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Acinetobacter guillouiae, a lipolytic strain isolated from sludge capable of partially depolymerising polyethylene terephthalate : genomic, proteomic, and biochemical insights

Akhtar, Naheed ; Najjari, Afef ; Magnone, Anna ; Ceylan Yerebakan, Esma ; Bernfur, Katja LU ; Tullberg, Cecilia LU orcid ; Siddique Awan, Muhammad ; Majeed, Zahid ; Grey, Carl LU orcid and Zhang, Baozhong LU , et al. (2026) In BMC Microbiology 26(1).
Abstract

Acinetobacter guillouiae I-MWF was isolated by incubating amorphous polyethylene terephthalate (PET) film in sludge samples. The strain partially depolymerised PET powder with 11.3% crystallinity, as confirmed by FT-IR, HPLC-UV, and LC-MS analyses. Extracellular enzymes released terephthalic acid (TPA), mono(2-hydroxyethyl) terephthalate (MHET), and bis(2-hydroxyethyl) terephthalate (BHET). Genomic analysis identified 18 putative extracellular hydrolases, including lipases and esterases, each with a conserved catalytic triad. Proteomic profiling revealed expression of two triacylglycerol lipases and two additional lipase-family proteins when the strain was cultivated with PET or a PET-Tween 80 mixture. These enzymes were cloned in... (More)

Acinetobacter guillouiae I-MWF was isolated by incubating amorphous polyethylene terephthalate (PET) film in sludge samples. The strain partially depolymerised PET powder with 11.3% crystallinity, as confirmed by FT-IR, HPLC-UV, and LC-MS analyses. Extracellular enzymes released terephthalic acid (TPA), mono(2-hydroxyethyl) terephthalate (MHET), and bis(2-hydroxyethyl) terephthalate (BHET). Genomic analysis identified 18 putative extracellular hydrolases, including lipases and esterases, each with a conserved catalytic triad. Proteomic profiling revealed expression of two triacylglycerol lipases and two additional lipase-family proteins when the strain was cultivated with PET or a PET-Tween 80 mixture. These enzymes were cloned in Escherichia coli, but most formed insoluble, inactive inclusion bodies, and one was not expressed. Molecular modelling highlighted structural features likely to influence their catalytic interaction with PET. Although the strain partially depolymerised PET powder, it was unable to grow on PET, TPA, or ethylene glycol, indicating that PET depolymerisation occurs as a side activity rather than supporting growth. Instead, A. guillouiae displayed strong lipolytic activity and a clear preference for lipid-based substrates, achieving its highest growth with Tween 80. A lipid transporter was also expressed under these conditions, suggesting adaptation to hydrocarbon-rich environments. These findings indicate that A. guillouiae I-MWF can mediate partial PET depolymerisation without assimilating the resulting monomers, while preferentially growing on lipid-like substrates.

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type
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publication status
published
subject
keywords
Acinetobacter/isolation & purification, Polyethylene Terephthalates/metabolism, Sewage/microbiology, Lipase/genetics, Proteomics, Genomics, Lipolysis, Proteome/analysis, Spectroscopy, Fourier Transform Infrared, Escherichia coli/genetics, Esterases/genetics, Cloning, Molecular, Models, Molecular
in
BMC Microbiology
volume
26
issue
1
article number
763
publisher
BioMed Central (BMC)
external identifiers
  • pmid:42649483
ISSN
1471-2180
DOI
10.1186/s12866-026-05567-7
language
English
LU publication?
yes
id
0dbcf534-7e81-4a1d-b084-de1e7ccc7a61
date added to LUP
2026-08-21 19:06:53
date last changed
2026-08-31 08:03:59
@article{0dbcf534-7e81-4a1d-b084-de1e7ccc7a61,
  abstract     = {{<p>Acinetobacter guillouiae I-MWF was isolated by incubating amorphous polyethylene terephthalate (PET) film in sludge samples. The strain partially depolymerised PET powder with 11.3% crystallinity, as confirmed by FT-IR, HPLC-UV, and LC-MS analyses. Extracellular enzymes released terephthalic acid (TPA), mono(2-hydroxyethyl) terephthalate (MHET), and bis(2-hydroxyethyl) terephthalate (BHET). Genomic analysis identified 18 putative extracellular hydrolases, including lipases and esterases, each with a conserved catalytic triad. Proteomic profiling revealed expression of two triacylglycerol lipases and two additional lipase-family proteins when the strain was cultivated with PET or a PET-Tween 80 mixture. These enzymes were cloned in Escherichia coli, but most formed insoluble, inactive inclusion bodies, and one was not expressed. Molecular modelling highlighted structural features likely to influence their catalytic interaction with PET. Although the strain partially depolymerised PET powder, it was unable to grow on PET, TPA, or ethylene glycol, indicating that PET depolymerisation occurs as a side activity rather than supporting growth. Instead, A. guillouiae displayed strong lipolytic activity and a clear preference for lipid-based substrates, achieving its highest growth with Tween 80. A lipid transporter was also expressed under these conditions, suggesting adaptation to hydrocarbon-rich environments. These findings indicate that A. guillouiae I-MWF can mediate partial PET depolymerisation without assimilating the resulting monomers, while preferentially growing on lipid-like substrates.</p>}},
  author       = {{Akhtar, Naheed and Najjari, Afef and Magnone, Anna and Ceylan Yerebakan, Esma and Bernfur, Katja and Tullberg, Cecilia and Siddique Awan, Muhammad and Majeed, Zahid and Grey, Carl and Zhang, Baozhong and Linares-Pastén, Javier A.}},
  issn         = {{1471-2180}},
  keywords     = {{Acinetobacter/isolation & purification; Polyethylene Terephthalates/metabolism; Sewage/microbiology; Lipase/genetics; Proteomics; Genomics; Lipolysis; Proteome/analysis; Spectroscopy, Fourier Transform Infrared; Escherichia coli/genetics; Esterases/genetics; Cloning, Molecular; Models, Molecular}},
  language     = {{eng}},
  month        = {{08}},
  number       = {{1}},
  publisher    = {{BioMed Central (BMC)}},
  series       = {{BMC Microbiology}},
  title        = {{Acinetobacter guillouiae, a lipolytic strain isolated from sludge capable of partially depolymerising polyethylene terephthalate : genomic, proteomic, and biochemical insights}},
  url          = {{http://dx.doi.org/10.1186/s12866-026-05567-7}},
  doi          = {{10.1186/s12866-026-05567-7}},
  volume       = {{26}},
  year         = {{2026}},
}