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Phylum-level studies of bacterial cutinases for unravelling enzymatic specificity toward PET degradation: an in silico approach.
Kumar, Shubham; Chaudhary, Bhupendra; Singhal, Barkha.
Afiliação
  • Kumar S; School of Biotechnology, Gautam Buddha University, Greater Noida, U.P., India.
  • Chaudhary B; School of Life Sciences, Jawaharlal Nehru University, New Delhi, 110067, India.
  • Singhal B; School of Biotechnology, Gautam Buddha University, Greater Noida, U.P., India. barkha@gbu.ac.in.
Braz J Microbiol ; 55(3): 2385-2400, 2024 Sep.
Article em En | MEDLINE | ID: mdl-38750346
ABSTRACT
The overwhelming use of PET plastic in various day-to-day activities led to the voluminous increase in PET waste and growing environmental hazards. A plethora of methods have been used that are associated with secondary pollutants. Therefore, microbial degradation of PET provides a sustainable approach due to its versatile metabolic diversity and capacity. The present work highlights the cutinase enzyme's role in PET degradation. This study focuses on the bacterial cutinases homologs screened from 43 reported phylum of bacteria. The reported bacterial cutinases for plastic degradation have been chosen as reference sequences, and 917 sequences have shown homology across the bacterial phyla. The dienelactone hydrolase (DLH) domain was identified for attaining specificity towards PET binding in 196 of 917 sequences. Various computational tools have been used for the physicochemical characterization of 196 sequences. The analysis revealed that most selected sequences are hydrophilic, extracellular, and thermally stable. Based on this analysis, 17 sequences have been further pursued for three-dimensional structure prediction and validation. The molecular docking studies of 17 selected sequences revealed efficient PET binding with the three sequences derived from the phylum Bacteroidota, the lowest binding energy of -5.9 kcal/mol, Armatimonadota, and Nitrososphaerota with -5.8 kcal/mol. The two enzyme sequences retrieved from the phylum Bacteroidota and Armatimonadota are metagenomically derived. Therefore, the present studies concluded that there is a high probability of finding cutinase homologs in various environmental resources that can be further explored for PET degradation.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Bactérias / Proteínas de Bactérias / Hidrolases de Éster Carboxílico / Simulação de Acoplamento Molecular Idioma: En Revista: Braz J Microbiol Ano de publicação: 2024 Tipo de documento: Article País de afiliação: Índia País de publicação: Brasil

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Bactérias / Proteínas de Bactérias / Hidrolases de Éster Carboxílico / Simulação de Acoplamento Molecular Idioma: En Revista: Braz J Microbiol Ano de publicação: 2024 Tipo de documento: Article País de afiliação: Índia País de publicação: Brasil