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Literature summary for 3.2.1.73 extracted from

  • Mao, S.; Lu, Z.; Zhang, C.; Lu, F.; Bie, X.
    Purification, characterization, and heterologous expression of a thermostable beta-1,3-1,4-glucanase from Bacillus altitudinis YC-9 (2013), Appl. Biochem. Biotechnol., 169, 960-975.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
DNA and amino acid sequence determination and analysis, sequence comparisons, and phylogenetic analysis. Recombinant expression of the enzyme fused to the Trx-tag/His-tag/S-tag sequences in Escherichia coli strain BL21 (DE3), the enzyme is located in the cell lysate and the cell culture supernatant Bacillus altitudinis

Inhibitors

Inhibitors Comment Organism Structure
Cu2+
-
Bacillus altitudinis
EDTA
-
Bacillus altitudinis
Mn2+
-
Bacillus altitudinis
Zn2+ slightly inhibitory Bacillus altitudinis

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ activates slightly Bacillus altitudinis
Co2+ activates Bacillus altitudinis
Fe2+ activates Bacillus altitudinis
additional information no or poor effects by K+, Na+, and Mg2+ Bacillus altitudinis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
27470
-
x * 27470, sequence calculation. x * 45000, recombinant tagged enzyme, SDS-PAGE Bacillus altitudinis
45000
-
x * 27470, sequence calculation. x * 45000, recombinant tagged enzyme, SDS-PAGE Bacillus altitudinis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
lichenan + H2O Bacillus altitudinis
-
?
-
?
lichenan + H2O Bacillus altitudinis YC-9
-
?
-
?
additional information Bacillus altitudinis beta-1,3-1,4-glucanase strictly hydrolyzes beta-1,4-glycosidic linkage adjacent to a 3-O-substituted glucose residue in mixed linked beta-glucans but cannot act on beta-1,4-glucans ?
-
?
additional information Bacillus altitudinis YC-9 beta-1,3-1,4-glucanase strictly hydrolyzes beta-1,4-glycosidic linkage adjacent to a 3-O-substituted glucose residue in mixed linked beta-glucans but cannot act on beta-1,4-glucans ?
-
?

Organism

Organism UniProt Comment Textmining
Bacillus altitudinis K7XFI7 isolated from spring silt
-
Bacillus altitudinis YC-9 K7XFI7 isolated from spring silt
-

Purification (Commentary)

Purification (Comment) Organism
native enzyme 37fold from strain YC-9 by ammonium sulfate precipitation, anion exchange chromatography, and gel filtration, recombinant enzyme from Escherichia coli strain BL21 (DE3) cell culture supernatant by ammonium sulfate precipitation, anion exchange chromatography, and gel filtration Bacillus altitudinis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2373
-
purified native enzyme, pH 6.0, 65°C Bacillus altitudinis
5393
-
purified recombinant enzyme, pH 6.0, 65°C Bacillus altitudinis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
lichenan + H2O
-
Bacillus altitudinis ?
-
?
lichenan + H2O
-
Bacillus altitudinis YC-9 ?
-
?
additional information beta-1,3-1,4-glucanase strictly hydrolyzes beta-1,4-glycosidic linkage adjacent to a 3-O-substituted glucose residue in mixed linked beta-glucans but cannot act on beta-1,4-glucans Bacillus altitudinis ?
-
?
additional information native and recombinant enzymes are both inactive on laminarin, cellulose, xylan, or mannan Bacillus altitudinis ?
-
?
additional information beta-1,3-1,4-glucanase strictly hydrolyzes beta-1,4-glycosidic linkage adjacent to a 3-O-substituted glucose residue in mixed linked beta-glucans but cannot act on beta-1,4-glucans Bacillus altitudinis YC-9 ?
-
?
additional information native and recombinant enzymes are both inactive on laminarin, cellulose, xylan, or mannan Bacillus altitudinis YC-9 ?
-
?

Subunits

Subunits Comment Organism
? x * 27470, sequence calculation. x * 45000, recombinant tagged enzyme, SDS-PAGE Bacillus altitudinis

Synonyms

Synonyms Comment Organism
beta-1,3-1,4-glucanase
-
Bacillus altitudinis
Lichenase
-
Bacillus altitudinis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
65
-
native and recombinant enzyme Bacillus altitudinis

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
40 80 activity profile, overview Bacillus altitudinis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
60
-
purified recombinant enzyme, retains more than 90% activity after 2 h Bacillus altitudinis
70
-
purified recombinant enzyme, retains more 75% activity after 10 min Bacillus altitudinis
80
-
purified recombinant enzyme, retains more 44% activity after 10 min Bacillus altitudinis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
recombinant enzyme Bacillus altitudinis