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<p>Esterases, a class of α/β-hydrolases, are crucial enzymes used for the biotransformation of industrially important biomolecules. Exploring the pond metagenome, a lipolytic clone. (PLR5) was identified that exhibited activity against tributyrin. This clone encodes a unique putative α/β-hydrolase belonging to the lysophospholipase-like subgroup of the α/β-hydrolase superfamily, which harbours a PldB domain. PLR5 contains a canonical α/β-hydrolase Gly-X-Ser-X-Gly pentapeptide motif and a conserved catalytic triad (Ser97-Asp214-His241). PLR5 preferentially hydrolyses short-chain esters (C2-C4) at 45 ˚C and at a pH of 8.0. Furthermore, PLR5 exhibited significant tolerance to ethanol, acetone, DMSO, and DMF (10% v/v); however, approximately 50% and 35% activity were retained in the presence of higher concentrations of DMSO and DMF (50% v/v), respectively. PLR5 was strongly inhibited by PMSF and HgCl<sub>2</sub>. Modelled structural analysis confirmed the presence of the classical catalytic triad and a cysteine (119) in its vicinity, suggesting that inhibition by cysteine-binding molecules may result from occlusion of the active site pocket. Overall, this enzyme exhibits strong catalytic performance and solvent tolerance, uncovering its potential for biotransformation of industrially important short-chain esters.</p>

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Identification and characterization of PldB domain-containing esterase from a freshwater pond metagenome

  • 期刊论文

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  • 发表日期：

    2026年8月4日

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  • Manish Kumar Yadav,
  • Vineet Anand,
  • Rakesh Sharma

摘要

Esterases, a class of α/β-hydrolases, are crucial enzymes used for the biotransformation of industrially important biomolecules. Exploring the pond metagenome, a lipolytic clone. (PLR5) was identified that exhibited activity against tributyrin. This clone encodes a unique putative α/β-hydrolase belonging to the lysophospholipase-like subgroup of the α/β-hydrolase superfamily, which harbours a PldB domain. PLR5 contains a canonical α/β-hydrolase Gly-X-Ser-X-Gly pentapeptide motif and a conserved catalytic triad (Ser97-Asp214-His241). PLR5 preferentially hydrolyses short-chain esters (C2-C4) at 45 ˚C and at a pH of 8.0. Furthermore, PLR5 exhibited significant tolerance to ethanol, acetone, DMSO, and DMF (10% v/v); however, approximately 50% and 35% activity were retained in the presence of higher concentrations of DMSO and DMF (50% v/v), respectively. PLR5 was strongly inhibited by PMSF and HgCl2. Modelled structural analysis confirmed the presence of the classical catalytic triad and a cysteine (119) in its vicinity, suggesting that inhibition by cysteine-binding molecules may result from occlusion of the active site pocket. Overall, this enzyme exhibits strong catalytic performance and solvent tolerance, uncovering its potential for biotransformation of industrially important short-chain esters.