Purification and characterization of xylanases from Cellulomonas sp. N.C.I.M. 2353

Priya Chaudhary, Dileep N. Deobagkar

Research output: Contribution to journalArticlepeer-review

14 Scopus citations

Abstract

Cellulomonas produces multiple xylanases in the presence of xylan, carboxymethylcellulose (CMC), starch and, to a very much lesser extent, cellobiose. A procedure involving (NH4)2SO4 precipitation, DEAE-cellulose chromatography and gel filtration was used to purify the xylanases. True xylanases and xylanases with multiple specificity were detected. True xylanases had an optimum pH of 6.5, a temperature optimum of about 55°C, and pI values of about 8.0. The molecular masses of the purified xylanases were found to be 23, 33 and 53 kDa. The K(m) and V(max) values of the 33 and 53 kDa enzymes were 1.7 and 1.5 mg/ml, and 380 and 690 μmol/min per mg respectively. The 33 and 53 kDa enzymes were totally inactivated in the presence of HgCl2 and AgNO3. These two enzymes were not affected by 5 mM concentrations of KCl, MgCl2, NaCl and MnSO4. These enzymes were identified as endoxylanases on the basis of their end products. Xylanases other than these three enzymes were also found in a 'cellulosome' type of complex in Cellulomonas. Enzymes in this complex showed activity towards both CMC and xylan.

Original languageEnglish (US)
Pages (from-to)127-133
Number of pages7
JournalBiotechnology and Applied Biochemistry
Volume25
Issue number2
StatePublished - Apr 14 1997

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Molecular Medicine
  • Biomedical Engineering
  • Applied Microbiology and Biotechnology
  • Drug Discovery
  • Process Chemistry and Technology

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