Lactobacillus plantarum is a kind of facultative heterotrophic and facultative anaerobic homo-fermenting lactic acid bacteria， which has glycosidase activity and plays an important role in improving food flavor and fermentation characteristics. Using PCR technology， 8 6-phosphor-β-glucosidase genes from the glycoside hydrolase 1 family of L. plantarum WU14 were successfully cloned. It is showed that eight genes contain a complete open reading frame， and the amino acid sequence alignment reveals there are two conservative catalytic sites of the 6-phosphor-β-glucosidase gene in glycoside hydrolase 1 family， and the sequence identity is between 32%-74%. The results of SDS-PAGE shows that all proteins were expressed in E. coli. Among them， BglAW14， BglCW14， and BglFW14 are partially soluble expression. A purified and recovered to single target band was obtained， and the rest are expression of inclusion bodies. Bioinformatics analysis tells that the encoded proteins have weak hydrophobicity， and none of them have signal peptides and transmembrane structures. The prediction of subcellular structure shows that， except for BglEW14 mainly distributes in the secretion and BglHW14 mainly exists in the cell membrane. The remaining six genes are all present in the cytoplasm. The cloning， protein expression and biological sequence analysis of 6-phosphor-β-glucosidase genes laid a theoretical foundation for further exploring the molecular research of 6-phosphor-β-glucosidase derived from Lactobacillus plantarum.