Expression and characterization of Est2: a novel cold-adapted esterase from Antarctic bacterium defining the new esterase family XXII.
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ABSTRACT: Extremozymes from Antarctic microbiota represent a potential source of unique biocatalysts. In this study, a novel esterase gene est2 was identified from the Antarctic bacterium Pseudomonas sp. A6-5. Phylogenetic and sequence analyses classified it as the founding member of a new esterase family XXII. The catalytic triad of the enzyme consisted of Ser141, Asp275, and His303, with the nucleophilic Ser141 situated within the characteristic GXSXG motif of α/β-hydrolases. Est2 exhibited remarkable cold-adaptation where 20-85% of the maximum activity was observed at temperatures ranging from 0 to 15°C. Substrate specificity profiling revealed preferential hydrolysis of medium-chain p-nitrophenyl esters and triglyceride emulsions.
SUBMITTER: He Y
PROVIDER: S-EPMC12446244 | biostudies-literature | 2025
REPOSITORIES: biostudies-literature
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