A　β-glucosidase　gene　(bglI)　from　Trichoderma　reesei　was　cloned　into　the　pPIC9　vector　and　integrated　into　the　genome　of　Pichia　pastoris　GS115.　Under　the　control　of　the　methanol-inducible　alcohol　oxidase　(AOX)　promoter　and　using　Saccharomycescerevisiae　secretory　signal　peptide　(α-factor),　the　recombinant　β-glucosidase　was　expressed　and　secreted　into　the　culture　medium.　The　maximum　recombinant　β-glucosidase　activity　achieved　was　60　U/ml,　and　β-glucosidase　expression　reached　0.3　mg/ml.　The　recombinant　76　kDa　β-glucosidase　was　purified　1.8-fold　with　26%　yield　and　a　specific　activity　of　197　U/mg.　It　was　optimally　active　at　70°C　and　pH　5.0.　©　2011　Springer　Science+Business　Media　B.V.