New England Biolabs, Inc.

David Landry

Christopher H Taron

Chudi Guan

Ellen P Guthrie

Phillips W Robbins

Sharon Wong-Madden

Sharon T Wong-Madden

Substantially pure glycosidases capable for cleaving selected glycosidic bonds have been described including glycosidases isolated fromand recombinant glycosidases. Substrate specificity of isolated enzymes have been identified for GlcNac&#x3b2;1-x, Gal&#x3b1;1-3R, Gal&#x3b1;1-6R, Gal&#x3b2;1-3R, Fuc&#x3b1;-2R, Fuc&#x3b1;1-3R, Fuc&#x3b1;1-4R, Man&#x3b1;1-2R, Man&#x3b1;1-3R, Man&#x3b1;1-6R, Man&#x3b2;1-4R, Xyl&#x3b2;1-2R, Glc&#x3b2;1-4R, and Gal&#x3b2;1-4R providing improved capability for selectively cleaving a glycosidic linkage in a carbohydrate substrate and for forming modified carbohydrates.

Isolation and composition of novel glycosidases

In accordance with the present invention, there are provided substantially pure glycosidases obtainable from the genus Chryseobacterium. In particular, there is provided a substantially pure exo &agr;-N-Acetylgalactosaminidase from A method of cloning this enzyme and producing a recombinant form of the enzyme is also provided by the present invention.

Isolation and composition of a novel glycosidase from chryseobacterium

In accordance with the present invention, there are provided substantially pure glycosidases obtainable from the genus Chryseobacterium. In particular, there is provided a substantially pure exo &agr;-N-Acetylgalactosaminidase from . A method of cloning this enzyme and producing a recombinant form of the enzyme is also provided by the present invention.

Substantially pure glycosidases capable for cleaving selected glycosidic bonds have been described including glycosidases isolated from Xanthomonas and recombinant glycosidases. Substrate specificity of isolated enzymes have been identified for GlcNac&bgr;1-X, Gal&agr;1-3R, Gal&agr;1-6R, Gal&bgr;1-3R, Fuc&agr;-2R, Fuc&agr;1-3R, Fuc&agr;1-4R, Man&agr;1-2R, Man&agr;1-3R, Man&agr;1-6R, Man&bgr;1-4R, Xyl&bgr;1-2R, Glc&bgr;1-4R, and Gal&bgr;1-4R providing improved capability for selectively cleaving a glycosidic linkage in a carbohydrate substrate and for forming modified carbohydrates.

Substantially pure glycosidases capable for cleaving selected glycosidic bonds have been described including glycosidases isolated from Xanthomonas and recombinant glycosidases. Substrate specificity of isolated enzymes have been identified for GlcNac&bgr;1-X, Gal&agr;1-3R, Gal&agr;1-6R, Gal&bgr;1-3R, Fuc&agr;1-2R, Fuc&agr;1-3R, Fuc&agr;1-4R, Man&agr;1-2R, Man&agr;1-3R, Man&agr;1-6R, Man&bgr;1-4R, Xyl&bgr;1-2R, Glc&bgr;1-4R, and Gal&bgr;1-4R providing improved capability for selectively cleaving a glycosidic linkage in a carbohydrate substrate and for forming modified carbohydrates.

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Essex, MA, United States of America

David Landry