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Podophyllum Peltatum Possesses a β-Glucosidase with High Substrate Specificity for the Aryltetralin Lignan Podophyllotoxin by Franck E Dayan; Jeanne M Kuhajek; Camilo Canel; Susan B Watson; Rita M Moraes is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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A beta-glucosidase with high specificity for podophyllotoxin-4-O-beta-D-glucopyranoside was purified from the leaves of Podophyllum peltatum. The 65-kDa polypeptide had optimum activity at pH 5.0 and was essentially inactive at pH 6.5 or above. Maximum catalytic activity of this glucosidase was obtained at 45 degrees C, but the enzyme was not heat stable. This beta-glucosidase displayed higher substrate specificity for podophyllotoxin-4-O-beta-D-glucopyranoside than for the other lignans tested, and for the (1-->3) linkage of laminaribiose than for other glucosidic linkages.

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Author

Franck E Dayan; Jeanne M Kuhajek; Camilo Canel; Susan B Watson; Rita M Moraes

Publisher

Elsevier Science; Elsevier ; Elsevier BV (ISSN 1570-9639)

Published

2003

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)