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Literature summary for 3.2.1.8 extracted from

  • Bibi, Z.; Qader, S.A.; Aman, A.
    Calcium alginate matrix increases the stability and recycling capability of immobilized endo-beta-1,4-xylanase from Geobacillus stearothermophilus KIBGE-IB29 (2015), Extremophiles, 19, 819-827.
    View publication on PubMed

Application

Application Comment Organism
degradation immobilization of enzyme within calcium alginate beads using entrapment technique. Temperature (50°C) and pH (7.0) optima of immobilized enzyme remain same, but enzyme-substrate reaction time increases from 5.0 to 30.0 min as compared to free enzyme. The diffusion limit of high molecular weight xylan (corncob) causes a decline in Vmax of immobilized enzyme from 4773 to 203.7 U/min, whereas the Km value increases from 0.5074 to 0.5722 mg/ml. Immobilized endo-beta-1,4-xylanase is stable even at high temperatures and retains 18 and 9% residual activity at 70°C and 80°C, respectively. The immobilized enzyme also exhibits sufficient recycling efficiency up to five reaction cycles Geobacillus stearothermophilus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
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corncob xylan Km value of free enzyme is 0.507 mg/ml, of immobilized enzyme 0.572 mg/ml, pH 7.0, 50°C Geobacillus stearothermophilus

Organism

Organism UniProt Comment Textmining
Geobacillus stearothermophilus
-
-
-
Geobacillus stearothermophilus KIBGE-IB29
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
corncob xylan + H2O
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Geobacillus stearothermophilus xylo-oligosaccharides + ?
-
?
corncob xylan + H2O
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Geobacillus stearothermophilus KIBGE-IB29 xylo-oligosaccharides + ?
-
?

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
70
-
18% of maximum activity Geobacillus stearothermophilus
80
-
9% of maximum activity Geobacillus stearothermophilus