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The s-oph enzyme for efficient degradation of polyvinyl alcohol: soluble expression and catalytic properties

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Abstract

Background

Polyvinyl alcohol (PVA) is one of the most widely used water-soluble polymers with remarkable mechanical properties. However, water-soluble polymers are among the major organic pollutants of streams, river, and marine ecosystems. Once dispersed in aqueous systems, they can directly interfere with the life cycle of aquatic organisms via direct toxic effects. There is thus an urgent need for microorganisms or enzymes that can efficiently degrade them. Oxidized PVA hydrolase plays an important role in the pathway of PVA biodegradation. It is the key enzyme in the second step of the pathway for complete degradation of PVA.

Methods and results

The s-oph gene was cloned from the laboratory-isolated strain Sphingopyxis sp. M19. This gene was expressed in the Escherichia coli system pET32a/s-oph expression vector, with the products forming an inclusion body. By binding with a molecular chaperone, pET32a/s-oph/BL21 (DE3)/pGro7 was successfully constructed, which enabled the s-oph gene to be solubly expressed in E. coli. The protein encoded by the s-oph gene was purified at a yield of 16.8 mg L−1, and its catalytic activity reached 852.71 U mg−1. In the s-oph enzyme reaction system, the efficiency of PVA degradation was increased to 233.5% compared with that of controls.

Conclusions

The s-oph enzyme exhibited the characteristics of being able to degrade PVA with high efficiency, specificity, and stability. This enzyme has good potential for practical application in ameliorating plastic pollution and protecting the environment.

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Data Availability

The datasets supporting the conclusions of this article are included within the article and its additional files.

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Acknowledgements

The authors would like to express their deep gratitude to publishers for providing publication support for this work. We also thank NES Institution (http://www.nesediting.com/) for editing the language of a draft of the manuscript.

Funding

This study was supported by Joint Funds of the National Natural Science Foundation of China (Grant number: U1301231).

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Authors and Affiliations

  1. School of Biology and Biological Engineering, South China University of Technology, Guangzhou Higher Education Mega Center, Panyu District, Guangzhou, 510006, China

    Xinyu Wang, Jiaxuan Li, Xiaoshan Lin & Yi Zhang

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  1. Xinyu Wang
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  2. Jiaxuan Li
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Contributions

All authors contributed to the study conception and design. Material preparation, data collection and analysis were performed by Xinyu Wang and Jiaxuan Li. Xiaoshan Lin was responsible for the procurement of laboratory reagents. The first draft of the manuscript was written by Xinyu Wang, Yi Zhang modified the manuscript and all authors commented on previous versions of the manuscript. All authors read and approved the final manuscript.

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Correspondence to Yi Zhang.

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Wang, X., Li, J., Lin, X. et al. The s-oph enzyme for efficient degradation of polyvinyl alcohol: soluble expression and catalytic properties. Mol Biol Rep 50, 8523–8535 (2023). https://doi.org/10.1007/s11033-023-08712-x

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