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<p>Lignin, the second most abundant natural polymer on Earth after cellulose, is highly resistant to degradation, particularly in cold environments. In this study, a psychrotolerant bacterial strain, <i>Psychrobacter faecalis</i> CLB018, was isolated from the gut microbiota of the Antarctic fish <i>Trematomus bernacchii</i> near Zhongshan Station, Antarctica, using lignin as the sole carbon source at 4&#xa0;℃. Strain CLB018 exhibited high-efficiency lignin degradation, achieving a 40.39% degradation rate within 120&#xa0;h at 10&#xa0;℃. It also demonstrated robust enzymic activities, producing lignin peroxidase (284 U/L at 48&#xa0;h), laccase (111.9 U/L at 24&#xa0;h), and manganese peroxidase (41.7 U/L at 48&#xa0;h), essential for converting lignin into soluble aromatic compounds. Furthermore, CLB018 displayed versatility in utilizing diverse carbon source, including proteins, carboxylates, lipids, and aromatic compounds. Genomic analysis revealed the presence of genes encoding osmoprotectant transporters, cold shock proteins, an antioxidant system, and trehalose synthesis capability, which enhance its cold adaptation. These findings demonstrate that CLB018 possesses efficient lignin-degrading capabilities at low temperatures, highlighting its potential for sustainable biotechnological applications in cold environments.</p>

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Lignin degradation, metabolic profiling, and cold adaptation of Psychrobacter strain CLB018 isolated from the Antarctic fish Trematomus bernacchii

  • 期刊论文

  • 发表日期：

    2026年1月14日

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  • Wanying Zhai,
  • Hao Li,
  • Mingli Liu,
  • Lingjing Li,
  • Ziqin Wang,
  • Qianting Chen,
  • Jiahua Wang,
  • Liangbiao Chen

摘要

Lignin, the second most abundant natural polymer on Earth after cellulose, is highly resistant to degradation, particularly in cold environments. In this study, a psychrotolerant bacterial strain, Psychrobacter faecalis CLB018, was isolated from the gut microbiota of the Antarctic fish Trematomus bernacchii near Zhongshan Station, Antarctica, using lignin as the sole carbon source at 4 ℃. Strain CLB018 exhibited high-efficiency lignin degradation, achieving a 40.39% degradation rate within 120 h at 10 ℃. It also demonstrated robust enzymic activities, producing lignin peroxidase (284 U/L at 48 h), laccase (111.9 U/L at 24 h), and manganese peroxidase (41.7 U/L at 48 h), essential for converting lignin into soluble aromatic compounds. Furthermore, CLB018 displayed versatility in utilizing diverse carbon source, including proteins, carboxylates, lipids, and aromatic compounds. Genomic analysis revealed the presence of genes encoding osmoprotectant transporters, cold shock proteins, an antioxidant system, and trehalose synthesis capability, which enhance its cold adaptation. These findings demonstrate that CLB018 possesses efficient lignin-degrading capabilities at low temperatures, highlighting its potential for sustainable biotechnological applications in cold environments.