Characterization of Cloned Endoxylanase from Cellulomonas sp. NCIM 2353 Expressed in Escherichia coli |
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Authors: | Priya Chaudhary DN Deobagkar |
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Institution: | (1) Molecular Biology Research Laboratory, Department of Zoology, University of Pune, Ganeshkhind, Pune 411007, India , IN |
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Abstract: | A 22-kDa xylanase encoded by a cloned gene (XCs16)
of Cellulomonas was purified to homogeneity with an overall yield of
44%. It is a basic protein with a pI of 8.1 and has a
K
m
and V
max of 3 mg/ml and 1150
μmoles/mg/min, respectively, for oat spelt xylan at 55°C and pH 5.8.
Homologous xylanase from Cellulomonas could be identified with
antibodies raised against purified xylanase encoded by XCs16. The
enzyme from Cellulomonas also exhibited identical temperature and pH
optimum and had a molecular weight of 23 kDa. Modification of tryptophan
residue of purified xylanase resulted in the loss of xylanase activity. This
loss could be reversed by the addition of substrate, indicating the
involvement of tryptophan residue in the catalytic site.
Received: 12 April 1996 / Accepted: 28 October 1996 |
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Keywords: | |
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