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Gene expression and molecular characterization of a thermostable trehalose phosphorylase from Thermoanaerobacter tengcongensis

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Science China(Life Sciences) 2005年第3期48卷 221-227页

作者： REN Yuanyuan 1,2 , DAI Xiuyu 1 , ZHOU Jian 1 , LIU Jingfang 1 , PEI Huadong 1,2 & XIANG Hua 1 1. State Key Laboratory of Microbial Resources and Center for Molecular Microbiology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100080, China 2. Graduate School of Chinese Academy of Sciences, Beijing 100037, China State Key Laboratory of Microbial Resources and Center for Molecular Microbiology Institute of Microbiology Chinese Academy of Sciences Beijing China Graduate School of Chinese Academy of Sciences Beijing China

A gene encoding the trehalose phosphorylase (TreP), which reversibly catalyzes trehalose degradation and synthesis from α-glucose-1-phosphate (α-Glc-1-P) and glucose, was cloned from Thermoanaerobacter tengcongensis and successfully expressed in Escherichia coli. The overexpressed TreP, with a molecular mass of approximately 90 kDa, was determined by SDS-PAGE. It catalyzes trehalose synthesis and degradation optimally at 70℃ (for 30 min), with the optimum pHs at 6.0 and 7.0, respectively. It is highly thermostable, with a 77% residual ac- tivity after incubation at 50℃ for 7 h. Under the optimum reaction conditions, 50 μg crude en- zyme of the TreP is able to catalyze the synthesis of trehalose up to 11.6 mmol/L from 25 mmol/L α-Glc-1-P and 125 mmol/L glucose within 30 min, while only 1.5 mmol/L out of 250 mmol/L tre- halose is degraded within the same time period. Dot blotting revealed that the treP gene in T. tengcongensis was upregulated in response to salt stress but downregulated when trehalose was supplied. Both results indicate that the dominant function of the T. tengcongensis TreP is catalyzing trehalose synthesis but not degradation. Thus it might provide a novel route for indus- trial production of trehalose.

关键词： gene expression, Thermoanaerobacter tengcongensis, trehalose phosphorylase, dot blot.

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