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Literature summary extracted from

  • Li, N.; Yang, P.; Wang, Y.; Luo, H.; Meng, K.; Wu, N.; Fan, Y.; Yao, B.
    Cloning, expression, and characterization of protease-resistant xylanase from Streptomyces fradiae var. k11 (2008), J. Microbiol. Biotechnol., 18, 410-416.
    View publication on PubMed

Application

EC Number Application Comment Organism
3.2.1.8 industry Xyn10 can be an important candidate for protease-resistant mechanistic research and has potential applications in the food industry, cotton scouring, and improving animal nutrition Streptomyces fradiae

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.8 into vector pET-22b(+) and expressed in Escherichia coli BL21 (DE3) Streptomyces fradiae

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.8 Hg2+ completely inhibits Streptomyces fradiae
3.2.1.8 additional information shows resistance to neutral and alkaline proteases, enzyme activity is unchanged after incubation for 2 h with trypsin, chymotrypsin, collagenase, subtilisin A, proteinase K, and proleather, and retains over 60% of its activity following treatment with high concentrations of an alkaline protease from Bacillus pumilus Streptomyces fradiae
3.2.1.8 SDS strongly inhibits by 94.4% Streptomyces fradiae

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.2.1.8 Fe2+ enhances activity by 61.9% Streptomyces fradiae

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.8 47000
-
 1 * 47000, SDS-PAGE Streptomyces fradiae

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.8 Streptomyces fradiae A7TVD4 var. K11
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.8 to homogeneity by acetone precipitation and anion-exchange chromatography, 6.7fold with a final activity yield of 12.7% Streptomyces fradiae

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.2.1.8 45.7
-
 culture supernatant Streptomyces fradiae
3.2.1.8 304.2
-
 6.7fold purified enzyme Streptomyces fradiae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.8 birchwood xylan + H2O
-
 Streptomyces fradiae ?
-
 ?
3.2.1.8 oat spelt xylan + H2O
-
 Streptomyces fradiae ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.8 monomer 1 * 47000, SDS-PAGE Streptomyces fradiae

Synonyms

EC Number Synonyms Comment Organism
3.2.1.8 xylanase
-
 Streptomyces fradiae
3.2.1.8 Xyn10
-
 Streptomyces fradiae

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.8 60
-
 at pH 7.8 Streptomyces fradiae

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.8 50 60 remains stable at 50°C after incubation for 30 min at pH 7.8. More than 40% of the activity is retained after treating the enzyme at 60°C for 5 min Streptomyces fradiae

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.2.1.8 103.4
-
 birchwood xylan
-
 Streptomyces fradiae
3.2.1.8 170.8
-
 oat spelt xylan
-
 Streptomyces fradiae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.8 7.8
-
 at 50°C Streptomyces fradiae

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.2.1.8 6.5 8.5 over 80% of the peak activity Streptomyces fradiae

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.2.1.8 4 10 after incubation at 37°C for 1 h Streptomyces fradiae