Biochemical characterization and molecular docking analysis of novel esterases from Sphingobium chungbukense DJ77

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We identified three novel microbial esterase (Est1, Est2, and Est3) from Sphingobium chungbukense DJ77. Multiple sequence alignment showed the Est1 and Est3 have distinct motifs, such as tetrapeptide motif HGGG, a pentapeptide sequencemotif GXSXG, and catalytic triad residues Ser-Asp-His, indicating that the identified enzymes belong to family IV esterases. Interestingly, Est1 exhibited strong activity toward classical esterase substrates, pnitrophenyl ester of short-chain fatty acids and long-chain. However, Est3 did not exhibit any activity despite having high sequence similarity and sharing the identical catalytic active residues with Est1. Est3 only showed hydrolytic degradation activity to polycaprolactone (PCL). MOE-docking prediction also provided the parameters consisting of binding energy, molecular docking score, and molecular distance between substrate and catalytic nucleophilic residue, serine. The engineered mutEst3 has hydrolytic activity for a variety of esters ranging from p-nitrophenyl esters to PCL. In the present study, we demonstrated that MOE-docking simulation provides a valuable insight for facilitating biocatalytic performance.
Publisher
ELSEVIER
Issue Date
2021-01
Language
English
Article Type
Article
Citation

INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES, v.168, pp.403 - 411

ISSN
0141-8130
DOI
10.1016/j.ijbiomac.2020.12.077
URI
http://hdl.handle.net/10203/281062
Appears in Collection
BS-Journal Papers(저널논문)
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