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Information on EC 3.2.1.78 - mannan endo-1,4-beta-mannosidase and Organism(s) Aspergillus aculeatus and UniProt Accession Q00012
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EC Tree
3.2.1.78 mannan endo-1,4-beta-mannosidaseSpecify your search results
Word Map
- 3.2.1.78
- mannans
- galactomannans
- locust
- glucomannans
- guar
- konjac
- mannobiose
- alpha-galactosidase
- reesei
- manno-oligosaccharides
- carob
- radicle
-
micropylar
-
mannan-degrading
-
ivory
-
kraft
- mannotetraose
- beta-mannans
- mannopentaose
-
hemicellulase
-
softwood
-
endohydrolases
- cellulosome
- cellvibrio
- endo-1,4-beta-glucanase
-
copra
-
thermomonospora
-
mannan-binding
- food industry
- agriculture
- synthesis
- pharmacology
- degradation
- biotechnology
- paper production
- nutrition
- medicine
- industry
- drug development
The taxonomic range for the selected organisms is: Aspergillus aculeatus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
Synonyms
beta-mannanase, endo-beta-mannanase, man5a, endo-mannanase, manb-1601, endo-beta-1,4-mannanase, man26a, man26b, man5c, caman, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1,4-beta-D-mannan mannanohydrolase
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beta-1,4-mannan 4-mannanohydrolase
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beta-D-mannanase
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Beta-mannanase
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-
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beta-mannanase B
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endo-1,4-beta-mannanase
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endo-1,4-mannanase
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endo-beta-1,4-mannase
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endo-beta-mannanase
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mannanase, endo-1,4-beta-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
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SYSTEMATIC NAME
IUBMB Comments
4-beta-D-mannan mannanohydrolase
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CAS REGISTRY NUMBER
COMMENTARY
37288-54-3
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
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the enzyme is involved in release of mannooligosaccharides from spent coffee ground cleaving the backbone at random locations in galactomannan, glucomannan, galactoglucomannan and mannan
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
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the enzyme is involved in release of mannooligosaccharides from spent coffee ground cleaving the backbone at random locations in galactomannan, glucomannan, galactoglucomannan and mannan
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-
?
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
recombinant enzyme in Yarrowia lipolytica is produced with an activity of 183.5 U/ml and 0.23 mg protein/ml
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MANA_ASPAC
377
0
41082
Swiss-Prot
Secretory Pathway (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45000
x * 50000, recombinant protein, x * 45000, native protein, SDS-PAGE
50000
x * 50000, recombinant protein, x * 45000, native protein, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 50000, recombinant protein, x * 45000, native protein, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
treatment with PNGaseF results in a shift to 41000 Da, both for native and recombinant protein
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
additional information
-
glycerol at 30-40%, potassium sorbate/sodium benzoate at 0.2%, and sorbitol at 30-35% enhances enzyme thermostability and activity, overview
60
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a combination of mannanase with 0.2% sodium benzoate and 30% or 35% sorbitol presents the highest relative activity of about 150% when incubated at 60°C for 4 h, the control retains 63% of the initial activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant extracellular enzyme from Yarrowia lipolytica culture supernatant by ultrafiltration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene manA, recombinant expression in and secretion from Yarrowia lipolytica
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme production is improved by 150% via supplementation with 0.2% sodium benzoate and 35% sorbitol as a preservative and stabiliser, respectively
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
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production of enzyme by expression in Aspergillus niger under control of the Aspergillus niger glyceraldehyde-3-phosphate dehydrogenase promoter gpdP and the Aspergillus awamori glucoamylase terminator glaAT. The glucose concentration and the organic nitrogen source have an effect on both the volumetric enzyme activity and the specific enzyme activity. The highest mannanase activity levels of 16596 nkat ml-1 and 574 nkat mg-1 dcw are obtained for Aspergillus niger when cultivated in a process-viable medium containing corn steep liquor as the organic nitrogen source and high glucose concentrations
synthesis
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expression in Yarrowia lipolytica using beta-mannosidase's own secretion signal. Fed batch fermentations result in a 3.9fold increase in volumetric enzyme activity compared with batch fermentation, and a maximum titre of 26,139 nkat/ml
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Christgau, S.; Kauppinen, S.; Vind, J.; Kofod, L.V.; Dalboge, H.
Expression cloning, purification and characterization of a beta-1,4-mannanase from Aspergillus aculeatus
Biochem. Mol. Biol. Int.
33
917-925
1994
Aspergillus aculeatus
Setati, M.E.; Ademark, P.; van Zyl, W.H.; Hahn-Hagerdal, B.; Stalbrand, H.
Expression of the Aspergillus aculeatus endo-beta-1,4-mannanase encoding gene (man1) in Saccharomyces cerevisiae and characterization of the recombinant enzyme
Protein Expr. Purif.
21
105-114
2001
Aspergillus aculeatus (Q00012), Aspergillus aculeatus, Aspergillus aculeatus MRC 11624 (Q00012)
van Zyl, P.J.; Moodley, V.; Rose, S.H.; Roth, R.L.; van Zyl, W.H.
Production of the Aspergillus aculeatus endo-1,4-beta-mannanase in A. niger
J. Ind. Microbiol. Biotechnol.
36
611-617
2009
Aspergillus aculeatus, Aspergillus aculeatus MRC11624
Roth, R.; Moodley, V.; van Zyl, P.
Heterologous expression and optimized production of an Aspergillus aculeatus endo-1,4-beta-mannanase in Yarrowia lipolytica
Mol. Biotechnol.
43
112-120
2009
Aspergillus aculeatus
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