alpha-Glucosidase　was　immobilized　onto　an　epoxy-activated　resin　(Eupergit　C)　to　catalyze　maltose　into　isomaltooligosaccharides　(IMO),　and　then　the　effects　of　organic-aqueous　media　on　the　enzymatic　properties　of　immobilized　alpha-glucosidase　were　examined.　An　immobilization　efficiency　of　79.61%　was　obtained　under　the　condition　of　pH　6.0,　ionic　strength　of　2.0　M,　and　30　mg　of　protein/g　of　resin.　The　butyl　acetate-aqueous　biphasic　system　was　found　to　significantly　improve　the　catalytic　activity　of　the　immobilized　enzyme　and　the　yield　of　IMO.　The　highest　yield　of　IMO　(50.83%,　w/w)　was　obtained　at　pH　4.5　and　55　A　degrees　C　in　a　butyl　acetate/buffer　system　(25:75,　v/v).　In　addition,　the　immobilized　enzyme　particles　were　distributed　into　the　organic　phase　after　the　completion　of　transglycosylation,　which　facilitates　the　separation　and　recycling　use　of　the　immobilized　enzyme.　Immobilized　alpha-glucosidase　retains　a　robust　reusability　in　this　continuous　operation　model.　The　present　findings　are　of　potential　in　improving　the　IMO　manufacturing　process.