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ABSTRACTβ‐Glucosidase F42 of soy cotyledons was purified by ammonium sulfate fractionation, ion‐exchange chromatography (CM‐Sephadex‐C‐50, Sigma, St. Louis, MO) and gel filtration (Sephadex G‐100, Sigma). The enzyme was purified 111.8‐fold relative to its concentration in the crude extract. It had an apparent molecular mass of 53 kDa in gel filtration experiments and produced a 33‐kDa band in sodium...