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Literature summary extracted from

  • Michlmayr, H.; Schümann, C.; Barreira Braz Da Silva, N.; Kulbe, K.; Del Hierro, A.
    Isolation and basic characterization of a beta-glucosidase from a strain of Lactobacillus brevis isolated from a malolactic starter culture (2010), J. Appl. Microbiol., 108, 550-559.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.2.1.21 ethanol in the presence of 16% (v/v) ethanol the enzyme activity is increased more than 2fold Levilactobacillus brevis
3.2.1.21 methanol in the presence of 16% (v/v) methanol the enzyme activity is increased more than 2fold Levilactobacillus brevis
3.2.1.21 additional information high concentrations (up to 0.2 M) of fructose, malate, lactate, mannitol and sorbitol have little or no effect on the enzyme activity Levilactobacillus brevis

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.21 D-gluconate 17% of initial activity at 0.2 M Levilactobacillus brevis
3.2.1.21 D-gluconic acid delta-lactone 14% of initial activity at 10 mM Levilactobacillus brevis
3.2.1.21 D-glucose 59% of initial activity at 0.2 M Levilactobacillus brevis
3.2.1.21 additional information the enzyme is not inhibited by D-fructose Levilactobacillus brevis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.21 0.22
-
 4-nitrophenyl-beta-D-glucopyranoside in 0.2 mM citrate-phosphate buffer, pH 5.5, at 37°C Levilactobacillus brevis
3.2.1.21 1.14
-
 4-nitrophenyl-beta-D-xylopyranoside in 0.2 mM citrate-phosphate buffer, pH 5.5, at 37°C Levilactobacillus brevis
3.2.1.37 1.14
-
 4-nitrophenyl-beta-D-xylopyranoside pH 5.5, 37°C Levilactobacillus brevis

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.2.1.21 cytoplasm
-
 Levilactobacillus brevis 5737
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.21 80000
-
 4 * 80000, SDS-PAGE Levilactobacillus brevis
3.2.1.21 330000
-
 gel filtration Levilactobacillus brevis
3.2.1.37 80000
-
 4 * 80000, SDS-PAGE Levilactobacillus brevis
3.2.1.37 330000
-
 gel filtration Levilactobacillus brevis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.1.21 additional information Levilactobacillus brevis the pure glucosidase from Lactobacillus brevis has also side activities of xylosidase, arabinosidase, and cellobiosidase ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.21 Levilactobacillus brevis
-
-
-
3.2.1.37 Levilactobacillus brevis
-
 multifunctional enzyme with glucosidase, xylosidase, arabinosidase and cellobiosidase activities
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.21 ammonium sulfate precipitation, Macro-Prep methyl HIC column chromatography, Source 15 Q column chromatography, and Sephacryl S-300 gel filtration Levilactobacillus brevis

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.2.1.21 0.1
-
 after 244fold purification, using 4-nitrophenyl-beta-D-glalactopyranoside substrate, as at 37°C Levilactobacillus brevis
3.2.1.21 0.29
-
 crude extract, using 4-nitrophenyl-beta-D-glucopyranoside substrate, at 37°C Levilactobacillus brevis
3.2.1.21 3.5
-
 after 244fold purification, using 4-nitrophenyl-alpha-L-arabinopyranoside substrate, as at 37°C Levilactobacillus brevis
3.2.1.21 9.4
-
 after 244fold purification, using 4-nitrophenyl-beta-D-cellobioside substrate, as at 37°C Levilactobacillus brevis
3.2.1.21 33
-
 after 244fold purification, using 4-nitrophenyl-beta-D-xylopyranoside substrate, as at 37°C Levilactobacillus brevis
3.2.1.21 70.9
-
 after 244fold purification, using 4-nitrophenyl -beta-D-glucopyranoside substrate, as at 37°C Levilactobacillus brevis

