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Literature summary extracted from

  • Sakai, K.; Mochizuki, M.; Yamada, M.; Shinzawa, Y.; Minezawa, M.; Kimoto, S.; Murata, S.; Kaneko, Y.; Ishihara, S.; Jindou, S.; Kobayashi, T.; Kato, M.; Shimizu, M.
    Biochemical characterization of thermostable beta-1,4-mannanase belonging to the glycoside hydrolase family 134 from Aspergillus oryzae (2017), Appl. Microbiol. Biotechnol., 101, 3237-3245 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.78 expressed in Pichia pastoris Aspergillus oryzae

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.78 Cu2+ 72% inhibition at 20 mM Aspergillus oryzae
3.2.1.78 ethanol about 60% residual activity at 20% (v/v) Aspergillus oryzae
3.2.1.78 Fe2+ 38% inhibition at 20 mM Aspergillus oryzae
3.2.1.78 Isopropanol about 60% residual activity at 20% (v/v) Aspergillus oryzae
3.2.1.78 methanol about 60% residual activity at 20% (v/v) Aspergillus oryzae
3.2.1.78 additional information EDTA does not affect the activity of the enzyme Aspergillus oryzae
3.2.1.78 SDS about 45% residual activity at 10% (w/v) Aspergillus oryzae
3.2.1.78 TritonX-100 about 40% residual activity at 10% (v/v) Aspergillus oryzae
3.2.1.78 Tween-20 about 50% residual activity at 10% (v/v) Aspergillus oryzae

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.2.1.78 Mn2+ about 2.0fold increase of activity at 20 mM Aspergillus oryzae
3.2.1.78 additional information Co2+, Ni2+, Ca2+, and Mg2+ do not affect the activity of the enzyme Aspergillus oryzae
3.2.1.78 Zn2+ about 1.4fold increase of activity at 20 mM Aspergillus oryzae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.1.78 beta-galactomannan + H2O Aspergillus oryzae the catalytic efficiency of the enzyme is 6.8fold higher toward galactomannan from locust bean gum, than toward galactomannan from guar gum, but similar toward galactomannan from locust bean gum and glucomannan from konjac flour mannobiose + mannotriose + mannotetraose
-
?
3.2.1.78 beta-glucomannan + H2O Aspergillus oryzae the catalytic efficiency of the enzyme is 6.8fold higher toward galactomannan from locust bean gum, than toward galactomannan from guar gum, but similar toward galactomannan from locust bean gum and glucomannan from konjac flour mannobiose + mannotriose + mannotetraose
-
?

Organic Solvent Stability

EC Number Organic Solvent Comment Organism
3.2.1.78 additional information the enzyme activity is unaffected by up to 20% (v/v) acetone Aspergillus oryzae

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.78 Aspergillus oryzae
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.2.1.78 glycoprotein
-
Aspergillus oryzae

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.78 HiTrap Q column chromatography and Superose 6 column chromatography Aspergillus oryzae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.78 beta-galactomannan + H2O the catalytic efficiency of the enzyme is 6.8fold higher toward galactomannan from locust bean gum, than toward galactomannan from guar gum, but similar toward galactomannan from locust bean gum and glucomannan from konjac flour Aspergillus oryzae mannobiose + mannotriose + mannotetraose
-
?
3.2.1.78 beta-glucomannan + H2O the catalytic efficiency of the enzyme is 6.8fold higher toward galactomannan from locust bean gum, than toward galactomannan from guar gum, but similar toward galactomannan from locust bean gum and glucomannan from konjac flour Aspergillus oryzae mannobiose + mannotriose + mannotetraose
-
?
3.2.1.78 guar gum + H2O galactose-mannose ratio of 2:3 Aspergillus oryzae ?
-
?
3.2.1.78 konjac flour + H2O
-
Aspergillus oryzae ?
-
?
3.2.1.78 locust bean gum + H2O galactose-mannose ratio of 1:4 Aspergillus oryzae ?
-
?
3.2.1.78 mannohexaose + H2O
-
Aspergillus oryzae mannobiose + mannotriose + mannotetraose
-
?
3.2.1.78 mannopentaose + H2O
-
Aspergillus oryzae mannobiose + mannotriose
-
?
3.2.1.78 additional information no activity with mannobiose, mannotriose, and mannotetraose Aspergillus oryzae ?
-
?
3.2.1.78 tara gum + H2O galactose-mannose ratio of 1:3 Aspergillus oryzae ?
-
?

Subunits

EC Number Subunits Comment Organism
3.2.1.78 ? x * 19000, SDS-PAGE Aspergillus oryzae

Synonyms

EC Number Synonyms Comment Organism
3.2.1.78 beta-1,4-mannanase
-
Aspergillus oryzae
3.2.1.78 Man134A
-
Aspergillus oryzae

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.78 30
-
-
Aspergillus oryzae

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.78 70 90 after incubation at 70°C for 120 min, the enzyme activity toward glucomannan decreases to 50% of the maximal activity at 30°C. After incubation at 70°C for 120 min, the activity of the enzyme toward glucomannan decreases to 50% of the maximal activity at 30°C. The activity of the enzyme toward mannohexaose decreases to 73% after incubation at 70°C for 60 min. Further increases of temperature to 80 and 90°C for 60 min result in 70 and 26% of the enzyme activity remaining, respectively Aspergillus oryzae

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.2.1.78 290
-
guar gum at pH 6.0 and 30°C Aspergillus oryzae
3.2.1.78 520
-
tara gum at pH 6.0 and 30°C Aspergillus oryzae
3.2.1.78 580
-
locust bean gum at pH 6.0 and 30°C Aspergillus oryzae
3.2.1.78 620
-
konjac flour at pH 6.0 and 30°C Aspergillus oryzae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.78 6
-
-
Aspergillus oryzae

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.2.1.78 5 10 after incubation for 90 min at 30°C at pHs ranging from 5.0 to 10.0, the enzyme retains more than 75% of its maximal activity Aspergillus oryzae