Structure Report for: 7XTW

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, Rey-Ting Guo

Title: Complete bio-degradation of poly(butylene adipate-co-terephthalate) via engineered cutinases
Yang Y, Min J, Xue T, Jiang P, Liu X, Peng R, Huang JW, Qu Y, Li X and Guo RT <6 more author(s)> Yang Y, Min J, Xue T, Jiang P, Liu X, Peng R, Huang JW, Qu Y, Li X, Ma N, Tsai FC, Dai L, Zhang Q, Liu Y, Chen CC, Guo RT (- 6)
Ref: Nat Commun, 14:1645, 2023 : PubMed
Abstract


ESTHER: Yang_2023_Nat.Commun_14_1645
PubMedSearch: Yang 2023 Nat.Commun 14 1645
PubMedID: 36964144
Gene_locus related to this paper: idesa-peth, thefu-q6a0i4
Inhibitor(s) related to this paper: Terephthalic-acid, MHET

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.