Abstract
A 100-fold purification of acid β-fructofuranosidase activity (optimum pH 4.5) was obtained from Opuntia ficus-indica fruits using ion exchange (DEAE-Sephadex A50) and affinity (concanavalin-A) column chromatography. The purified enzyme is a glycoprotein from its ability to bind the lectin concanavalin-A. SDS polyacrylamide gel electrophoresis resolved one major diffuse band at 54000. This band exhibited invertase activity in the native gel. The enzyme was stable between pH 5 and 7 and exhibited high sensitivity to Hg 2+. Thermal inactivation appeared biphasic. A saturable protection effect against thermal inactivation was afforded by glucose.
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