Complete bio-degradation of poly(butylene adipate-co-terephthalate) via engineered cutinases

Yu Yang, Jian Min, Ting Xue, Pengcheng Jiang, Xin Liu, Rouming Peng, Jian-Wen Huang, Yingying Qu, Xian Li, Ning Ma, Fang-Chang Tsai, Longhai Dai, Qi Zhang, Yingle Liu (), Chun-Chi Chen () and Rey-Ting Guo ()
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Yu Yang: Hubei University
Jian Min: Hubei University
Ting Xue: Hubei University
Pengcheng Jiang: Hubei University
Xin Liu: Hubei University
Rouming Peng: Hubei University
Jian-Wen Huang: Hubei University
Yingying Qu: Hubei University
Xian Li: Hubei University
Ning Ma: Hubei University
Fang-Chang Tsai: Hubei University
Longhai Dai: Hubei University
Qi Zhang: Wuhan University
Yingle Liu: Wuhan University
Chun-Chi Chen: Hubei University
Rey-Ting Guo: Hubei University

Nature Communications, 2023, vol. 14, issue 1, 1-8

Abstract: Abstract Poly(butylene adipate-co-terephthalate) (PBAT), a polyester made of terephthalic acid (TPA), 1,4-butanediol, and adipic acid, is extensively utilized in plastic production and has accumulated globally as environmental waste. Biodegradation is an attractive strategy to manage PBAT, but an effective PBAT-degrading enzyme is required. Here, we demonstrate that cutinases are highly potent enzymes that can completely decompose PBAT films in 48 h. We further show that the engineered cutinases, by applying a double mutation strategy to render a more flexible substrate-binding pocket exhibit higher decomposition rates. Notably, these variants produce TPA as a major end-product, which is beneficial feature for the future recycling economy. The crystal structures of wild type and double mutation of a cutinase from Thermobifida fusca in complex with a substrate analogue are also solved, elucidating their substrate-binding modes. These structural and biochemical analyses enable us to propose the mechanism of cutinase-mediated PBAT degradation.

Date: 2023
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DOI: 10.1038/s41467-023-37374-3

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