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alpha galactosidase/jagung

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Arabidopsis ATSIP2 has recently been suggested to be a raffinose synthase gene. However, it has high amino acid identity to functionally characterized alkaline α-galactosidases from Cucumis melo and Zea mays. Using the Sf9 insect cell expression system, we demonstrate that recombinant ATSIP2 is a
Cross-linked enzyme aggregates (CLEAs) of α-galactosidase, partially purified from maize (Zea mays) flour, were prepared. The impact of various parameters on enzyme activity was examined to optimize the immobilization procedure. Biochemical characterization of the free and immobilized

α-and β-Glycosidases in maize roots.

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Four glycosidases were analyzed in 10 mm apical segments prepared from growing roots (15 mm) of Zea mays L. The pH optima were found to be 5.8 for β-glucosidase, 4.4 for β-galactosidase, 6.4 for α-glucosidase and 6.0 for α-galactosidase. The β-glucosidase showed 4-fold higher activity than the
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