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- W2063925073 abstract "Glucoamylase (1,4 α-d glucan glucohydrolase, EC 3.2.1.3) was covalently immobilized on porous glass fibres and beads. The size of the glass beads (125 μm) was chosen to be small enough to avoid diffusional resistance. A comparison of both supports was established and discussed. Enzyme loadings were similar, 1·70–1·85 mg protein/m2 for fibres and 1·65 mg protein/m2 for beads. A 28% w/v maltose and 39% w/v α-amylase-hydrolysed dextrin 12 DE (Dextrose equivalent) syrups were used as model and real feed substrates respectively. A 98·8% maltose conversion was obtained with the glass fibre reactor. However, the hydrolysis of the dextrin syrup (12 DE, 39% dissolved solids, pH 4·5) was incomplete (93·5% conversion with the same reactor and 91·2% with the glass bead reactor). Glucose production from this syrup was poor for both systems: 85·7 and 83·9% respectively. The continuous operational enzyme stability was found to be highly dependent on substrate concentration, up to 57 days being achieved with a feed of 27·6% w/v maltose solution at pH 4·5 and 50°C." @default.
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- W2063925073 date "1992-05-01" @default.
- W2063925073 modified "2023-09-26" @default.
- W2063925073 title "Hydrolysis of maltose and cornstrarch by glucoamylase immobilized in porous glass fibres and beads" @default.
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- W2063925073 doi "https://doi.org/10.1016/0032-9592(92)87006-3" @default.
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