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Literature summary for 3.2.1.4 extracted from

  • Lin, L.; Meng, X.; Liu, P.; Hong, Y.; Wu, G.; Huang, X.; Li, C.; Dong, J.; Xiao, L.; Liu, Z.
    Improved catalytic efficiency of endo-beta-1,4-glucanase from Bacillus subtilis BME-15 by directed evolution (2009), Appl. Microbiol. Biotechnol., 82, 671-679.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Bacillus subtilis

Protein Variants

Protein Variants Comment Organism
I62T/L79I/A93T/S308P/I370V/L374P/M416V/F472I/I484V/W494R S40 mutant, DNA shuffling. Higher hydrolytic activities than the wild-type enzyme Bacillus subtilis
K120E/D272H/S283G/S308P/L374P M1-23 mutant, random mutation. Higher hydrolytic activities than the wild-type enzyme Bacillus subtilis
K120E/S283G/S308P/L374P M1 mutant, random mutation. Higher hydrolytic activities than the wild-type enzyme, shows 1.25fold increase in activity Bacillus subtilis
additional information variants (M44-11, S75 and S78) show 2.03fold to 2.68fold increased activities toward sodium carboxymethyl cellulose Bacillus subtilis
N39D/K120E/N175H/V255A/S308P/L386S/K398R S75 mutant, DNA shuffling. Higher hydrolytic activities than the wild-type enzyme Bacillus subtilis
T32I/N39D/K120E/S248G/S283G/S308P/R314G/I370N/L374P/N403D/N451D/S467N S78 mutant, DNA shuffling. Higher hydrolytic activities than the wild-type enzyme Bacillus subtilis
V74A/K120E/D272G/K337E/S355P/D459G/K479E/K482E/K491N M44 mutant, random mutation. Higher hydrolytic activities than the wild-type enzyme, shows 1.56fold increase in activity Bacillus subtilis
V74A/K120E/D272G/K337E/S355P/T449I/D459G/K479E/K482E/D488N/K491N M44-11 mutant, random mutation. Higher hydrolytic activities than the wild-type enzyme Bacillus subtilis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
52170
-
-
Bacillus subtilis

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
BME-15
-
Bacillus subtilis BME-15
-
BME-15
-

Purification (Commentary)

Purification (Comment) Organism
-
Bacillus subtilis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.91
-
Cel5A, carboxymethyl cellulose as substrate Bacillus subtilis
3.88
-
M44-11 mutant, carboxymethyl cellulose as substrate Bacillus subtilis
4.84
-
S75 mutant, carboxymethyl cellulose as substrate Bacillus subtilis
4.88
-
S78 mutant, carboxymethyl cellulose as substrate Bacillus subtilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
barley glucan + H2O
-
Bacillus subtilis ?
-
?
barley glucan + H2O
-
Bacillus subtilis BME-15 ?
-
?
carboxymethylcellulose + H2O
-
Bacillus subtilis ?
-
?
carboxymethylcellulose + H2O
-
Bacillus subtilis BME-15 ?
-
?
cellulose + H2O
-
Bacillus subtilis ?
-
?
cellulose + H2O
-
Bacillus subtilis BME-15 ?
-
?
sodium carboxymethyl cellulose + H2O
-
Bacillus subtilis ?
-
?
sodium carboxymethyl cellulose + H2O
-
Bacillus subtilis BME-15 ?
-
?

Synonyms

Synonyms Comment Organism
Cel5A
-
Bacillus subtilis
Cellulase
-
Bacillus subtilis
endo-beta-1,4-glucanase
-
Bacillus subtilis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
40
-
S75 mutant Bacillus subtilis
50
-
Cel5A wild-type and M44-11 mutant Bacillus subtilis
60
-
S78 mutant Bacillus subtilis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
80
-
M44-11 mutant shows higher stability than others and retains more than 50% of its activity after incubation at 80°C for 1 h Bacillus subtilis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5
-
for mutants M44-11, S75, and S78 Bacillus subtilis