[논문]Production of extracellular PETase from Ideonella sakaiensis using sec-dependent signal peptides in E. coli

Seo, Hogyun; Kim, Seongmin; Son, Hyeoncheol Francis; Sagong, Hye-Young; Joo, Seongjoon; Kim, Kyung-Jin

doi:10.1016/j.bbrc.2018.11.087

Production of extracellular PETase from Ideonella sakaiensis using sec-dependent signal peptides in E. coli

Biochemical and biophysical research communications, v.508 no.1, 2019년, pp.250 - 255

Seo, Hogyun (School of Life Sciences, KNU Creative BioResearch Group, Kyungpook National University) , Kim, Seongmin (School of Life Sciences, KNU Creative BioResearch Group, Kyungpook National University) , Son, Hyeoncheol Francis (School of Life Sciences, KNU Creative BioResearch Group, Kyungpook National University) , Sagong, Hye-Young (School of Life Sciences, KNU Creative BioResearch Group, Kyungpook National University) , Joo, Seongjoon (School of Life Sciences, KNU Creative BioResearch Group, Kyungpook National University) , Kim, Kyung-Jin (School of Life Sciences, KNU Creative BioResearch Group, Kyungpook National University)

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Abstract Poly(ethylene terephthalate) (PET) is the most commonly used polyester polymer resin in fabrics and storage materials, and its accumulation in the environment is a global problem. The ability of PET hydrolase from Ideonella sakaiensis 201-F6 (IsPETase) to degrade PET at moderate temperatures has been studied extensively. However, due to its low structural stability and solubility, it is difficult to apply standard laboratory-level IsPETase expression and purification procedures in industry. To overcome this difficulty, the expression of IsPETase can be improved by using a secretion system. This is the first report on the production of an extracellular IsPETase, active against PET film, using Sec-dependent translocation signal peptides from E. coli. In this work, we tested the effects of fusions of the Sec-dependent and SRP-dependent signal peptides from E. coli secretory proteins into IsPETase, and successfully produced the extracellular enzyme using pET22b-SPMalE:IsPETase and pET22b-SPLamB:IsPETase expression systems. We also confirmed that the secreted IsPETase has PET-degradation activity. The work will be used for development of a new E. coli strain capable of degrading and assimilating PET in its culture medium. Highlights PETase from Ideonella sakaiensis (IsPETase) was successfully produced using the protein secretory expression system. Extracellular production of IsPETase is achieved by sec-dependent secretion system. The extracellularly produced IsPETase shows a PET degradation activity.

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Production of extracellular PETase from Ideonella sakaiensis using sec-dependent signal peptides in E. coli

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Production of extracellular PETase from Ideonella sakaiensis using sec-dependent signal peptides in E. coli

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