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Discovery and engineering of cold-active lipases facilitating the biodegradation of poly(ε-caprolactone) and polyurethane from the functional mixed genomic library.

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Title: Discovery and engineering of cold-active lipases facilitating the biodegradation of poly(ε-caprolactone) and polyurethane from the functional mixed genomic library.
Authors: Jeong C; Division of Life Sciences, Korea Polar Research Institute, Incheon, 21990, South Korea; Department of Polar Sciences, University of Science and Technology, Incheon, 21990, South Korea., Yu SH; Division of Life Sciences, Korea Polar Research Institute, Incheon, 21990, South Korea; Department of Polar Sciences, University of Science and Technology, Incheon, 21990, South Korea., Won SJ; Division of Life Sciences, Korea Polar Research Institute, Incheon, 21990, South Korea., Kim JH; Division of Life Sciences, Korea Polar Research Institute, Incheon, 21990, South Korea., Choi W; Division of Life Sciences, Korea Polar Research Institute, Incheon, 21990, South Korea., Lee YM; Division of Life Sciences, Korea Polar Research Institute, Incheon, 21990, South Korea., Shin SC; Division of Life Sciences, Korea Polar Research Institute, Incheon, 21990, South Korea., Kim HW; Division of Life Sciences, Korea Polar Research Institute, Incheon, 21990, South Korea; Department of Polar Sciences, University of Science and Technology, Incheon, 21990, South Korea. Electronic address: hwkim@kopri.re.kr.
Source: International journal of biological macromolecules [Int J Biol Macromol] 2026 Sep; Vol. 374, pp. 153331. Date of Electronic Publication: 2026 Jul 03.
Publication Type: Journal Article
Language: English
Journal Info: Publisher: Elsevier Country of Publication: Netherlands NLM ID: 7909578 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1879-0003 (Electronic) Linking ISSN: 01418130 NLM ISO Abbreviation: Int J Biol Macromol Subsets: MEDLINE
Imprint Name(s): Publication: Amsterdam : Elsevier
Original Publication: Guildford, Eng., IPC Science and Technology Press.
MeSH Terms: Lipase*/genetics , Lipase*/chemistry , Lipase*/metabolism , Polyesters*/metabolism , Polyesters*/chemistry , Polyurethanes*/metabolism , Polyurethanes*/chemistry , Cold Temperature* , Protein Engineering* , Gene Library*, Biodegradation, Environmental ; Amino Acid Sequence ; Models, Molecular
Abstract: Plastic pollution has become a serious environmental issue, leading to increased research efforts toward the development of biodegradable plastics. Poly(ε-caprolactone) (PCL) is a representative biodegradable polymer. PCL-based materials such as polyurethane (PU) still require long periods for degradation and consequently accumulate in the environment. The biopolymer degradation occurs through the hydrolysis of ester bonds, which can be significantly accelerated by enzymes such as esterases, cutinases, and lipases. Cold-active lipolytic enzymes isolated from extreme environments are promising candidates for various industrial and environmental applications. Accordingly, polar and alpine microbial strains were used as enzyme sources. Therefore, we aimed to elucidate the structural determinants of the catalytic efficiency of these enzymes against PCL and PU. Five cold-active lipases were identified in a fosmid library comprising bacterial genomic DNAs from 3062 strains, derived from the Polar and Alpine Microbial Collection (PAMC). These enzymes have homologous sequences between them and exhibited high lipolytic activity against plant oils. In particular, the enzymes PLI 131 and PLI 137 exhibited considerable activity against PCL and PU. A mutational analysis based on the protein structure model was performed using PLI 137 to improve the degrading activity against PCL and PU. These results suggest that specific loop regions near the lid domain of the protein are involved in the interactions with the PCL substrate. The alanine residue mutant in the loop also showed approximately two-fold greater activity against PCL. This study highlights the potential of cold-active lipases as eco-friendly biocatalysts for plastic biodegradation.
(Copyright © 2026. Published by Elsevier B.V.)
Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
Contributed Indexing: Keywords: Cold-active enzyme; Lipase; Plastic biodegradation; Pseudomonas
Substance Nomenclature: EC 3.1.1.3 (Lipase)
0 (Polyesters)
0 (Polyurethanes)
24980-41-4 (polycaprolactone)
Entry Date(s): Date Created: 20260703 Date Completed: 20260821 Latest Revision: 20260821
Update Code: 20260821
DOI: 10.1016/j.ijbiomac.2026.153331
PMID: 42398602
Database: MEDLINE
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  Data: Discovery and engineering of cold-active lipases facilitating the biodegradation of poly(ε-caprolactone) and polyurethane from the functional mixed genomic library.
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  Data: <searchLink fieldCode="AU" term="%22Jeong+C%22">Jeong C</searchLink>; Division of Life Sciences, Korea Polar Research Institute, Incheon, 21990, South Korea; Department of Polar Sciences, University of Science and Technology, Incheon, 21990, South Korea.<br /><searchLink fieldCode="AU" term="%22Yu+SH%22">Yu SH</searchLink>; Division of Life Sciences, Korea Polar Research Institute, Incheon, 21990, South Korea; Department of Polar Sciences, University of Science and Technology, Incheon, 21990, South Korea.<br /><searchLink fieldCode="AU" term="%22Won+SJ%22">Won SJ</searchLink>; Division of Life Sciences, Korea Polar Research Institute, Incheon, 21990, South Korea.<br /><searchLink fieldCode="AU" term="%22Kim+JH%22">Kim JH</searchLink>; Division of Life Sciences, Korea Polar Research Institute, Incheon, 21990, South Korea.<br /><searchLink fieldCode="AU" term="%22Choi+W%22">Choi W</searchLink>; Division of Life Sciences, Korea Polar Research Institute, Incheon, 21990, South Korea.<br /><searchLink fieldCode="AU" term="%22Lee+YM%22">Lee YM</searchLink>; Division of Life Sciences, Korea Polar Research Institute, Incheon, 21990, South Korea.<br /><searchLink fieldCode="AU" term="%22Shin+SC%22">Shin SC</searchLink>; Division of Life Sciences, Korea Polar Research Institute, Incheon, 21990, South Korea.<br /><searchLink fieldCode="AU" term="%22Kim+HW%22">Kim HW</searchLink>; Division of Life Sciences, Korea Polar Research Institute, Incheon, 21990, South Korea; Department of Polar Sciences, University of Science and Technology, Incheon, 21990, South Korea. Electronic address: hwkim@kopri.re.kr.
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  Data: <i>Publisher: </i><searchLink fieldCode="PB" term="%22Elsevier%22">Elsevier </searchLink><i>Country of Publication: </i>Netherlands <i>NLM ID: </i>7909578 <i>Publication Model: </i>Print-Electronic <i>Cited Medium: </i>Internet <i>ISSN: </i>1879-0003 (Electronic) <i>Linking ISSN: </i><searchLink fieldCode="IS" term="%2201418130%22">01418130 </searchLink><i>NLM ISO Abbreviation: </i>Int J Biol Macromol <i>Subsets: </i>MEDLINE
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  Data: <i>Publication</i>: Amsterdam : Elsevier<br /><i>Original Publication</i>: Guildford, Eng., IPC Science and Technology Press.
