of soymilk, overview Lacticaseibacillus casei
nutrition the enzyme is important in hydrolysis of the predominant isoflavone glycosides into isoflavone aglycones in order to improve biological activity of soymilk, overview Lactobacillus acidophilus
nutrition the enzyme is important in hydrolysis of the predominant isoflavone glycosides into isoflavone aglycones in order to improve biological activity of soymilk, overview Bifidobacterium animalis

Organism

Organism UniProt Comment Textmining
Bifidobacterium animalis
-
 ssp. lactis, strain Bb12
-
Lacticaseibacillus casei
-
-
-
Lacticaseibacillus casei 2607
-
-
-
Lactobacillus acidophilus
-
 strain ATCC 4461
-

Source Tissue

Source Tissue Comment Organism Textmining
additional information organism in soymilk Lacticaseibacillus casei
-
additional information organism in soymilk Lactobacillus acidophilus
-
additional information organism in soymilk Bifidobacterium animalis
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
 detection of enzyme activity and concentration of isoflavone aglycones during fermentation of soymilk, overview Lacticaseibacillus casei
additional information
-
 detection of enzyme activity and concentration of isoflavone aglycones during fermentation of soymilk, overview Lactobacillus acidophilus
additional information
-
 detection of enzyme activity and concentration of isoflavone aglycones during fermentation of soymilk, overview Bifidobacterium animalis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-nitrophenyl beta-D-galactopyranoside + H2O
-
 Lacticaseibacillus casei 2-nitrophenol + beta-D-galactose
-
 ?
2-nitrophenyl beta-D-galactopyranoside + H2O
-
 Lactobacillus acidophilus 2-nitrophenol + beta-D-galactose
-
 ?
2-nitrophenyl beta-D-galactopyranoside + H2O
-
 Bifidobacterium animalis 2-nitrophenol + beta-D-galactose
-
 ?
2-nitrophenyl beta-D-galactopyranoside + H2O
-
 Lacticaseibacillus casei 2607 2-nitrophenol + beta-D-galactose
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 in vivo fermentation temperature and assay at Lacticaseibacillus casei
37
-
 in vivo fermentation temperature and assay at Lactobacillus acidophilus
37
-
 in vivo fermentation temperature and assay at Bifidobacterium animalis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.7
-
 in vivo fermentation pH Lacticaseibacillus casei
6.7
-
 in vivo fermentation pH Lactobacillus acidophilus
6.7
-
 in vivo fermentation pH Bifidobacterium animalis
6.8
-
 assay at Lacticaseibacillus casei
6.8
-
 assay at Lactobacillus acidophilus
6.8
-
 assay at Bifidobacterium animalis