A sucrose: sucrose 1-fructosyltransferase has been highly purified from the extract of asparagus roots by successive chromatographies with DEAE-, CM-cellulose, Sephadex G-200 and sucrose-coupled Sepharose 6B. The disc-electrophoretically homogeneous enzyme (mol. wt. ca. 65000), free from the activity of β-fructofuranosidase and other fructosyltransferases, catalyzes fructosyltransfer from sucrose producing 1-kestose and glucose. The reaction is reversible. The transferase also exhibits an activity of fructosyltransfer from sucrose to the fructose in the sucrose moiety of neokestose and its homologous 6G(1-β-fructofuranosyl)n-sucrose. The enzyme, however, does not catalyze fructosyltransfer to 1F(1-β-fructofuranosyl)m-sucrose and 1F(1-β-fructofuranosyl)m-6G(1-β-fructofuranosyl), tsucrose (except form=0). Other properties of this enzyme are as follows: opt. pH, ca. 5.0; Km for sucrose, 0.11M; stable on heating at 30°C, pH 4.0_??_8.0; labile (ca. 50% loss) on heating at 45°C, pH 5.0_??_6.5; inhibited by Hg2+, p-chloromercuribenzoate, Mn2+ and Ag+.
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Shiomi et al. (1980) studied this question.