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Literature summary for 3.2.1.78 extracted from

  • Yang, H.; Shi, P.; Lu, H.; Wang, H.; Luo, H.; Huang, H.; Yang, P.; Yao, B.
    A thermophilic beta-mannanase from Neosartorya fischeri P1 with broad pH stability and significant hydrolysis ability of various mannan polymers (2015), Food Chem., 173, 283-289.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
2-mercaptoethanol
-
Aspergillus fischeri

Cloned(Commentary)

Cloned (Comment) Organism
gene man5P1, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of extracellular enzyme in Pichia pastoris strain GS115 Aspergillus fischeri

Inhibitors

Inhibitors Comment Organism Structure
Ag+
-
Aspergillus fischeri
Co2+
-
Aspergillus fischeri
Cu2+
-
Aspergillus fischeri
EDTA
-
Aspergillus fischeri
Fe3+
-
Aspergillus fischeri
K+
-
Aspergillus fischeri
Li+
-
Aspergillus fischeri
Mg2+
-
Aspergillus fischeri
additional information the purified recombinant enzyme has a strong resistance to SDS and Ag+ and proteases pepsin and trypsin Aspergillus fischeri
Ni2+
-
Aspergillus fischeri
SDS
-
Aspergillus fischeri
Zn2+
-
Aspergillus fischeri

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information recombinant enzyme, Km for locust bean gum is 0.83 ± 0.2 mg/ml, pH 4.0, 80°C Aspergillus fischeri

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular the enzyme contains a putative 19-residue signal peptide at the N-terminus Aspergillus fischeri
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
additional information poor effects by Na+, Ca2+, and Mn2+ Aspergillus fischeri

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
39500
-
x * 39500, about, sequence calculation, x * 43000, recombinant glycosylated enzyme, SDS-PAGE, x * 40000, recombinant deglycosylated enzyme, SDS-PAGE Aspergillus fischeri
40000
-
x * 39500, about, sequence calculation, x * 43000, recombinant glycosylated enzyme, SDS-PAGE, x * 40000, recombinant deglycosylated enzyme, SDS-PAGE Aspergillus fischeri
43000
-
x * 39500, about, sequence calculation, x * 43000, recombinant glycosylated enzyme, SDS-PAGE, x * 40000, recombinant deglycosylated enzyme, SDS-PAGE Aspergillus fischeri

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Aspergillus fischeri the enzyme is highly active towards galactomannan and glucomannan, and exhibits classic endo-activity producing a mixture of mannooligosaccharides ?
-
?
additional information Aspergillus fischeri P1 the enzyme is highly active towards galactomannan and glucomannan, and exhibits classic endo-activity producing a mixture of mannooligosaccharides ?
-
?

Organism

Organism UniProt Comment Textmining
Aspergillus fischeri
-
gene man5P1
-
Aspergillus fischeri P1
-
gene man5P1
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein the enzyme contains two putative N-glycosylation sites and no O-glycosylation site, deglycosylation by endo-beta-N-acetylglucosaminidase H Aspergillus fischeri

Purification (Commentary)

Purification (Comment) Organism
recombinant extracellular enzyme from Pichia pastoris strain GS115 culture supernatant by ultrafiltration and anion exchange chromatography Aspergillus fischeri

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1703
-
purified recombinant enzyme, substrate locust bean gum, pH 4.0, 80°C Aspergillus fischeri

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
galactomannan + H2O different contents of glucose and mannose, overview Aspergillus fischeri mannose + mannobiose + mannotriose + mannotetraose + galactose-linked mannotetraose + mannopentaose + mannohexaose product ratio overview ?
guar gum + H2O
-
Aspergillus fischeri mannose + mannobiose + mannotriose + mannotetraose + galactose-linked mannotetraose + mannopentaose + mannohexaose product ratio overview ?
locust bean gum + H2O
-
Aspergillus fischeri mannose + mannobiose + mannotriose + mannotetraose + galactose-linked mannotetraose + mannopentaose + mannohexaose product ratio overview ?
mannohexaose + H2O
-
Aspergillus fischeri ?
-
?
mannopentaose + H2O
-
Aspergillus fischeri ?
-
?
mannopentaose + H2O
-
Aspergillus fischeri P1 ?
-
?
mannotetraose + H2O
-
Aspergillus fischeri ?
-
?
mannotetraose + H2O
-
Aspergillus fischeri P1 ?
-
?
mannotriose + H2O
-
Aspergillus fischeri ?
-
?
mannotriose + H2O
-
Aspergillus fischeri P1 ?
-
?
additional information the enzyme is highly active towards galactomannan and glucomannan, and exhibits classic endo-activity producing a mixture of mannooligosaccharides Aspergillus fischeri ?
-
?
additional information the enzyme has no exo-activity and is a typical endo-acting beta-mannanase, substrate specificity, overview. No activity with mannobiose, beechwood xylan, barley beta-glucan, 4-nitrophenyl beta-D-mannoside, and carboxymethyl cellulose Aspergillus fischeri ?
-
?
additional information the enzyme is highly active towards galactomannan and glucomannan, and exhibits classic endo-activity producing a mixture of mannooligosaccharides Aspergillus fischeri P1 ?
-
?
additional information the enzyme has no exo-activity and is a typical endo-acting beta-mannanase, substrate specificity, overview. No activity with mannobiose, beechwood xylan, barley beta-glucan, 4-nitrophenyl beta-D-mannoside, and carboxymethyl cellulose Aspergillus fischeri P1 ?
-
?

Subunits

Subunits Comment Organism
? x * 39500, about, sequence calculation, x * 43000, recombinant glycosylated enzyme, SDS-PAGE, x * 40000, recombinant deglycosylated enzyme, SDS-PAGE Aspergillus fischeri

Synonyms

Synonyms Comment Organism
Beta-mannanase
-
Aspergillus fischeri
Man5P1
-
Aspergillus fischeri

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
80
-
recombinant enzyme Aspergillus fischeri

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
40 90 recombinant enzyme, over 20% of maximal activity within this range Aspergillus fischeri

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
the glycosylation status of the enzyme has no effect on the thermostability Aspergillus fischeri
60
-
purified recombinant enzyme, 6 h, over 80% activity remaining Aspergillus fischeri
70
-
purified recombinant enzyme, 80% activity remaining after 1 h, inactivation after 2 h Aspergillus fischeri

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
4
-
recombinant enzyme Aspergillus fischeri

pH Range

pH Minimum pH Maximum Comment Organism
2 9 recombinant enzyme, over 20% of maximal activity at pH 2.0 and pH 9.0 Aspergillus fischeri

pH Stability

pH Stability pH Stability Maximum Comment Organism
2 12 purified recombinant enzyme, 1 h, over 65% activity remaining Aspergillus fischeri

pI Value

Organism Comment pI Value Maximum pI Value
Aspergillus fischeri sequence calculation
-
5.93

General Information

General Information Comment Organism
evolution the enzyme belongs to the glycosyl hydrolase family 5, GH5 Aspergillus fischeri