Characterization of cloned endoxylanase from Cellulomonas sp. NCIM 2353 expressed in Escherichia coli

Priya Chaudhary, D. N. Deobagkar

Research output: Contribution to journalArticle

5 Citations (Scopus)

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 pl 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.

Original languageEnglish (US)
Pages (from-to)273-279
Number of pages7
JournalCurrent Microbiology
Volume34
Issue number5
DOIs
StatePublished - May 1997
Externally publishedYes

Fingerprint

Cellulomonas
Endo-1,4-beta Xylanases
Escherichia coli
Tryptophan
Xylans
Catalytic Domain
Molecular Weight
Temperature
Antibodies
Enzymes
Genes
Proteins

ASJC Scopus subject areas

  • Microbiology

Cite this

Characterization of cloned endoxylanase from Cellulomonas sp. NCIM 2353 expressed in Escherichia coli. / Chaudhary, Priya; Deobagkar, D. N.

In: Current Microbiology, Vol. 34, No. 5, 05.1997, p. 273-279.

Research output: Contribution to journalArticle

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