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Literature summary for 3.2.1.8 extracted from

  • Sakka, K.; Fukumura, M.; Tanaka, A.; Ohmiya, K.
    Characterization of thermostability of Clostridium stercorarium xylanase (1996), Ann. N. Y. Acad. Sci., 799, 341-345.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Thermoclostridium stercorarium
-
xylanase B
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Thermoclostridium stercorarium F-9
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xylanase B
-

Purification (Commentary)

Purification (Comment) Organism
xylanase B Thermoclostridium stercorarium

Renatured (Commentary)

Renatured (Comment) Organism
the enzyme begins to denature at around 80°C and is completely denatured at 100°C. After 5 min at 100°C a large quantity of precipitate without any activity is formed. Aggregated xylanase B is disentangled and dissolved by urea treatment. The native structure is restored by rapid refolding after dilution of urea. Irreversible denaturation of the protein is caused by the same mechanism in solution and in aggregate. The remaining activity detected at 60°C after incubation at pH 7.0 and 100°C is due to the activity of the enzyme that recovers its native structure by correct protein refolding from the denatured state during chilling on ice Thermoclostridium stercorarium

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
80
-
-
Thermoclostridium stercorarium

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
80
-
enzyme begins to denature at around 80°C Thermoclostridium stercorarium
100
-
pH 7.0, 10 min, about 40% loss of activity. pH 5.5, 10 min, complete inactivation Thermoclostridium stercorarium