High-glucose　syrup　has　wide　applications　in　the　feed　and　fermentation　industries.　However,　during　its　regular　production　process,　because　of　the　slow　hydrolysis　of　alpha-1,6-glucosidic　linkages　in　maltodextrins　by　glucoamylase,　yields　of　glucose　higher　than　96%　are　rarely　achieved.　To　find　a　suitable　enzyme　for　the　saccharification　process,　two　novel　genes　encoding　oligo-1,6-glucosidases　(OGL,　EC　3.2.1.10)　from　Bacillus　mycoides　(bmogl)　and　Thermomyces　lanuginosus　(tlogl)　were　successfully　cloned　and　overexpressed　in　Pichia　pastoris　GS115.　At　the　shake-flask　fermentation　level,　the　OGL　activities　of　the　two　recombinants　GS115　(pPIC9K-bmogl)　and　GS115　(pPIC9K-tlogl)　were　994　and　1219U/mL,　respectively;　and　mature　enzymes　around　66-68kDa　were　purified　for　characterization.　Recombinant　enzyme　TlOGL　exhibited　higher　thermostability　than　ever　reported　for　OGLs,　whereas　BmOGL　was　stable　under　acidic　pH,　ranging　from　4.0　to　8.0.　Among　the　substrates　tested,　these　two　recombinant　enzymes　efficiently　hydrolyzed　isomaltose　and　isomaltotriose,　but　had　no　activity　against　maltose　and　maltotriose.　Besides　these　characteristics,　nearly　complete　hydrolysis　of　isomaltotriose　and　90%　of　isomaltooligosaccharides　(IMOs)　into　glucose　was　also　observed　for　them,　which　makes　them　good　candidates　for　subsequent　use　in　improving　the　yield　of　glucose　from　starch.　To　the　best　of　our　knowledge,　this　is　the　first　report　on　the　expression　and　characterization　of　OGLs　from　B.　mycoides　and　T.　lanuginosus.