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- W4320482886 abstract "Enzymatic recycling of poly-l-lactic acid (PLLA) plastic has recently become an area of interest; however, investigation of enzymatic mechanisms and engineering strategies to improve activity remains limited. In this study, we have identified a subtilisin from Bacillus pumilus that has the ability to depolymerize high-molecular-weight PLLA. We performed a comparative, mutational analysis of this enzyme with a less active homologue from Bacillus subtilis to determine residues favored for activity. Our results demonstrate that both enzymes contain residues favored for PLLA depolymerization, with the generation of several hyperactive variants. In silico modeling suggests that increases in activity are due to opening of the binding pockets and increased surface hydrophobicity. Combinations of hyperactive mutations have synergistic effects with the generation of subtilisin variants with 830- and 184-fold increases in activity for B. subtilis and B. pumilus subtilisins, respectively. One B. pumilus subtilisin variant can visibly dissolve high-molecular-weight PLLA films." @default.
- W4320482886 created "2023-02-14" @default.
- W4320482886 creator A5055749338 @default.
- W4320482886 creator A5066798942 @default.
- W4320482886 date "2023-02-13" @default.
- W4320482886 modified "2023-10-12" @default.
- W4320482886 title "Synergistic Mutations Create <i>Bacillus</i> Subtilisin Variants with Enhanced Poly-<scp>l</scp>-Lactic Acid Depolymerization Activity" @default.
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- W4320482886 doi "https://doi.org/10.1021/acs.biomac.2c01198" @default.
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- W4320482886 hasPublicationYear "2023" @default.
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