An α-l-fucosidase was purified approximately 600-fold from Clostridium perfringens; it is free of other glycosidases present in the crude extract. The fucosidase occurs in multiple isozymic forms with molecular weights greater than 200,000. It is an α-(1 → 2)-specific l-fucosidase with action on oligosaccharides and glycoproteins, but with no action on simple methyl or nitrophenyl fucosides. Action on the H-specific hog submaxillary glycoprotein results in the loss of the serological specificity. The enzyme has a pH optimum of 6.0, with a Km of 0.175 mm and its activity is enhanced by the presence of salts, the most effective being calcium chloride.
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Aminoff et al. (1970) studied this question.
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