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Catalytic properties of the immobilized Aspergillus tamarii xylanase.

Authors
  • Gouda, Mona K
  • Abdel-Naby, Mohamed A
Type
Published Article
Journal
Microbiological Research
Publisher
Elsevier
Publication Date
Jan 01, 2002
Volume
157
Issue
4
Pages
275–281
Identifiers
PMID: 12501991
Source
Medline
License
Unknown

Abstract

Xylanase from Aspergillus tamarii was covalently immobilized on Duolite A147 pretreated with the bifunctional agent glutaraldehyde. The bound enzyme retained 54.2% of the original specific activity exhibited by the free enzyme (120 U/mg protein). Compared to the free enzyme, the immobilized enzyme exhibited lower optimum pH, higher optimum reaction temperature, lower energy of activation, higher Km (Michaelis constant), lower Vmax (maximal reaction rate). The half-life for the free enzyme was 186.0, 93.0, and 50.0 min for 40, 50, and 60 degrees C, respectively, whereas the immobilized form at the same temperatures had half-life of 320, 136, and 65 min. The deactivation rate constant at 60 degrees C for the immobilized enzyme is about 6.0 x 10(-3), which is lower than that of the free enzyme (7.77 x 10(-3) min). The energy of thermal deactivation was 15.22 and 20.72 kcal/mol, respectively for the free and immobilized enzyme, confirming stabilization by immobilization. An external mass transfer resistance was identified with the immobilization carrier (Duolite A147). The effect of some metal ions on the activity of the free and immobilized xylanase has been investigated. The immobilized enzyme retained about 73.0% of the initial catalytic activity even after being used 8 cycles.

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