MISC

2003年4月

Purification and characterization of an extracellular beta-agarase from Bacillus sp MK03

JOURNAL OF BIOSCIENCE AND BIOENGINEERING
  • H Suzuki
  • ,
  • Y Sawai
  • ,
  • T Suzuki
  • ,
  • K Kawai

95
4
開始ページ
328
終了ページ
334
記述言語
英語
掲載種別
DOI
10.1263/jbb.95.328
出版者・発行元
SOC BIOSCIENCE BIOENGINEERING JAPAN

A new beta-agarase was purified from an agarolytic bacterium, Bacillus sp. MK03. The enzyme was purified 129-fold from the culture supernatant by ammonium sulfate precipitation, anion exchange and gel filtration column chromatographic methods. The purified enzyme appeared as a single band on sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). Estimation of the molecular mass by SDS-PAGE and gel filtration gave values of 92 kDa and 113 kDa, respectively. The N-terminal amino acid sequence of the enzyme showed no homology to those of other known agarases. The optimum pH and temperature for this enzyme were 7.6 and 40degreesC, respectively. The predominant hydrolysis product of agarose by this enzyme was neoagarotetraose, indicating the cleavage of beta-1,4 linkage. This enzyme could hydrolyze neoagarohexaose to produce neoagarotetraose and neoagarobiose; it could not hydrolyze these products. The enzyme digested agarose by endo-type hydrolysis.

Web of Science ® 被引用回数 : 50

リンク情報
DOI
https://doi.org/10.1263/jbb.95.328
CiNii Articles
http://ci.nii.ac.jp/naid/110002687571
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000183494100002&DestApp=WOS_CPL
ID情報
  • DOI : 10.1263/jbb.95.328
  • ISSN : 1389-1723
  • CiNii Articles ID : 110002687571
  • Web of Science ID : WOS:000183494100002

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