Theoretical calculation on degradation mechanism of novel copolyesters under CALB enzyme.

Poly(butylene succinate-co-furandicarboxylate) (PBSF) and poly(butylene adipate-co-furandicarboxylate) (PBAF) are novel furandicarboxylic acid-based biodegradable copolyesters with great potential to replace fossil-derived terephthalic acid-based copolyesters such as poly(butylene succinate-co-terep...

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Bibliographic Details
Published in:Journal of Environmental Sciences
Main Authors: Ren, Yuanyang, Cheng, Zhiwen, Cheng, Luwei, Liu, Yawei, Li, Mingyue, Yuan, Tao, Shen, Zhemin
Format: Article in Journal/Newspaper
Language:English
Published: Elsevier Science 2025
Subjects:
Candida antarctica lipase B
Degradation mechanism
Poly(butylene adipate-co-furandicarboxylate)
Poly(butylene succinate-co-furandicarboxylate)
Site-directed mutations
Antarc*
Antarctica
Online Access:https://doi.org/10.1016/j.jes.2023.12.018
https://pubmed.ncbi.nlm.nih.gov/39181639
Description
Summary:Poly(butylene succinate-co-furandicarboxylate) (PBSF) and poly(butylene adipate-co-furandicarboxylate) (PBAF) are novel furandicarboxylic acid-based biodegradable copolyesters with great potential to replace fossil-derived terephthalic acid-based copolyesters such as poly(butylene succinate-co-terephthalate) (PBST) and poly(butylene adipate-co-terephthalate) (PBAT). In this study, quantum chemistry techniques after molecular dynamics simulations are employed to investigate the degradation mechanism of PBSF and PBAF catalyzed by Candida antarctica lipase B (CALB). Computational analysis indicates that the catalytic reaction follows a four-step mechanism resembling the ping-pong bibi mechanism, with the initial two steps being acylation reactions and the subsequent two being hydrolysis reactions. Notably, the first step of the hydrolysis is identified as the rate-determining step. Moreover, by introducing single-point mutations to expand the substrate entrance tunnel, the catalytic distance of the first acylation step decreases. Additionally, energy barrier of the rate-determining step is decreased in the PBSF system by site-directed mutations on key residues increasing hydrophobicity of the enzyme's active site. This study unprecedently show the substrate binding pocket and hydrophobicity of the enzyme's active site have the potential to be engineered to enhance the degradation of copolyesters catalyzed by CALB.

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