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Mechanism and evolutionary divergence of a novel oxidized polyvinyl alcohol hydrolase in Stenotrophomonas rhizophila QL-P4
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  • Published: 27 January 2026

Mechanism and evolutionary divergence of a novel oxidized polyvinyl alcohol hydrolase in Stenotrophomonas rhizophila QL-P4

  • Yunheng Zhou1 na1,
  • Nomin Bold2 na1,
  • Jie Feng1 na1,
  • Chunyu Jia1,
  • Kerang Huang3,
  • Yiqing Yao4,
  • Ling Qiu4,
  • Shaolin Chen1,
  • Lili Huang5 &
  • …
  • Yahong Wei  ORCID: orcid.org/0000-0002-9533-53771 

Scientific Reports , Article number:  (2026) Cite this article

We are providing an unedited version of this manuscript to give early access to its findings. Before final publication, the manuscript will undergo further editing. Please note there may be errors present which affect the content, and all legal disclaimers apply.

Subjects

  • Biotechnology
  • Computational biology and bioinformatics
  • Microbiology

Abstract

Polyvinyl alcohol (PVA) is a widely used industrial polymer, and its persistence in the environment poses significant challenges, making the study of its biodegradation both a major production concern and an important scientific issue. This study aimed to elucidate the enzymatic mechanisms of PVA biodegradation by identifying and characterizing a novel oxidized polyvinyl alcohol hydrolase (OPH) from Stenotrophomonas rhizophila QL-P4, and to investigate its evolutionary divergence across microbial species. Through genomic analysis, we identified a gene, BAY15_0160 (996 bp), encoding a putative OPH. Its essential role in PVA degradation was confirmed via gene deletion, overexpression, and functional complementation assays. Site-directed mutagenesis demonstrated that the signal peptide and active site are indispensable for enzymatic function. The recombinant enzyme expressed in E. coli BL21(DE3) exhibited optimal specific activity (5.19 U/mg) at pH 7.0 and 30 °C, with a Michaelis constant (Km) of 0.1765 mM. Structural modeling and domain analysis revealed conserved catalytic features, which were further supported by simulated docking between the catalytic domain and substrate molecules. These results experimentally validate the functional importance of these domains. Furthermore, comparative sequence alignment with bacterial and fungal homologs uncovered a highly adapted fungal homolog, suggesting evolutionary divergence in OPH functionality. These findings provide a theoretical foundation for understanding PVA biodegradation mechanisms and developing microbial-based bioremediation strategies, while also demonstrating the potential of BAY15_0160 in environmental engineering applications—paving the way for designing efficient industrial microbial agents and enzyme preparations.

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Data availability

The S. rhizophila QL-P4 strain has been deposited in the China General Microbiological Culture Collection Center (CGMCC) under accession number CGMCC 1.15515 (https://www.cgmcc.net/resources/details?uuid=78f2e782-8ef2-11f0-94c6-78ac44479d74). The complete genome sequence of QL-P4 has been deposited in GenBank under accession number CP016294 (https://www.ncbi.nlm.nih.gov/nuccore/CP016294.1/).The coding sequence (CDS) of BAY15_0160 reported in this paper is available in the ENA database under accession number OZ389620 (http://www.ebi.ac.uk/ena/data/view/OZ389620).All homologous sequences used for comparative analysis were downloaded from public databases (NCBI https://www.ncbi.nlm.nih.gov/, UniProt https://www.uniprot.org/, and ENA https://www.ebi.ac.uk/). Their detailed accession numbers are provided in Figure S19. The chemical structures of the substrate pNPA (CID: 13243, https://pubchem.ncbi.nlm.nih.gov/compound/13243) and the PVA metabolic intermediate (CID: 3083375, https://pubchem.ncbi.nlm.nih.gov/compound/3083375) are available from the PubChem database.

