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Literature summary for 3.2.1.8 extracted from

  • Liu, J.R.; Duan, C.H.; Zhao, X.; Tzen, J.T.; Cheng, K.J.; Pai, C.K.
    Cloning of a rumen fungal xylanase gene and purification of the recombinant enzyme via artificial oil bodies (2008), Appl. Microbiol. Biotechnol., 79, 225-233.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
additional information in the insoluble fraction of cell lysate or embedding in artificial oil bodies, XynS20-intein M-oleosin does not show any enzymatic activity. After release from artificial oil bodies by inclusion of DTT to induce intein linker self-splicing, XynS20 reveals a xylanase activity band of about 36 kDa Neocallimastix patriciarum

Cloned(Commentary)

Cloned (Comment) Organism
DNA fragments of xynS20 genes subcloned into vector pOSP2. XynS20 expressed as a recombinant protein fused to the N-terminus of oleosin by a linker polypeptide, intein M, in Escherichia coli Neocallimastix patriciarum

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
36000
-
sequence analysis Neocallimastix patriciarum

Organism

Organism UniProt Comment Textmining
Neocallimastix patriciarum A8TGA1
-
-

Purification (Commentary)

Purification (Comment) Organism
affinity-purified by formation of artificial oil bodies Neocallimastix patriciarum

Source Tissue

Source Tissue Comment Organism Textmining

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1983
-
toward oat spelt xylan Neocallimastix patriciarum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information no activity against carboxy methyl cellulose, beta-glucan, lichenan, laminarin, agarose, starch, and kappa-carageenan Neocallimastix patriciarum ?
-
?
oat spelt xylan + H2O
-
Neocallimastix patriciarum ?
-
?

Synonyms

Synonyms Comment Organism
xylanase
-
Neocallimastix patriciarum
XynS20
-
Neocallimastix patriciarum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
45
-
-
Neocallimastix patriciarum

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
30 55 at temperatures below 30°C and above 55°C, enzyme activity is less than 50% of that at the optimal temperature Neocallimastix patriciarum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
-
Neocallimastix patriciarum

pH Range

pH Minimum pH Maximum Comment Organism
5 6
-
Neocallimastix patriciarum

pH Stability

pH Stability pH Stability Maximum Comment Organism
4 7 when pH is below 4.0 or above 7.0, less than 60% of the optimal activity is retained and the enzyme shows no activity at pH 9.0 Neocallimastix patriciarum