|
KMID : 0545119980080030258
|
|
Journal of Microbiology and Biotechnology
1998 Volume.8 No. 3 p.258 ~ p.263
|
|
|
Purification and Characterization of the Bacillus sp. KK-1 β-Xylosidase from a Recombinant Escherichia coli
|
|
Jung, Kyung Hwa
Chun, Yong Chin/Lee, Jae Chan/Park, Seung Hwan/Yoon, Ki Hong
|
|
|
Abstract
|
|
|
|
β-Xylosidase was purified from the recombinant Escherichia coli carrying the Bacillus sp. KK-1 β-xylosidase gene (xylB). The molecular mass of the purified enzyme was estimated to be 62 kDa by sodium dodecyl sulfatepolyacrylamide gel electrophoresis. However, the apparent molecular mass of the β-xylosidase was 140 kDa, indicating that the native β-xylosidase has an oligomeric structure composed of two identical subunits. The isoelectric point was determined to be pH 5.5. The enzyme was highly active on p-nitrophenyl-β-D-xylopyranoside but it barely hydrolyzed xylan substrates, and d.id not exhibit activity towards carboxymethylcellulose and p-nitrophenyl-β-oglucopyranoside. The enzyme had a pH optimum for its activity at pH 6.5 and a temperature optimum at 40℃. The enzyme activity was completely inhibited by the presence of Hg^++, and also markedly inhibited by D-xylose and D-glucose.
|
|
|
KEYWORD
|
|
|
|
|
|
FullTexts / Linksout information
|
|
|
|
|
|
Listed journal information
|
|
  
|