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首页> 外文期刊>Bioprocess and Biosystems Engineering >Production of a recombinant polyester-cleaving hydrolase from Thermobifida fusca in Escherichia coli
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Production of a recombinant polyester-cleaving hydrolase from Thermobifida fusca in Escherichia coli

机译：在大肠杆菌中由Thermobifida fusca生产重组的聚酯裂解水解酶

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The hydrolase (Thermobifida fusca hydrolase; TfH) from T. fusca was produced in Escherichia coli as fusion protein using the OmpA leader sequence and a His_6 tag. Productivity could be raised more than 100-fold. Both batch and fed-batch cultivations yield comparable cell specific productivities whereas volumetric productivities differ largely. In the fed-batch cultivations final rTfH concentrations of 0.5 g L~(-1) could be achieved. In batch cultivations the generated rTfH is translocated to the periplasm wherefrom it is completely released into the extracellular medium. In fed-batch runs most of the produced rTfH remains as soluble protein in the cytoplasm and only a fraction of about 35% is translocated to the periplasm. Migration of periplas-mic proteins in the medium is obviously coupled with growth rate and this final transport step possibly plays an important role in product localization and efficacy of the Sec translocation process.
机译：使用OmpA前导序列和His_6标签，在大肠杆菌中产生来自福氏螺旋体的水解酶（Thermobifida fusca水解酶； TfH）作为融合蛋白。生产率可以提高100倍以上。分批和补料分批培养均可产生可比的细胞比生产率，而容积生产率差异很大。在分批补料培养中，最终的rTfH浓度可达到0.5 g L〜（-1）。在分批培养中，生成的rTfH易位至周质，并从中完全释放到细胞外培养基中。在分批补料运行中，大多数产生的rTfH仍以可溶性蛋白形式保留在细胞质中，只有约35％的一部分转移到周质中。质膜蛋白在培养基中的迁移显然与生长速率有关，该最终转运步骤可能在Sec转运过程的产物定位和功效中起重要作用。

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