Journal of Basic MicrobiologyMicrobiologyPeer-reviewed journal article
Characterization of Newly Discovered Polyester Polyurethane-degrading Methylobacterium Aquaticum Strain A1
Seong Hyeon LeeiD, Haemin Jeong, I Yeon Jung, Myounghyun Choi, Ah‐Ram KimiD
Abstract
In this study, we present Methylobacterium aquaticum A1, a novel strain capable of degrading polyester polyurethane (PE-PUR). The attachment of M. aquaticum A1 to PE-PUR and its degradation capabilities were verified using Scanning Electron Microscopy (SEM) and Fourier-Transform Infrared Spectroscopy (FT-IR). Analysis of the reference genome of M. aquaticum revealed genes encoding enzymes with potential PE-PUR degrading activity, including esterases, lipase, proteases and amidase such as tesA, pgpB, aes, aprE, lon, degQ, and gatA. An esterase activity assay using p-nitrophenyl acetate (p-NPA) showed increased ester bond-cleaving activity when M. aquaticum A1 was exposed to polyurethane diol (PU-diol), suggesting inducible enzymatic activity involved in PE-PUR degradation. These findings highlight the potential of M. aquaticum A1 as a promising biocatalyst for PE-PUR degradation. IMPORTANCEMicrobial biodegradation is increasingly recognized as a sustainable approach to addressing microplastic pollution. This study introduces M. aquaticum A1, a newly isolated strain capable of adhering to and degrading polyester polyurethane (PE-PUR), one of the most widely utilized plastics. To our knowledge, this is the first report of PE-PUR degradation by a member of the Methylobacterium genus. This paper provides a detailed characterization of M. aquaticum A1 and identifies several enzyme candidates--tesA, pgpB, aes, aprE, lon, degQ, and gatA--as potentially involved in the degradation process. Given that Methylobacterium species are known to be ecologically beneficial and inhabit diverse environments, the capacity of M. aquaticum A1 to degrade PE-PUR presents a promising strategy for mitigating microplastic pollution across a range of ecosystems.
- organism: bacteria (other)
- assay: proteomics
- research focus: host-pathogen & immune response
- approach: experimental assay
- Citations
- 3
- FWCI
- 0.71
- Field percentile
- top 38%
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