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primary topic: Unravelling biochemical and molecular mechanism of a carboxylesterase from Dietzia kunjamensis IITR165 reveal novel activities against polyethylene terephthalate

Unravelling biochemical and molecular mechanism of a carboxylesterase from Dietzia kunjamensis IITR165 reveal novel activities against polyethylene terephthalate
type: AcademicArticle
type: Article
abstract: Plastics and plasticizers accumulate in the ecological niches affecting biodiversity, and human and environmental health. Bacteria degrading polyethylene terephthalate (PET) were screened and PETases involved in PET degradation were characterized. Here, we identified a carboxylesterase Dkca1 of 48.44 kDa molecular mass from Dietzia kunjamensis IITR165 shown to degrade amorphous PET film into bis(2-hydroxyethyl) terephthalate (BHET) and terephthalic acid (TPA) formed 64.35 μM and 35.26 μM, respectively within 96 h at 37 °C as revealed by LC-MS analysis showed significant PET hydrolase activity similar to reported PETases. SEM analysis confirms the surface erosion as cavities and holes. Dkca1 also hydrolysed BHET and dibutyl phthalate (DBP) at a concentration of 1 mM within 3 h indicating its versatility. Fluorescence quenching shows Dkca1 protein has a maximum affinity (Kd) towards BHET (86.55 μM) than DBP (134.2 μM). The protein demonstrated high stability under temperatures above 40 °C and at the pH range of 6.0-9.0. Moreover, Amino acid composition showed that the Dkca1 enzyme belongs to family VII carboxylesterase containing conserved catalytic triad of Ser183-Glu289-His378 with pentapeptide motif GXSAG and an oxyanion hole H103GGG106, sharing 37.47 % and 32.44 % similarity with a PET hydrolase TfCa from Thermobifida fusca and PAE hydrolase CarEW from Bacillus sp. K91, respectively. A docking study revealed that ligand PET, BHET, and DBP showed favourable binding in the catalytic pocket of the Dkca1 protein.
date: 2024-11
volume: 735
issue: 150833
author list: authors
type: EPrint
type: ArticleEPrint
is part of: repository

Elsevier BV
type: Organization

Biochem. Biophys. Res. Commun.
type: Collection

Srikrishna Subramanian
type: Person
given name: Srikrishna
family name: Subramanian

J Venkatesh Pratap
type: Person
given name: J
family name: Venkatesh Pratap

Natesan Manickam
type: Person
given name: Natesan
family name: Manickam

Deepali Tripathi
type: Person
given name: Deepali
family name: Tripathi

Neha Gupta
type: Person
given name: Neha
family name: Gupta

Mohini Soni
type: Person
given name: Mohini
family name: Soni

Saurabh Singh
type: Person
given name: Saurabh
family name: Singh

Padmani Sandhu
type: Person
given name: Padmani
family name: Sandhu

HTML Summary of #3346 Unravelling biochemical and molecular mechanism of a carboxylesterase from Dietzia kunjamensis IITR165 reveal novel activities against polyethylene terephthalate
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primary topic: Unravelling biochemical and molecular mechanism of a carboxylesterase from Dietzia kunjamensis IITR165 reveal novel activities against polyethylene terephthalate