Characterization of a GH36 α-D-Galactosidase Associated with Assimilation of Gum Arabic in <i>Bifidobacterium longum </i>subsp.<i> longum </i>JCM7052
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- Sasaki Yuki
- The United Graduate School of Agricultural Sciences, Kagoshima University
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- Uchimura Yumi
- Department of Food Science and Biotechnology, Faculty of Agriculture, Kagoshima University
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- Kitahara Kanefumi
- The United Graduate School of Agricultural Sciences, Kagoshima University Department of Food Science and Biotechnology, Faculty of Agriculture, Kagoshima University
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- Fujita Kiyotaka
- The United Graduate School of Agricultural Sciences, Kagoshima University Department of Food Science and Biotechnology, Faculty of Agriculture, Kagoshima University
Bibliographic Information
- Other Title
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- Characterization of a GH36 α-D-Galactosidase Associated with Assimilation of Gum Arabic in Bifidobacterium longum subsp. longum JCM7052
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Abstract
<p>We recently characterized a 3-O-α-D-galactosyl-α-L-arabinofuranosidase (GAfase) for the release of α-D-Gal-(1→3)-L-Ara from gum arabic arabinogalactan protein (AGP) in Bifidobacterium longum subsp. longum JCM7052. In the present study, we cloned and characterized a neighboring α-galactosidase gene (BLGA_00330; blAga3). It contained an Open Reading Frame of 2151-bp nucleotides encoding 716 amino acids with an estimated molecular mass of 79,587 Da. Recombinant BlAga3 released galactose from α-D-Gal-(1→3)-L-Ara, but not from intact gum arabic AGP, and a little from the related oligosaccharides. The enzyme also showed the activity toward blood group B liner trisaccharide. The specific activity for α-D-Gal-(1→3)-L-Ara was 4.27- and 2.10-fold higher than those for melibiose and raffinose, respectively. The optimal pH and temperature were 6.0 and 50 °C, respectively. BlAga3 is an intracellular α-galactosidase that cleaves α-D-Gal-(1→3)-L-Ara produced by GAfase; it is also responsible for a series of gum arabic AGP degradation in B. longum JCM7052.</p>
Journal
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- Journal of Applied Glycoscience
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Journal of Applied Glycoscience 68 (2), 47-52, 2021-06-11
The Japanese Society of Applied Glycoscience
