Abstract
By means of specific exoglycosidases, sugars have been removed under non-denaturing conditions from ascorbic acid oxidase (AAO), different deglycation schedules being followed. Our results indicate that deglycation clearly affects the kinetic features of AAO, leading to an increase of 'affinity' and 'catalytic ability' of the enzymic forms so generated. A better exposure of the catalytic-site residues could be supposed to occur upon treatment with exoglycosidases. This is supported by the three-dimensional X-ray structure of zucchini (Cucurbita pepo medullosa; courgette) AAO.
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