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Applied and Environmental Microbiology, April 2008, p. 2379-2383, Vol. 74, No. 8
0099-2240/08/$08.00+0     doi:10.1128/AEM.01733-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Characterization of an Endo-β-1,6-Galactanase from Streptomyces avermitilis NBRC14893{triangledown}

Hitomi Ichinose,1 Toshihisa Kotake,2 Yoichi Tsumuraya,2 and Satoshi Kaneko1*

Food Biotechnology Division, National Food Research Institute, 2-1-12 Kannondai, Tsukuba, Ibaraki 305-8642, Japan,1 Graduate School of Science and Engineering, Saitama University, 255 Shimo-okubo, Sakura-ku, Saitama 338-8570, Japan2

Received 27 July 2007/ Accepted 14 February 2008

The putative endo-β-1,6-galactanase gene from Streptomyces avermitilis was cloned and expressed in Escherichia coli, and the enzymatic properties of the recombinant enzyme were characterized. The gene consisted of a 1,476-bp open reading frame and encoded a 491-amino-acid protein, comprising an N-terminal secretion signal sequence and glycoside hydrolase family 5 catalytic module. The recombinant enzyme, Sa1,6Gal5A, catalyzed the hydrolysis of β-1,6-linked galactosyl linkages of oligosaccharides and polysaccharides. The enzyme produced galactose and a range of β-1,6-linked galacto-oligosaccharides, predominantly β-1,6-galactobiose, from β-1,6-galactan chains. There was a synergistic effect between the enzyme and Sa1,3Gal43A in degrading tomato arabinogalactan proteins. These results suggest that Sa1,6Gal5A is the first identified endo-β-1,6-galactanase from a prokaryote.

* Corresponding author. Mailing address: National Food Research Institute, 2-1-12 Kannondai, Tsukuba, Ibaraki 305-8642, Japan. Phone: 81-298-38-8022. Fax: 81-298-38-7996. E-mail: sakaneko{at}affrc.go.jp

{triangledown} Published ahead of print on 29 February 2008.

Applied and Environmental Microbiology, April 2008, p. 2379-2383, Vol. 74, No. 8
0099-2240/08/$08.00+0     doi:10.1128/AEM.01733-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.





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