Abstract

Alpha- d-mannosidase from sweet almond emulsin was purified by ion exchange chromatography on CM-cellulose or by electrofocusing technique. The properties of of the purified almond emulsin β- d-mannosidase were also studied. Several components of β- d-glucosidase were present in sweet almond emulsin. Although these β- d-glucosidase components still contained β- d-galactosidase activity, some β- d-galactosidase activities were not conincident with the β- d-glucosidase enzyme in their response to inhibitors.

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