Puri¢cation and Characterisation of Xylanolytic Enzymes of a Cellulase-freeThermophilic strain of Clostridiumabsonum CFR-702

Swaroopa Rani, D. and Nand, Krishna (2001) Puri¢cation and Characterisation of Xylanolytic Enzymes of a Cellulase-freeThermophilic strain of Clostridiumabsonum CFR-702. Anaerobe, 7. pp. 45-53.

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Abstract

Two endo-b-1-4-xylanases (EC 3.2.1.8), xylanase-I and xylanase-II, were purified from Clostridium absonum CFR-702 by ammonium sulphate precipitation and chromatographed on DEAE-Cellulose and phenyl-Sepharose. The enzymes in sodium dodecyl sulphate polyacrylamide gels resolved as proteins corresponding to molecular mass 150 and 95 kDa for xylanase-I and xylanase-II, respectively. The optimum pH and temperature ranges for the enzyme activities on birchwood xylan were between 6.5 and 7.5 and 758C for xyl-I and 7.5 and 808C for xyl-II. Xyl-I was stable up to 608C whereas xyl-II was stable at 508C. Both the enzymes liberated xylobiose,xylotriose and xylotetraose from birchwood xylan. Xyl-I and xyl-II with birchwood xylan had Km values of 1.1 and 1.4%, and Vmax values of 454.54 and 363.63 mmol/min/mg protein respectively.

Item Type:	Article
Uncontrolled Keywords:	Clostridium absonum, cellulase-free xylanase, purification, characterisation, anaerobic thermophilic bacteria
Subjects:	500 Natural Sciences and Mathematics > 07 Life Sciences > 03 Biochemistry & Molecular Biology > 12 Microbial Biochemistry 500 Natural Sciences and Mathematics > 04 Chemistry and Allied Sciences > 28 Polysaccharide Chemistry
Divisions:	Food Microbiology
Depositing User:	Food Sci. & Technol. Information Services
Date Deposited:	22 Jun 2007 10:18
Last Modified:	28 Dec 2011 09:28
URI:	http://ir.cftri.res.in/id/eprint/1251

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