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Applied and Environmental Microbiology, May 2007, p. 3109-3112, Vol. 73, No. 9
0099-2240/07/$08.00+0     doi:10.1128/AEM.02101-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Characterization of Fusarium oxysporum ß-1,6-Galactanase, an Enzyme That Hydrolyzes Larch Wood Arabinogalactan{triangledown}

Tatsuji Sakamoto,1* Yuya Taniguchi,1 Shiho Suzuki,1 Hideshi Ihara,2 and Haruhiko Kawasaki1

Division of Applied Life Sciences, Graduate School of Life and Environmental Sciences, Osaka Prefecture University, Osaka 599-8531, Japan,1 Department of Biological Science, Graduate School of Science, Osaka Prefecture University, Osaka 599-8531, Japan2

Received 6 August 2006/ Accepted 4 March 2007

A type II arabinogalactan-degrading enzyme (FoGal1) was purified from Fusarium oxysporum 12S, and the corresponding cDNA was isolated. FoGal1 had high similarity to enzymes of glycoside hydrolase family 5. Treatment of larch wood arabinogalactan with the recombinant enzyme indicated that FoGal1 is a ß-1,6-galactanase that preferentially debranches ß-1,6-galactobiose from the substrate.

* Corresponding author. Mailing address: Division of Applied Life Sciences, Graduate School of Life and Environmental Sciences, Osaka Prefecture University, Osaka 599-8531, Japan. Phone: 81 72 254 9456. Fax: 81 72 254 9921. E-mail: sakamoto{at}biochem.osakafu-u.ac.jp

{triangledown} Published ahead of print on 9 March 2007.

Applied and Environmental Microbiology, May 2007, p. 3109-3112, Vol. 73, No. 9
0099-2240/07/$08.00+0     doi:10.1128/AEM.02101-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Ichinose, H., Kotake, T., Tsumuraya, Y., Kaneko, S. (2008). Characterization of an Endo-{beta}-1,6-Galactanase from Streptomyces avermitilis NBRC14893. Appl. Environ. Microbiol. 74: 2379-2383 [Abstract] [Full Text]  


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