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- W1966042602 abstract "A p-nitrophenyl α-d-glucopyranoside-hydrolyzing α-glucosidase of an obligate thermophile, Bacillus stearothermophilus ATCC 12016, was purified to an electrophoretically and immunologically homogeneous state. The specific activity was 113 μmol p-nitrophenyl α-d-glucopyranoside hydrolyzed/min per mg protein at 60°C and pH 6.8. The molecular weight, Stokes radius, sedimentation coefficient (s20,w), extinction coefficient at 280 nm and pH 6.8, and isoelectric point were estimated as 47 000, 3.06 nm, 3.98 S, 2.88 cm2 · mg−1 and 5.2, respectively. The NH2-terminal amino acid of the enzyme was menthionine. Neither carbohydrate nor cysteine residue was present in the enzyme. The pH and temperature optima for activity were 6.3 and 70°C, respectively. The Km for the nitrophenyl glucoside was 0.63 mM. The enzyme produced α-glucose by the cleavage of single glucose units from the non-reducing terminal α-1,4-bonds of maltosaccharides (chain length = 2–6 glucose units), α-limit dextrins, phenyl α-d-maltoside, dextrin, amylose, amylopectin and soluble starch. The α-1,6-bonds in these saccharides, were not attacked. Sucrose, turanose and melezitose were weakly hydrolyzed, while there was no activity towards the α-glucosidic linkages in methyl α-d-glucoside, nigerose, kojibiose, panose, β-limit dextrins, isomaltosaccharides (2–6 glucose units), α- and β-cyclodextrins, pullulan and dextran. The greatly restricted substrate specificity proposed the assignment of the enzyme to an exo-α-1,4-glucosidase. Other catalytic properties, along with amino acid composition, are described in this report." @default.
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- W1966042602 date "1984-06-01" @default.
- W1966042602 modified "2023-09-27" @default.
- W1966042602 title "Assignment of a p-nitrophenyl α-d-glucopyranosidase of bacillus stearothermophilus ATCC 12016 to a novel exo-α-1,4-glucosidase active for oligomaltosaccharides and α-glucans" @default.
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- W1966042602 doi "https://doi.org/10.1016/0167-4838(84)90321-2" @default.
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