The Purification and Characterization of a Cutinase-like Enzyme with Activity on Polyethylene Terephthalate (PET) from a Newly Isolated Bacterium Stenotrophomonas maltophilia PRS8 at a Mesophilic Temperature

Author:

Din Salah Ud123,Kalsoom 1,Satti Sadia Mehmood4ORCID,Uddin Salah1ORCID,Mankar Smita V.5,Ceylan Esma2,Hasan Fariha1,Khan Samiullah1ORCID,Badshah Malik1,Beldüz Ali Osman2ORCID,Çanakçi Sabriye2,Zhang Baozhong5ORCID,Linares-Pastén Javier A.3ORCID,Shah Aamer Ali1ORCID

Affiliation:

1. Department of Microbiology, Faculty of Biological Sciences, Quaid-i-Azam University, Islamabad 45320, Pakistan

2. Department of Biology, Karadeniz Technical University, Trabzon 61080, Turkey

3. Division of Biotechnology, Department of Chemistry, Faculty of Engineering (LTH), Lund University, P.O. Box 124, SE-22100 Lund, Sweden

4. Department of Microbiology, Kohsar University Murree, Murree 47150, Pakistan

5. Centre for Analysis and Synthesis, Department of Chemistry, Faculty of Engineering (LTH), Lund University, SE-22100 Lund, Sweden

Abstract

A polyethylene terephthalate (PET)-degrading bacterium identified as Stenotrophomonas maltophilia PRS8 was isolated from the soil of a landfill. The degradation of the PET bottle flakes and the PET prepared as a powder were assessed using live cells, an extracellular medium, or a purified cutinase-like enzyme. These treated polymers were analyzed using Fourier transform infrared spectroscopy (FTIR) and scanning electron microscopy (SEM). The depolymerization products, identified using HPLC and LC-MS, were terephthalic acid (TPA), mono(2-hydroxyethyl)-TPA (MHET), and bis(2-hydroxyethyl)-TPA (BHET). Several physicochemical factors were optimized for a better cutinase-like enzyme production by using unique single-factor and multi-factor statistical models (the Plackett–Burman design and the central composite design software). The enzyme was purified for homogeneity through column chromatography using Sephadex G-100 resin. The molecular weight of the enzyme was approximately 58 kDa. The specific activity on para nitrophenyl butyrate was estimated at 450.58 U/mg, with a purification of 6.39 times and a yield of 48.64%. The enzyme was stable at various temperatures (30–40 °C) and pH levels (8.0–10.0). The enzyme activity was significantly improved by the surfactants (Triton X-100 and Tween-40), organic solvent (formaldehyde), and metals (NiCl2 and Na2SO4). The extracellular medium containing the cutinase-type enzyme showed a depolymerization yield of the PET powder comparable to that of Idonella skaiensis IsPETase and significantly higher than that of Humicola insolens thermostable HiCut (HiC) cutinase. This study suggests that S. maltophilia PRS8 is able to degrade PET at a mesophilic temperature and could be further explored for the sustainable management of plastic waste.

Publisher

MDPI AG

Subject

Fluid Flow and Transfer Processes,Computer Science Applications,Process Chemistry and Technology,General Engineering,Instrumentation,General Materials Science

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