ArticleApplied and environmental microbiology2013
Extracellular location of Thermobifida fusca cutinase expressed in Escherichia coli BL21(DE3) without mediation of a signal peptide.
Article in Applied and environmental microbiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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26 citing papers in PubMed, 76 citations in OpenAlex.
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- High-Level Expression of Humicola insolens Cutinase in Bacillus subtilis.Applied biochemistry and biotechnology · 2025Article
- EngineeringInternational journal of molecular sciences · 2025Review
- Metabolomic and Genomic Analysis of Bioactive Compounds of Phacidium infestans Karsten DSM 5139 Cultivated on Pinus sylvestris Needles.Environmental microbiology reports · 2025Article
- Article
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- Efficient Expression and Characterization of an Endo-Type Lyase HCLase_M28 and Its Gradual Scale-Up Fermentation for the Preparation of Chondroitin Sulfate Oligosaccharides.Applied biochemistry and biotechnology · 2024Article
- Direct Screening of PET Hydrolase Activity in Culture Medium Based on Turbidity Reduction.ACS omega · 2024Article
- Bioengineering Comamonas testosteroni CNB-1: a robust whole-cell biocatalyst for efficient PET microplastic degradation.Bioresources and bioprocessing · 2023Article
- Valorization of Polyethylene Terephthalate to Muconic Acid by EngineeringInternational journal of molecular sciences · 2022Article
- Expression of a Cutinase ofMicrobiology spectrum · 2021Article
- Perspectives on the Role of Enzymatic Biocatalysis for the Degradation of Plastic PET.International journal of molecular sciences · 2021Review
- The N-terminus of Lactobacillus amylovorus feruloyl esterase plays an important role in its secretion by Lactobacillus plantarum and Escherichia coli.Microbial cell factories · 2021Article
- "Applied and environmental microbiology · 2021Article
- Engineering Microbes to Bio-Upcycle Polyethylene Terephthalate.Frontiers in bioengineering and biotechnology · 2021Review
- Comparison of Enzyme Secretion and Ferulic Acid Production byFrontiers in microbiology · 2020Article
- Enzymatic Degradation of p-Nitrophenyl Esters, Polyethylene Terephthalate, Cutin, and Suberin by Sub1, a Suberinase Encoded by the Plant Pathogen Streptomyces scabies.Microbes and environments · 2020Article
- Enhanced production of heterologous proteins via engineering the cell surface of Bacillus licheniformis.Journal of industrial microbiology & biotechnology · 2019Article
- Current knowledge on enzymatic PET degradation and its possible application to waste stream management and other fields.Applied microbiology and biotechnology · 2019Review
- Secretion of recombinant proteins fromEngineering in life sciences · 2018Review
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cutinase is a multifunctional esterase with potential industrial applications. In the present study, a truncated version of the extracellular Thermobifida fusca cutinase without a signal peptide (referred to as cutinase(NS)) was heterologously expressed in Escherichia coli BL21(DE3). The results showed that the majority of the cutinase activity was located in the culture medium. In a 3-liter fermentor, the cutinase activity in the culture medium reached 1,063.5 U/ml (2,380.8 mg/liter), and the productivity was 40.9 U/ml/h. Biochemical characterization of the purified cutinase(NS) showed that it has enzymatic properties similar to those of the wild-type enzyme. In addition, E. coli cells producing inactive cutinase(NS)S130A were constructed, and it was found that the majority of the inactive enzyme was located in the cytoplasm. Furthermore, T. fusca cutinase was confirmed to have hydrolytic activity toward phospholipids, an important component of the cell membrane. Compared to the cells expressing the inactive cutinase(NS)S130A, the cells expressing cutinase(NS) showed increased membrane permeability and irregular morphology. Based on these results, a hypothesis of "cell leakage induced by the limited phospholipid hydrolysis of cutinase(NS)" was proposed to explain the underlying mechanism for the extracellular release of cutinase(NS).
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