Abstract
β-D-glucosidase (βG) gene from Oenococcus oeni SD-2a and 31MBR was cloned, sequenced and analyzed, also intracellular βG of the two strains was further localized. The results showed that βG gene of the two strains was in high homology (> 99%) to reported βG gene, confirming both strains possess βG activity at the molecular level. Intracellular βG of SD-2a is a mainly soluble protein, existing mostly in the cytoplasm and to some extent in the periplasm. While for 31MBR, intracellular βG is mainly insoluble protein existing in the cytoplasmic membrane. This study provides basic information for further study of the metabolic mechanism of βG from O. oeni SD-2a and 31MBR.