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Literature summary for 3.2.1.4 extracted from

  • Wang, C.; Hsieh, Y.; Ng, C.; Chan, H.; Lin, H.; Tzeng, W.; Shyu, Y.
    Purification and characterization of a novel halostable cellulase from Salinivibrio sp. strain NTU-05 (2009), Enzyme Microb. Technol., 44, 373-379.
No PubMed abstract available
Search for more literature for 3.2.1.4

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information kinetics, native enzyme Salinivibrio sp. NTU-05

Localization

Localization Comment Organism GeneOntology No. Textmining
cellulosome
-
 Salinivibrio sp. NTU-05 43263
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ activates Salinivibrio sp. NTU-05
Cu2+ activates Salinivibrio sp. NTU-05
Fe3+ activates Salinivibrio sp. NTU-05
Hg2+ activates Salinivibrio sp. NTU-05
K+ activates Salinivibrio sp. NTU-05
Mg2+ activates Salinivibrio sp. NTU-05
Mn2+ activates Salinivibrio sp. NTU-05
Na+ activate sat 0-20% v/w, optimally at 5% v/w Salinivibrio sp. NTU-05
Zn2+ activates Salinivibrio sp. NTU-05

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
29000
-
 gel filtration Salinivibrio sp. NTU-05

Organism

Organism UniProt Comment Textmining
Salinivibrio sp. NTU-05
-
-
-

Purification (Commentary)

Purification (Comment) Organism
native enzyme 29.5fold by anion exchange chromatography and gel filtration Salinivibrio sp. NTU-05

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
32.4
-
 purified native enzyme Salinivibrio sp. NTU-05

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information carboxymethyl cellulose and beta-glucan are the best substrates with relative activities of 100% and 83%, respectively, birch wood xylan and oat spelt xylan have moderate activities of 68% and 60%, respectively, which otherwise supports low level of cellulase activity, Avicel has the lowest activity of 12%, substrate specificity, overview Salinivibrio sp. NTU-05 ?
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 29000, SDS-PAGE Salinivibrio sp. NTU-05

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
35
-
-
 Salinivibrio sp. NTU-05

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
10 60 activity range, profile, overview Salinivibrio sp. NTU-05

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
10 70 purified native enzyme, highly stable in the temperature range of 10-40°C, the activity declines rapidly as the temperature increases above 60°C, 12% activity remains at 70°C after 4 h. At 10°C, the enzyme exhibits no loss of activity, even after 24 h Salinivibrio sp. NTU-05

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
-
 Salinivibrio sp. NTU-05

pH Range

pH Minimum pH Maximum Comment Organism
5 9 activity range, 80% of maximal activity at pH 6.5 and pH 8.5, profile, overview Salinivibrio sp. NTU-05

pH Stability

pH Stability pH Stability Maximum Comment Organism
5 8 the purified native enzyme retains 100% of its activity at pH 7.0 and pH 8.0 for 24 h, but only 35% at pH 5.0 Salinivibrio sp. NTU-05