Abbreviations

PVA:

Polyvinyl alcohol

CAGR:

Compound annual growth rate

OVA:

PVA/vinyl alcohol oligomer

OPH:

Oxidized polyvinyl alcohol hydrolase

PVADH:

Polyvinyl alcohol dehydrogenase

pNPA:

p-nitrophenyl acetate

V max :

Maximum velocity

K m :

Michaelis–Menten kinetic parameters

K cat :

Catalytic constant

PQQ:

Ppyrroloquinoline quinone

IPTG:

Isopropyl-β-D-thiogalactopyranoside

PAGE:

Polyacrylamide gel electrophoresis

BCA:

Bicinchoninic acid assay

NCBI:

National Center for Biotechnology Information

BLAST:

Basic Local Alignment Search Tool

BD-FAE:

Bifunctional domain- feruloyl and acetyl xylan esterase

MFS:

Major facility superfamily transporter

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Acknowledgements

The authors would like to thank the Life Science Research Core Services of NWAFU for their support.

Funding

This work was supported by the National Key R&D Program of China (2024YFD1700500), Agricultural Key-scientific and Core-technological Project of Shaanxi Province (2025NYGG011), Xianyang City Major Science, Technology Innovation Project (L2023-ZDKJ-CYJQ-NY-002) and Shaanxi Science and Technology Innovation Team Project (2025RS-CXTD-032). These funders had no role in the study design, data collection, and interpretation, or the decision to submit the work for publication.

Author information

Author notes

  1. These authors contributed equally: Yunheng Zhou, Nomin Bold and Jie Feng.

Authors and Affiliations

  1. State Key Laboratory for Crop Stress Resistance and High-Efficiency Production, College of Life Sciences, Biomass Energy Center for Arid and Semi-Arid Lands, Northwest A&F University, Yangling, 712100, Shaanxi, P. R. China

    Yunheng Zhou, Jie Feng, Chunyu Jia, Shaolin Chen & Yahong Wei

  2. Laboratory of Molecular Biology, Institute of Biology, Mongolian Academy of Sciences, Peace Avenue-54B, Bayanzurkh District, Ulaanbaatar, 13330, Mongolia

    Nomin Bold

  3. Life Science Research Core Services, Northwest A&F University, Yangling, 712100, Shaanxi, P. R. China

    Kerang Huang

  4. College of Mechanical and Electronic Engineering, The West Scientific Observing and Experimental Station of Rural Renewable Energy Exploitation and Utilization of the Ministry of Agriculture, Northwest A&F University, Yangling, 712100, Shaanxi, P. R. China

    Yiqing Yao & Ling Qiu

  5. State Key Laboratory for Crop Stress Resistance and High-Efficiency Production, College of Plant Protection, Northwest A&F University, Yangling, 712100, Shaanxi, P. R. China

    Lili Huang

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Contributions

Yunheng Zhou: Investigation, Writing – original draft. Nomin Bold: Investigation, Writing – original draft. Jie Feng: Conceptualization formal analysis. Chunyu Jia: Resources, Investigation. Kerang Huang: Investigation. Yiqing Yao: Data curation. Ling Qiu: Writing – review and editing. Shaolin Chen: Supervision, Writing – review & editing. Lili Huang: Supervision. Yahong Wei: Funding acquisition, Writing – review & editing.

Corresponding authors

Correspondence to Shaolin Chen, Lili Huang or Yahong Wei.

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Zhou, Y., Bold, N., Feng, J. et al. Mechanism and evolutionary divergence of a novel oxidized polyvinyl alcohol hydrolase in Stenotrophomonas rhizophila QL-P4. Sci Rep (2026). https://doi.org/10.1038/s41598-026-37715-4

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  • Received: 15 September 2025

  • Accepted: 23 January 2026

  • Published: 27 January 2026

  • DOI: https://doi.org/10.1038/s41598-026-37715-4

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Keywords

  • Polyvinyl alcohol biodegradation
  • Oxidized polyvinyl alcohol hydrolase
  • Gene function
  • Enzyme kinetics
  • Stenotrophomonas rhizophila
  • Bioremediation
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