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ONLINEISSN:1347-6947
PRINTISSN:0916-8451
Bioscience, Biotechnology, and Biochemistry
Vol. 66 (2002) , No. 6 pp.1246-1255
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Cloning and Structural Analysis of bglM Gene Coding for the Fungal Cell Wall-lytic β-1,3-Glucan-hydrolase BglM of Bacillus circulans IAM1165
Takeshi ASANO1), Jiro TAKI1), Mami YAMAMOTO1) and Rikizo AONO1)
1) Department of Biological Information, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology
(Received October 25, 2001)
(Accepted January 10, 2002)
  Bacillus circulans IAM1165 produces isoforms of β-1,3-glucan-hydrolases. Of these enzymes, the 42-kDa enzyme BglM degrades Aspergillus oryzae cell walls the most actively. A gene coding for a BglM precursor consisting of 411 amino acid residues was cloned. The 27 N-terminal amino acid sequence of the precursor is a signal peptide. The 141 C-terminal amino acid sequence showed a motif of carbohydrate-binding module family 13. This domain bound to pachyman, lichenan, and A. oryzae cell walls. The central domain showed a bacterial β-1,3-glucan-hydrolase motif belonging to glycosyl hydrolase family 16. By removal of the C-terminal domain in the IAM1165 culture, mature BglM was processed to several 27-kDa fragments that hydrolyze a soluble β-1,3-glucan.
Key words:Bacillus circulans; β-1,3-glucanase; 1,3-(1,3;1,4)-β-D-glucan 3(4)-glucanohydrolase; fungal cell wall-binding domain; fungal cell wall lytic enzyme

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To cite this article:
Takeshi ASANO, Jiro TAKI, Mami YAMAMOTO and Rikizo AONO, “Cloning and Structural Analysis of bglM Gene Coding for the Fungal Cell Wall-lytic β-1,3-Glucan-hydrolase BglM of Bacillus circulans IAM1165”, Biosci. Biotechnol. Biochem., Vol. 66, 1246-1255 (2002) .

doi:10.1271/bbb.66.1246
JOI  JST.JSTAGE/bbb/66.1246
Copyright (c) 2003 by Japan Society for Bioscience, Biotechnology, and Agrochemistry



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