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Literature summary for 3.2.1.32 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
Search for more literature for 3.2.1.32

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
 Bacillus subtilis
-
-

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
 CCMI 966, enzymes alkaline Xyl I, neutral Xyl II
-

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
60
-
 Xyl I, 3 h, 20% of initial activity Bacillus subtilis
60
-
 Xyl I, 3 h, presence of 0.5 M trehalose, 50% of initial activity Bacillus subtilis
60
-
 Xyl II, 3 h, complete inactivation Bacillus subtilis
60
-
 Xyl II, 3 h, presence of 0.5 M trehalose, 50% of initial activity Bacillus subtilis
70
-
 Xyl I, 3 h, no activity Bacillus subtilis
70
-
 Xyl I, 3 h, presence of 0.5 M trehalose, 36% of initial activity Bacillus subtilis
70
-
 Xyl II, 3 h, presence of 0.5 M trehalose, 50% of initial activity Bacillus subtilis

pI Value

Organism Comment pI Value Maximum pI Value
Bacillus subtilis or higher, enzyme Xyl I 4.7 4.6
Bacillus subtilis enzyme Xyl II
-
 7.5