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Literature summary for 3.2.1.8 extracted from

  • Sa-Pereira, P.; Carvalho, A.S.L.; Costa-Ferreira, M.; Aires-Barros, M.R.
    Thermostabilization of Bacillus subtilis CCMI 966 xylanases with trehalose. Study of deactivation kinetics (2004), Enzyme Microb. Technol., 34, 278-282.
No PubMed abstract available

Activating Compound

Activating Compound Comment Organism Structure
trehalose activates both isozymes and stabilizes them at higher temperatures Bacillus subtilis

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
2 isozymes: alkaline XylI and neutral XylII
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Bacillus subtilis CCMI 966
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2 isozymes: alkaline XylI and neutral XylII
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Synonyms

Synonyms Comment Organism
xylanase
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Bacillus subtilis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
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trehalose stabilizes both isozymes at 60°C and 70°C and increases the enzyme activity, thermal deactivation kinetics of enzyme forms XylI and XylII Bacillus subtilis
60
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50% final residual activity in presence of 0.5 M trehalose as well as 8fold increased half-life of XylII and 2.5fold of XylI, inactivation in absence of trehalose Bacillus subtilis
70
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35% final residual activity in presence of 0.5 M trehalose as well as 2fold increased half-lives of XylII and XylI, inactivation in absence of trehalose Bacillus subtilis

pI Value

Organism Comment pI Value Maximum pI Value
Bacillus subtilis alkaline isozyme XylI 4.7 4.6
Bacillus subtilis neutral isozyme XylII
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7.5