Biochemical Characterisation of Sis: A Distinct Thermophilic PETase with Enhanced NanoPET Substrate Hydrolysis and Thermal Stability-Reference-Cited by-同舟云学术

Biochemical Characterisation of Sis: A Distinct Thermophilic PETase with Enhanced NanoPET Substrate Hydrolysis and Thermal Stability

Published:2024-07-25 Issue:15 Volume:25 Page:8120
ISSN:1422-0067
Container-title:International Journal of Molecular Sciences
language:en
Short-container-title:IJMS

Author:

Ercolano Carmen¹,Iacono Roberta¹²^ORCID,Cafaro Valeria¹^ORCID,Pizzo Elio¹³^ORCID,Giovannelli Donato¹²⁴⁵⁶⁷,Feuerriegel Golo⁸^ORCID,Streit Wolfgang R.⁸,Strazzulli Andrea¹²^ORCID,Moracci Marco¹²^ORCID

Affiliation:

1. Department of Biology, University of Naples Federico II, Complesso Universitario di Monte S. Angelo, Via Cinthia 21, 80126 Naples, Italy

2. National Biodiversity Future Center (NBFC), 90133 Palermo, Italy

3. Centro Servizi Metrologici e Tecnologici Avanzati (CeSMA), University of Naples Federico II, 80126 Naples, Italy

4. Institute for Marine Biological Resources and Biotechnologies, Italian National Research Council, CNR-IRBIM, 60125 Ancona, Italy

5. Department of Marine and Coastal Science, Rutgers University, New Brunswick, NJ 08901, USA

6. Marine Chemistry and Geochemistry Department, Woods Hole Oceanographic Institution, Woods Hole, MA 02543, USA

7. Earth-Life Science Institute (ELSI), Tokyo Institute of Technology, Tokyo 152-8552, Japan

8. Department of Microbiology and Biotechnology, University of Hamburg, 22609 Hamburg, Germany

Abstract

Polyethylene terephthalate (PET) degradation by enzymatic hydrolysis is significant for addressing plastic pollution and fostering sustainable waste management practices. Identifying thermophilic and thermostable PET hydrolases is particularly crucial for industrial bioprocesses, where elevated temperatures may enhance enzymatic efficiency and process kinetics. In this study, we present the discovery of a novel thermophilic and thermostable PETase enzyme named Sis, obtained through metagenomic sequence-based analysis. Sis exhibits robust activity on nanoPET substrates, demonstrating effectiveness at temperatures up to 70 °C and displaying exceptional thermal stability with a melting temperature (Tm) of 82 °C. Phylogenetically distinct from previously characterised PET hydrolases, Sis represents a valuable addition to the repertoire of enzymes suitable for PET degradation.

Funder

Ministero dell’Università e della Ricerca

Publisher

MDPI AG

Link

https://www.mdpi.com/1422-0067/25/15/8120/pdf

Reference40 articles.

1. Biocatalysis as a green route for recycling the recalcitrant plastic polyethylene terephthalate;Wei;Microb. Biotechnol.,2017

2. Enzymes′ Power for Plastics Degradation;Tournier;Chem. Rev.,2023

3. Khairul Anuar, N.F.S., Huyop, F., Ur-Rehman, G., Abdullah, F., Normi, Y.M., Sabullah, M.K., and Abdul Wahab, R. (2022). An Overview into Polyethylene Terephthalate (PET) Hydrolases and Efforts in Tailoring Enzymes for Improved Plastic Degradation. Int. J. Mol. Sci., 23.

4. Structural insight into catalytic mechanism of PET hydrolase;Han;Nat. Commun.,2017

5. Isolation of a novel cutinase homolog with polyethylene terephthalate-degrading activity from leaf-branch compost by using a metagenomic approach;Sulaiman;Appl. Environ. Microbiol.,2012