【 摘 要 】
A β-glycosidase gene homolog of Pyrococcus horikoshii (BGPh) was successfully expressed in Escherichia coli. The enzyme was localized in a membrane fraction and solubilized with 2.5% Triton X-100 at 85°C for 15 min. The optimum pH was 6.0 and the optimum temperature was over 100°C, respectively. BGPh stability was dependent on the presence of Triton X-100, the enzyme's half-life at 90°C (pH 6.0) was 15 h. BGPh has a novel substrate specificity with k cat/K m values high enough for hydrolysis of β-D-Glcp derivatives with long alkyl chain at the reducing end and low enough for the hydrolysis of β-linked glucose dimer more hydrophilic than aryl- or alkyl-β-D-Glcp.
【 授权许可】
Unknown
【 预 览 】
Files | Size | Format | View |
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RO201912020308985ZK.pdf | 324KB | download |