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Literature summary for 3.2.1.73 extracted from

  • Sun, J.; Wang, H.; Lv, W.; Ma, C.; Lou, Z.; Dai, Y.
    Construction and characterization of a fusion beta-1,3-1,4-glucanase to improve hydrolytic activity and thermostability (2011), Biotechnol. Lett., 33, 2193-2199.
    View publication on PubMed

Application

Application Comment Organism
synthesis construction of a fusion gene, encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, via end-to-end fusion and expression in Escherichia coli. The catalytic efficiency of the fusion enzyme for oat beta-glucan is 2.7- and 20fold higher than that of the parental Bacillus amyloliquefaciens and Clostridium thermocellum enzymes, respectively, and the fusion enzyme can retain more than 50% of activity following incubation at 80°C for 30 min, whereas the residual activities of Bacillus amyloliquefaciens and Clostridium thermocellum enzymes are both less than 30% Bacillus amyloliquefaciens
synthesis construction of a fusion gene, encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, via end-to-end fusion and expression in Escherichia coli. The catalytic efficiency of the fusion enzyme for oat beta-glucan is 2.7- and 20fold higher than that of the parental Bacillus amyloliquefaciens and Clostridium thermocellum enzymes, respectively, and the fusion enzyme can retain more than 50% of activity following incubation at 80°C for 30 min, whereas the residual activities of Bacillus amyloliquefaciens and Clostridium thermocellum enzymes are both less than 30% Acetivibrio thermocellus

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Bacillus amyloliquefaciens
expression in Escherichia coli Acetivibrio thermocellus

Protein Variants

Protein Variants Comment Organism
additional information construction of a fusion gene, encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, via end-to-end fusion and expression in Escherichia coli. The catalytic efficiency of the fusion enzyme for oat beta-glucan is 2.7- and 20fold higher than that of the parental Bacillus amyloliquefaciens and Clostridium thermocellum enzymes, respectively, and the fusion enzyme can retain more than 50% of activity following incubation at 80°C for 30 min, whereas the residual activities of Bacillus amyloliquefaciens and Clostridium thermocellum enzymes are both less than 30% Bacillus amyloliquefaciens
additional information construction of a fusion gene, encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, via end-to-end fusion and expression in Escherichia coli. The catalytic efficiency of the fusion enzyme for oat beta-glucan is 2.7- and 20fold higher than that of the parental Bacillus amyloliquefaciens and Clostridium thermocellum enzymes, respectively, and the fusion enzyme can retain more than 50% of activity following incubation at 80°C for 30 min, whereas the residual activities of Bacillus amyloliquefaciens and Clostridium thermocellum enzymes are both less than 30% Acetivibrio thermocellus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information KM value for native enzyme, substrate beta-D-glucan, is 1.5 mg/ml, for fusion protein encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, substrate beta-D-glucan, is 1.2 mg/ml Bacillus amyloliquefaciens
additional information
-
additional information KM value for native enzyme, substrate beta-D-glucan, is 2.7 mg/ml, for fusion protein encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, substrate beta-D-glucan, 1.2 mg/ml Acetivibrio thermocellus

Organism

Organism UniProt Comment Textmining
Acetivibrio thermocellus Q84C00
-
-
Bacillus amyloliquefaciens Q84F88
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
192
-
native enzyme, substrate lichenan, pH 6.0, 70°C Acetivibrio thermocellus
275
-
native enzyme, substrate beta-D-glucan, pH 6.0, 70°C Acetivibrio thermocellus
851
-
native enzyme, substrate lichenan, pH 6.0, 50°C Bacillus amyloliquefaciens
1106
-
native enzyme, substrate beta-D-glucan, pH 6.0, 50°C Bacillus amyloliquefaciens
1746
-
fusion protein encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, substrate lichenan, pH 6.0, 70°C Bacillus amyloliquefaciens
1746
-
fusion protein encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, substrate lichenan, pH 6.0, 70°C Acetivibrio thermocellus
2434
-
fusion protein encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, substrate beta-D-glucan, pH 6.0, 70°C Bacillus amyloliquefaciens
2434
-
fusion protein encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, substrate beta-D-glucan, pH 6.0, 70°C Acetivibrio thermocellus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
beta-D-glucan + H2O source of substrate: oat Bacillus amyloliquefaciens ?
-
?
beta-D-glucan + H2O source of substrate: oat Acetivibrio thermocellus ?
-
?
lichenan + H2O
-
Bacillus amyloliquefaciens ?
-
?
lichenan + H2O
-
Acetivibrio thermocellus ?
-
?
additional information no substrate: carboxymethyl cellulose, xylan from birch, soluble starch Bacillus amyloliquefaciens ?
-
?
additional information no substrate: carboxymethyl cellulose, xylan from birch, soluble starch Acetivibrio thermocellus ?
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.3
-
Beta-D-glucan native enzyme, pH 6.0, 70°C Acetivibrio thermocellus
9.2
-
Beta-D-glucan native enzyme, pH 6.0, 50°C Bacillus amyloliquefaciens
20.3
-
Beta-D-glucan fusion protein encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, pH 6.0, 70°C Bacillus amyloliquefaciens
20.3
-
Beta-D-glucan fusion protein encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, pH 6.0, 70°C Acetivibrio thermocellus

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
additional information
-
additional information Kcat/KM value for native enzyme, substrate beta-D-glucan, is 369 mg/ml/min, for fusion protein encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, substrate beta-D-glucan, is 1014 mg/ml/min Bacillus amyloliquefaciens
additional information
-
additional information kcat/KM value for native enzyme, substrate beta-D-glucan, is 51 ml/mg/min, for fusion protein encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, substrate beta-D-glucan, 1014 ml/mg/min Acetivibrio thermocellus