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

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Ana-01-01
 
Title Puri¢cation and Characterisation of Xylanolytic
Enzymes of a Cellulase-freeThermophilic strain of
Clostridiumabsonum CFR-702
 
Creator Swaroopa Rani, D.
Nand, Krishna
 
Subject 12 Microbial Biochemistry
28 Polysaccharide Chemistry
 
Description 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.
 
Date 2001
 
Type Article
PeerReviewed
 
Format application/pdf
 
Language en
 
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Identifier http://ir.cftri.com/1251/1/Anaerobe_%282001%29_7%2C_45-53.pdf
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.