Abstract
A maltotriose-forming amylase (G3Amy) from Kitasatospora sp. MK-1785 was successfully isolated from a soil sample by inhibiting typical extracellular α-amylases using a proteinaceous α-amylase inhibitor. G3Amy was purified from the MK-1785 culture supernatant and characterized. G3Amy produced maltotriose as the principal product from starch and was categorized as an exo-α-amylase. G3Amy could also transfer maltotriose to phenolic and alcoholic compounds. Therefore, G3Amy can be useful for not only maltotriose manufacture but also maltooligosaccharide-glycoside synthesis. Further, the G3Amy gene was cloned and expressed in Escherichia coli cells. Analysis of its deduced amino acid sequence revealed that G3Amy consisted of an N-terminal GH13 catalytic domain and two C-terminal repeat starch-binding domains belonging to CBM20. It is suggested that natural G3Amy was subjected to proteolysis at N-terminal region of the anterior CBM20 in the C-terminal region. As with natural G3Amy, recombinant G3Amy could produce and transfer maltotriose from starch.
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This work was financially supported by grants-in-aid for scientific research (26450100) from the Japan Society for the Promotion of Science.
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Kamon, M., Sumitani, Ji., Tani, S. et al. Characterization and gene cloning of a maltotriose-forming exo-amylase from Kitasatospora sp. MK-1785. Appl Microbiol Biotechnol 99, 4743–4753 (2015). https://doi.org/10.1007/s00253-015-6396-5
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DOI: https://doi.org/10.1007/s00253-015-6396-5