Storage Stability

EC Number Storage Stability Organism
3.2.1.21 4°C, in 20 mM citrate-phosphate buffer, half-lives of 4 days at pH 4.0 and 50 days at pH 7.0 Levilactobacillus brevis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.21 4-nitrophenyl beta-D-cellobioside + H2O 13% activity compared to 4-nitrophenyl beta-D-glucopyranoside Levilactobacillus brevis 4-nitrophenol + cellobiose
-
 ?
3.2.1.21 4-nitrophenyl beta-D-galactopyranoside + H2O 0.1% activity compared to 4-nitrophenyl beta-D-glucopyranoside Levilactobacillus brevis 4-nitrophenol + beta-D-galactose
-
 ?
3.2.1.21 4-nitrophenyl beta-D-glucopyranoside + H2O 100% activity Levilactobacillus brevis 4-nitrophenol + D-glucopyranose
-
 ?
3.2.1.21 4-nitrophenyl beta-D-xylopyranoside + H2O 46% activity compared to 4-nitrophenyl beta-D-glucopyranoside Levilactobacillus brevis 4-nitrophenol + beta-D-xylose
-
 ?
3.2.1.21 4-nitrophenyl-alpha-L-arabinopyranoside + H2O 4.9% activity compared to 4-nitrophenyl beta-D-glucopyranoside Levilactobacillus brevis 4-nitrophenol + alpha-L-arabinopyranose
-
 ?
3.2.1.21 cellobiose + H2O
-
 Levilactobacillus brevis 2 beta-D-glucose
-
 ?
3.2.1.21 additional information the pure glucosidase from Lactobacillus brevis has also side activities of xylosidase, arabinosidase, and cellobiosidase Levilactobacillus brevis ?
-
 ?
3.2.1.21 additional information no hydrolysis of 4-nitrophenyl-alpha-L-arabinopyranoside, 4-nitrophenyl-alpha-L-rhamnopyranoside, 4-nitrophenyl-beta-D-mannopyranoside, 4-nitrophenyl-alpha-D-glucopyranoside, 4-nitrophenyl-alpha-D-xylopyranoside, 4-nitrophenyl-alpha-D-mannopyranoside, and 4-nitrophenyl-alpha-D-galactopyranoside Levilactobacillus brevis ?
-
 ?
3.2.1.37 4-nitrophenyl beta-D-xylopyranoside + H2O 46% of the activity with 4-nitrophenyl-beta-D-glucopyranoside Levilactobacillus brevis 4-nitrophenol + beta-D-xylopyranose
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.21 homotetramer 4 * 80000, SDS-PAGE Levilactobacillus brevis
3.2.1.37 tetramer 4 * 80000, SDS-PAGE Levilactobacillus brevis

Synonyms

EC Number Synonyms Comment Organism
3.2.1.21 beta-D-glucosidase
-
 Levilactobacillus brevis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.21 45
-
-
 Levilactobacillus brevis
3.2.1.37 45
-
 xylosidase activity Levilactobacillus brevis

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.21 25 45 the enzyme displays good stability when it is kept at 25 and 37°C, with approximate half-lives of 160 and 3.5 h, respectively. When the enzyme is kept at 45°C, less than 5% of initial activity is detectable after 30 min Levilactobacillus brevis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.21 5.5
-
-
 Levilactobacillus brevis
3.2.1.37 5.5 6 xylosidase activity Levilactobacillus brevis

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.2.1.21 4 7 the free enzyme is stable at pH 7.0 (half-life of 50 days) but not at pH 4.0 (half-life of 4 days) Levilactobacillus brevis
3.2.1.37 4
-
 half-life 4 days Levilactobacillus brevis
3.2.1.37 7
-
 stable Levilactobacillus brevis

pI Value

EC Number Organism Comment pI Value Maximum pI Value
3.2.1.21 Levilactobacillus brevis isoelectric focusing
-
 3.5
3.2.1.37 Levilactobacillus brevis isoelectric focusing
-
 3.5