Characterization of an endo-beta-1,6-Galactanase from Streptomyces avermitilis NBRC14893 |
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Authors: | Ichinose Hitomi Kotake Toshihisa Tsumuraya Yoichi Kaneko Satoshi |
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Institution: | National Food Research Institute, 2-1-12 Kannondai, Tsukuba, Ibaraki 305-8642, Japan. |
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Abstract: | The putative endo-beta-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 beta-1,6-linked galactosyl linkages of oligosaccharides and polysaccharides. The enzyme produced galactose and a range of beta-1,6-linked galacto-oligosaccharides, predominantly beta-1,6-galactobiose, from beta-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-beta-1,6-galactanase from a prokaryote. |
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