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Literature summary extracted from

  • Monnet, D.; Joly, C.; Dole, P.; Bliard, C.
    Enhanced mechanical properties of partially beta-amylase trimmed starch for material applications (2010), Carbohydr. Polym., 80, 747-752.
No PubMed abstract available

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.2 Hordeum vulgare
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variety A 7130
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.2 additional information beta-amylase is an exo-enzyme that specifically binds to a double (1-4-alpha-D-glucopyranosyl-1-4-alpha-D-glucopyranosyl-) unit from the non-reducing ends of polymaltosidic polysaccharides, and sequentially cleaves glucose disaccharidic units until it encounters any structural variation, producing maltose as sole hydrolysis product Hordeum vulgare ?
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3.2.1.2 starch + H2O
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Hordeum vulgare maltose + ?
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