Journal
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Volume 66, Issue 50, Pages 13217-13227Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.jafc.8b05038
Keywords
polyethylene terephthalate hydrolase; twin-arginine signal peptide; Tat-independent pathway; Bacillus subtilis 168
Funding
- National Natural Science Foundation of China [31770075, 31170117]
- Science & Technology Projects of Guangzhou [201804010285]
- China Postdoctoral Science Foundation [2017M622859]
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Widespread utilization of polyethylene terephthalate (PET) has caused critical environmental pollution. The enzymatic degradation of PET is a promising solution to this problem. In this study, PETase, which exhibits much higher PET-hydrolytic activity than other enzymes, was successfully secreted into extracellular milieu from Bacillus subtilis 168 under the direction of its native signal peptide (named SPPETase). SPPETase is predicted to be a twin-arginine signal peptide. Intriguingly, inactivation of twin-arginine translocation (Tat) complexes improved the secretion amount by 3.8-fold, indicating that PETase was exported via Tat-independent pathway. To the best of our knowledge, this is the first report on the improvement of Tat-independent secretion by inactivating Tat components of B. subtilis 168 in LB medium. Furthermore, PET film degradation assay showed that the secreted PETase was fully active. This study paves the first step to construct an efficient engineered strain for PET degradation.
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