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Purification and characterization of thermoalkalophilic xylanase isolated from the Enterobacter sp. MTCC 5112

DRS at CSIR-National Institute of Oceanography

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Title Purification and characterization of thermoalkalophilic xylanase isolated from the Enterobacter sp. MTCC 5112
 
Creator Khandeparker, R.
Bhosle, N.B.
 
Subject Enterobacter sp
Thermophilic
 
Description Thermoalkalophilic Enterobacter sp MTCC 5112 was isolated from a sediment sample collected from the Mandovi estuary, west coat of India. This culture produced extracellular xylanase. The xylanase enzyme was isolated by ammonium sulfate (80 %) fractionation, and purified to homogeneity using size exclusion and ion exchange chromatography. The molecular mass of the xylanase was ~ 43 kDa. The optimal pH of the xylanase activity was 9, and at room temperature it showed 100% stability for 3 h at pH 7, 8 and 9. The optimal temperature for the enzyme activity was 100 ?C at pH 9.0. At 80 oC and pH 9, 90 % of the enzyme activity was retained after 40 min. At 70 oC and 60 oC, the enzyme retained 64 % and 85 % of its activity after 18 h, respectively. While at 50 oC and pH 9 the enzyme remained stable for days. For xylan, the enzyme gave a Km value of 3.3 mg/ml, and Vmax value of 5000 ?mol.min-1. mg-1 when the reaction was carried out at 100 oC and pH 9. In the presence of metal ions such as Co+2, Zn+2 , Fe+2, Cu+2 , Mg+2 and Ca+2 the activity of the enzyme increased. Whereas, strong inhibition of the enzyme activity was observed in the presence of Hg+2 and EDTA. To the best of our knowledge this is the first report on the production of xylanase by this bacterium.
 
Date 2006-06-14T05:03:14Z
2006-06-14T05:03:14Z
2006
 
Type Journal Article
 
Identifier Research in Microbiology, vol. 157, 315?325
http://drs.nio.org/drs/handle/2264/115
 
Language en
 
Rights 2005 Elsevier SAS. All rights reserved.
 
Format 338186 bytes
application/pdf
 
Publisher Elsevier