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Studies on the Glycosidases in Jack Bean Meal

I. ISOLATION AND PROPERTIES OF -MANNOSIDASE

From the ¹ From the Department of Biochemistry, Tulane University Delta Regional Primate Research Center, Covington, Louisiana 70433

-Mannosidase was purified approximately 500-fold from jack bean meal. This enzyme was able to hydrolyze -1,6', -1,2'-, and -1,3'-linked oligomannosides, but not phenyl-ß-d-mannoside and ß-1,4'-linked mannobiose. Approximately 5% of the total mannose present in the yeast mannan was set free by -mannosidase after prolonged incubation. The fact that no sugars other than mannose were detected in the mannan digests indicates that this enzyme is not a polysaccharidase (endoenzyme) in nature. The enzyme hydrolyzes mannobiose, mannotriose, and mannotetraose derived from yeast mannan.

The K_m values obtained were: p-nitrophenyl--d-mannoside, 2.5 x 10^-3 m; benzyl--d-mannoside, 3.1 x 10^-2 m; methyl--d-mannoside, 1.2 x 10^-1 m. The enzyme was competitively inhibited by mannono-(1 4)- and (1 5)-lactone. With p-nitrophenyl--d-mannoside as substrate, K_i values for (1 4)- and (1 5)-lactone were 1.0 x 10^-2 m and 1.2 x 10^-4 m, respectively.

-Mannosidase catalyzes hydrolysis, glycosyl transfer, and synthesis. One of the two disaccharides synthesized from mannose by -mannosidase was identified as -1,6'-linked mannobiose.

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