Secretion Pathway Identification of Pyrococcus yayanosii L-Asparaginase in Bacillus subtilis and the Secretion Level Improvement
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Q933

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    Abstract:

    Bacillus subtilis, generally recognized as safe (GRAS),waswidely used as host strain to express heterologous proteins due to its good secretion ability and easy geneticmanipulations. In B. subtilis, most of the signal peptide-mediated secretion was depended on Sec-pathway(General secretion pathway) or Tat-pathway(Twin-arginine translocation pathway). In this study, through signal peptide prediction and protein N terminal sequencing, the secretion of Pyrococcus yayanosii L-asparaginase in B. subtilis was confirmedto depend onnon-classical protein secretion pathway. By signal peptidescreening, the Tat-pathway signal peptide SPphoD was found to bebeneficial for the L-asparaginase secretion in B. subtilis. With the co-expression of SPphoD and molecular chaperone PrsA, the L-asparaginase secretion was increased by 72.11% compared with that of the original one.

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LI Xu, XU Shuqin, ZHANG Xian, XU Meijuan, YANG Taowei, ZHANG Huiling, FANG Haitian, RAO Zhiming. Secretion Pathway Identification of Pyrococcus yayanosii L-Asparaginase in Bacillus subtilis and the Secretion Level Improvement[J]. Journal of Food Science and Biotechnology,2020,39(11):34-40.

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  • Online: April 06,2021
  • Published: November 25,2020
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