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Issue 12, 2020
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Biodegradation mechanism of polycaprolactone by a novel esterase MGS0156: a QM/MM approach

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Abstract

Nowadays micro-plastic pollution has become one of the most serious global environmental problems. A potential strategy in managing micro-plastic waste is enzyme-catalyzed degradation. MGS0156 is a hydrolase screened from environmental metagenomes, which can efficiently degrade commercial plastics such as polycaprolactone, polylactide, etc. Here a combined molecular dynamics, molecular mechanics Poisson–Boltzmann surface area, and quantum mechanics/molecular mechanism method was used to reveal the enzymatic depolymerization mechanism. By systematically analyzing the binding processes of nine oligomers (from a monomer to tetramer), we found that longer oligomers have relatively stronger binding energy. The degradation process involves two concerted elementary steps: triad-assisted nucleophilic attack and C–O bond cleavage. C–O bond cleavage is the rate determining step with an average barrier of 15.7 kcal mol−1, which is consistent with the experimentally determined kcat (1101 s−1, corresponds to 13.3 kcal mol−1). The electrostatic influence analysis of twenty amino acids highlights His231 and Asp237 as potential mutation targets for designing more efficient MGS0156 mutants.

Graphical abstract: Biodegradation mechanism of polycaprolactone by a novel esterase MGS0156: a QM/MM approach

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Supplementary files

Article information


Submitted
07 Aug 2020
Accepted
05 Oct 2020
First published
07 Oct 2020

Environ. Sci.: Processes Impacts, 2020,22, 2332-2344
Article type
Paper

Biodegradation mechanism of polycaprolactone by a novel esterase MGS0156: a QM/MM approach

S. Feng, Y. Yue, J. Chen, J. Zhou, Y. Li and Q. Zhang, Environ. Sci.: Processes Impacts, 2020, 22, 2332
DOI: 10.1039/D0EM00340A

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