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Biodegradable plastic-degrading enzyme from Pseudozyma antarctica: cloning, sequencing, and characterization

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Abstract

Pseudozyma antarctica JCM 10317 exhibits a strong degradation activity for biodegradable plastics (BPs) such as agricultural mulch films composed of poly(butylene succinate) (PBS) and poly(butylene succinate-co-adipate) (PBSA). An enzyme named PaE was isolated and the gene encoding PaE was cloned from the strain by functional complementation in Saccharomyces cerevisiae. The deduced amino acid sequence of PaE contains 198 amino acids with a predicted molecular weight of 20,362.41. High identity was observed between this sequence and that of cutinase-like enzymes (CLEs) (61–68 %); therefore, the gene encoding PaE was named PaCLE1. The specific activity of PaE against emulsified PBSA was 54.8 ± 6.3 U/mg. In addition to emulsified BPs, PaE degraded solid films of PBS, PBSA, poly(ε-caprolactone), and poly(lactic acid).

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Acknowledgments

We thank Showa Denko K. K. for generously supplying all the Bionolle materials (PBS and PBSA), Toyota Motor Co. Ltd. for generously supplying the PLA pellet, and Dr. Elvila Suto for proofreading of the manuscript. This research was financially supported by the Ministry of the Environment, KAKENHI (235658083), and the National Institute for Agro-Environmental Sciences, Japan.

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Correspondence to Hiroko K. Kitamoto.

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Shinozaki, Y., Morita, T., Cao, Xh. et al. Biodegradable plastic-degrading enzyme from Pseudozyma antarctica: cloning, sequencing, and characterization. Appl Microbiol Biotechnol 97, 2951–2959 (2013). https://doi.org/10.1007/s00253-012-4188-8

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  • DOI: https://doi.org/10.1007/s00253-012-4188-8

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