α-Mannosidase from Pineapple Fruit: Partial Purification and Action on Glycopeptides

Abstract

α-Mannosidase [EC 3. 2. 1. 24, α-D-mannoside mannohydrolase] from the acetone powder of pineapple fruit juice was purified 190-fold by column chromatographic procedures. The partially purified α-mannosidase was detected to be contaminated with little other glycosidases, using p-nitrophenyl derivatives of glycosides. The enzyme released mannose from both the carbohydrate moiety of stem bromelain and glycopeptide prepared from the parent protein. The enzyme split about 70% of the total mannose of ovalbumin glycopeptide.