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  Data: <searchLink fieldCode="MM" term="%22Lipase%22">Lipase*</searchLink>/<searchLink fieldCode="MM" term="%22Lipase+genetics%22">genetics</searchLink> <br /><searchLink fieldCode="MM" term="%22Lipase%22">Lipase*</searchLink>/<searchLink fieldCode="MM" term="%22Lipase+chemistry%22">chemistry</searchLink> <br /><searchLink fieldCode="MM" term="%22Lipase%22">Lipase*</searchLink>/<searchLink fieldCode="MM" term="%22Lipase+metabolism%22">metabolism</searchLink> <br /><searchLink fieldCode="MM" term="%22Polyesters%22">Polyesters*</searchLink>/<searchLink fieldCode="MM" term="%22Polyesters+metabolism%22">metabolism</searchLink> <br /><searchLink fieldCode="MM" term="%22Polyesters%22">Polyesters*</searchLink>/<searchLink fieldCode="MM" term="%22Polyesters+chemistry%22">chemistry</searchLink> <br /><searchLink fieldCode="MM" term="%22Polyurethanes%22">Polyurethanes*</searchLink>/<searchLink fieldCode="MM" term="%22Polyurethanes+metabolism%22">metabolism</searchLink> <br /><searchLink fieldCode="MM" term="%22Polyurethanes%22">Polyurethanes*</searchLink>/<searchLink fieldCode="MM" term="%22Polyurethanes+chemistry%22">chemistry</searchLink> <br /><searchLink fieldCode="MM" term="%22Cold+Temperature%22">Cold Temperature*</searchLink> <br /><searchLink fieldCode="MM" term="%22Protein+Engineering%22">Protein Engineering*</searchLink> <br /><searchLink fieldCode="MM" term="%22Gene+Library%22">Gene Library*</searchLink><br /><searchLink fieldCode="MH" term="%22Biodegradation%2C+Environmental%22">Biodegradation, Environmental</searchLink> ; <searchLink fieldCode="MH" term="%22Amino+Acid+Sequence%22">Amino Acid Sequence</searchLink> ; <searchLink fieldCode="MH" term="%22Models%2C+Molecular%22">Models, Molecular</searchLink>
– Name: Abstract
  Label: Abstract
  Group: Ab
  Data: Plastic pollution has become a serious environmental issue, leading to increased research efforts toward the development of biodegradable plastics. Poly(ε-caprolactone) (PCL) is a representative biodegradable polymer. PCL-based materials such as polyurethane (PU) still require long periods for degradation and consequently accumulate in the environment. The biopolymer degradation occurs through the hydrolysis of ester bonds, which can be significantly accelerated by enzymes such as esterases, cutinases, and lipases. Cold-active lipolytic enzymes isolated from extreme environments are promising candidates for various industrial and environmental applications. Accordingly, polar and alpine microbial strains were used as enzyme sources. Therefore, we aimed to elucidate the structural determinants of the catalytic efficiency of these enzymes against PCL and PU. Five cold-active lipases were identified in a fosmid library comprising bacterial genomic DNAs from 3062 strains, derived from the Polar and Alpine Microbial Collection (PAMC). These enzymes have homologous sequences between them and exhibited high lipolytic activity against plant oils. In particular, the enzymes PLI 131 and PLI 137 exhibited considerable activity against PCL and PU. A mutational analysis based on the protein structure model was performed using PLI 137 to improve the degrading activity against PCL and PU. These results suggest that specific loop regions near the lid domain of the protein are involved in the interactions with the PCL substrate. The alanine residue mutant in the loop also showed approximately two-fold greater activity against PCL. This study highlights the potential of cold-active lipases as eco-friendly biocatalysts for plastic biodegradation.<br /> (Copyright © 2026. Published by Elsevier B.V.)
– Name: Abstract
  Label: Competing Interests
  Group: Ab
  Data: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
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  Data: <i>Keywords: </i>Cold-active enzyme; Lipase; Plastic biodegradation; Pseudomonas
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  Data: EC 3.1.1.3 (Lipase)<br />0 (Polyesters)<br />0 (Polyurethanes)<br />24980-41-4 (polycaprolactone)
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        Value: 10.1016/j.ijbiomac.2026.153331
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      – Code: eng
        Text: English
    PhysicalDescription:
      Pagination:
        StartPage: 153331
    Subjects:
      – SubjectFull: Biodegradation, Environmental
        Type: general
      – SubjectFull: Amino Acid Sequence
        Type: general
      – SubjectFull: Models, Molecular
        Type: general
      – SubjectFull: Lipase genetics
        Type: general
      – SubjectFull: Lipase chemistry
        Type: general
      – SubjectFull: Lipase metabolism
        Type: general
      – SubjectFull: Polyesters metabolism
        Type: general
      – SubjectFull: Polyesters chemistry
        Type: general
      – SubjectFull: Polyurethanes metabolism
        Type: general
      – SubjectFull: Polyurethanes chemistry
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      – SubjectFull: Cold Temperature
        Type: general
      – SubjectFull: Protein Engineering
        Type: general
      – SubjectFull: Gene Library
        Type: general
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      – TitleFull: Discovery and engineering of cold-active lipases facilitating the biodegradation of poly(ε-caprolactone) and polyurethane from the functional mixed genomic library.
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              Text: 2026 Sep
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