Barley Malt alpha-Glucosidase. V. Degradation of Starch and Dextrins.
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چکیده
منابع مشابه
Purification, enzymatic characterization, and nucleotide sequence of a high-isoelectric-point alpha-glucosidase from barley malt.
High-isoelectric-point (pI) alpha-glucosidase was purified 7, 300-fold from an extract of barley (Hordeum vulgare) malt by ammonium sulfate fractionation, ion-exchange, and butyl-Sepharose chromatography. The enzyme had high activity toward maltose (k(cat) = 25 s(-1)), with an optimum at pH 4.5, and catalyzed the hydrolysis by a retaining mechanism, as shown by nuclear magnetic resonance. Acarb...
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Pea chloroplastic [alpha]-glucosidase (EC 3.2.1.20) involved in transitory starch degradation was purified to apparent homogeneity by ion exchange, reactive dye, hydroxylapatite, hydrophobic interaction, and gel filtration column chromatography. The native molecular mass and the subunit molecular mass were about 49.1 and 24.4 kD, respectively, suggesting that the enzyme is a homodimer. The enzy...
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A comparative chromatography of polyphenoloxidase isolated from barley, steeped barley, and green malt was made. It consisted ofextraction, precipitation, ion-exchange chromatography, gel filtration, and electrofocusing. Polyphenoloxidase was resolved into a high-molecularweight enzyme and a low-molecular-weight one. The proportion of the two enzymes underwent variations during malting. An incr...
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متن کاملPurification, Enzymatic Characterization, and Nucleotide Sequence of a High-Isoelectric-Point a-Glucosidase from Barley Malt
High-isoelectric-point (pI) a-glucosidase was purified 7,300-fold from an extract of barley (Hordeum vulgare) malt by ammonium sulfate fractionation, ion-exchange, and butyl-Sepharose chromatography. The enzyme had high activity toward maltose (kcat 5 25 s ), with an optimum at pH 4.5, and catalyzed the hydrolysis by a retaining mechanism, as shown by nuclear magnetic resonance. Acarbose was a ...
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ژورنال
عنوان ژورنال: Acta Chemica Scandinavica
سال: 1964
ISSN: 0904-213X
DOI: 10.3891/acta.chem.scand.18-1975