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Literature summary for 3.2.1.6 extracted from

  • Na, H.B.; Jung, W.K.; Jeong, Y.S.; Kim, H.J.; Kim, S.K.; Kim, J.; Yun, H.D.; Lee, J.K.; Kim, H.
    Characterization of a GH family 8 beta-1,3-1,4-glucanase with distinctive broad substrate specificity from Paenibacillus sp. X4 (2015), Biotechnol. Lett., 37, 643-655.
    View publication on PubMed
Search for more literature for 3.2.1.6

Cloned(Commentary)

Cloned (Comment) Organism
gene bglc8H, DNA and amino acid sequence determination and analysis, phylogenetic tree, cloning in Escherichia coli strain DH5alpha Paenibacillus sp.

Protein Variants

Protein Variants Comment Organism
D156A site-directed mutagenesis, the mutant shows a nearly complete loss of enzyme activity Paenibacillus sp.
E95A site-directed mutagenesis, the mutant shows a nearly complete loss of enzyme activity Paenibacillus sp.

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ activates, 5 mM Ca2+ increases the lichenase activity by 15%. Ca2+ increases the heat stability of the lichenase activity Paenibacillus sp.

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
40000
-
 x * 41561, sequence calculation, x * 40000, SDS-PAGE Paenibacillus sp.
41561
-
 x * 41561, sequence calculation, x * 40000, SDS-PAGE Paenibacillus sp.

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Paenibacillus sp. the enzyme has a broad substrate specificity and hydrolyzes barley-beta-D-glucan before chitosan, carboxymethyl-cellulose, and lichenan ?
-
 ?

Organism

Organism UniProt Comment Textmining
Paenibacillus sp. A0A088BCU2 clone HB 2-4, gene bglc8H or lic8H
-

Purification (Commentary)

Purification (Comment) Organism
native enzyme 10.1fold by anion exchange and hydroxyapatite chromatography Paenibacillus sp.

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.22
-
 purified native enzyme, pH 5.0, 50°C Paenibacillus sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
chitosan + H2O
-
 Paenibacillus sp. ?
-
 ?
laminarin + H2O
-
 Paenibacillus sp. ?
-
 ?
lichenan + H2O
-
 Paenibacillus sp. ?
-
 ?
additional information the enzyme has a broad substrate specificity and hydrolyzes barley-beta-D-glucan before chitosan, carboxymethyl-cellulose, and lichenan Paenibacillus sp. ?
-
 ?
additional information the enzyme hydrolyzes cello-oligosaccharides (G3-G6) to cellotriose and cellobiose but not to D-glucose. Barley beta-glucan and lichenan are hydrolyzed by the enzyme to cellotetraose as the major product Paenibacillus sp. ?
-
 ?

Subunits

Subunits Comment Organism
? x * 41561, sequence calculation, x * 40000, SDS-PAGE Paenibacillus sp.

Synonyms

Synonyms Comment Organism
barley-beta-D-glucanase
-
 Paenibacillus sp.
beta-1,3-1,4-glucanase
-
 Paenibacillus sp.
chitosanase
-
 Paenibacillus sp.
CMCase
-
 Paenibacillus sp.
laminarinase
-
 Paenibacillus sp.
Lic8H
-
 Paenibacillus sp.
Lichenase
-
 Paenibacillus sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50
-
 except for barley-beta-D-glucanase activity with an optimum at 40°C Paenibacillus sp.

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
 Ca2+ increases the heat stability of the lichenase activity retaining 59% activity in the presence of Ca2+ after 15 min of heat treatment at 70°C, compared to 34% in the absence of Ca2+. Ca2+ also increases the heat stability of the beta-glucanase activity (from 18 to 28%). No significant influence of Ca2+ on the heat stability of the chitosanase and CMCase activities are observed Paenibacillus sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5
-
 except for chitosanase activity with an optimum at pH 7.0 Paenibacillus sp.

pI Value

Organism Comment pI Value Maximum pI Value
Paenibacillus sp. sequence calculation
-
 7.61

General Information

General Information Comment Organism
evolution the enzyme belongs to glycoside hydrolase family 8 (GH8) and contains A154TDGDMDIAYSLLLADKQW172. The enzyme has a lower ratio of lichenase/barley-beta-D-glucanase activities compared to glycoside hydrolase family GH16 enzymes Paenibacillus sp.
additional information Glu95 and Asp156 are catalytically active residues Paenibacillus sp.