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Partial Purification and Characterization of Raucaffricine β‐ D ‐Glucosidase from Plant Cell‐Suspension Cultures of Rauwolfia serpentina B ENTH
Author(s) -
Schübel Helmut,
Stöckigt Joachim,
Feicht Richard,
Simon Helmut
Publication year - 1986
Publication title -
helvetica chimica acta
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.74
H-Index - 82
eISSN - 1522-2675
pISSN - 0018-019X
DOI - 10.1002/hlca.19860690303
Subject(s) - chemistry , enzyme , suspension culture , substrate (aquarium) , fructose , suspension (topology) , biochemistry , cell culture , chromatography , biology , ecology , mathematics , homotopy , pure mathematics , genetics
A novel highly substrate‐specific Rauwolfia enzyme, raucaffricine β‐ D ‐glucosidase, was isolated from cell‐suspension cultures of R. serpentina . The enzyme has been purified ca. 1350‐fold, its major characteristics such as M r = 66600 ± 5%, pH optimum 5.1, temperature optimum 38°, and inhibition of its activity by glucose and fructose were investigated. Its limited distribution in different cell cultures and differentiated plants indicates that the enzyme is present in significant amounts exclusively in cultured Rauwolfia cells.