Enzymes as Enhancers for the Biodegradation of Synthetic Polymers in Wastewater

Haernvall, Karolina; Zitzenbacher, Sabine; Biundo, Antonino; Yamamoto, Motonori; Schick, Michael; Ribitsch, Doris; Guebitz, Georg M.

doi:10.1002/cbic.201700364

Cited by 19 publications

(18 citation statements)

References 67 publications

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“…Enzymatic hydrolysis can be influenced by several different parameters as, for example, chemical composition, molecular weight, crystallinity, and glass transition temperature. The chemical composition of the polyesters can influence the enzymatic hydrolysis and have thoroughly been investigated before for different enzymes . In this case, the results indicated that Thc_Cut1 preferentially hydrolyzed polyesters with 1,5‐pentanediol and 1,9‐nonanediol as alcohol moiety.…”

Section: Resultsmentioning

confidence: 94%

Polyol Structure Influences Enzymatic Hydrolysis of Bio‐Based 2,5‐Furandicarboxylic Acid (FDCA) Polyesters

Haernvall

Zitzenbacher

Amer

et al. 2017

Biotechnology Journal

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Polyesters of 2,5-furandicarboxylic acid (FDCA) have gained attention as they can be regarded as the bio-based alternatives to the petroleum-based polyesters of terephthalic acid. However, only little is known about the biodegradation and enzymatic hydrolysis of FDCA-based polyesters. This work aims to investigate the influence of different polyols on enzymatic hydrolysis of FDCA-based polyesters. A series of polyesters containing various polyols are synthesized and analyzed regarding susceptibility to enzymatic hydrolysis by cutinase 1 from Thermobifida cellulosilytica (Thc_Cut1). FDCA-based polyesters' number average molecular weight (M ) ranged from 9360-35 800 g mol according to gel permeation chromatography (GPC) analysis. Differential scanning calorimetry (DSC) analyses show decreasing glass transition temperature (T ) with increasing diol chain length. Crystallinity of all polyesters is below 1% except for polyesters containing 1,6-hexanediol, 1,8-octanediol, and 1,12-dodecanediol for which calculated crystallinities are 27, 37, and 30%, respectively. Thc_Cut1 hydrolyzes all tested polyesters with preference for polyesters containing 1,5-pentanediol and 1,9-nonanediol (57.7 ± 7.5 and 52.8 ± 4.0% released FDCA). Enzyme activity increases when the linear diol 1,3-propanediol is replaced by the branched analog 1,2-propanediol or ethoxy units are introduced into the polyester chain. The results will contribute to expand the knowledge of microbial biodegradation of FDCA-based polyesters.

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Section: Resultsmentioning

confidence: 94%

Polyol Structure Influences Enzymatic Hydrolysis of Bio‐Based 2,5‐Furandicarboxylic Acid (FDCA) Polyesters

Haernvall

Zitzenbacher

Amer

et al. 2017

Biotechnology Journal

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“…However, additional applications appear feasible for PE-H as it has been demonstrated that the PE-H homologous enzyme PpelaLip originating from the closely related genus Pseudomonas pelagia can be used for the biodegradation of different synthetic polyesters and may thus be applicable for waste water treatment (Haernvall et al, 2017). In this case, the activity of the respective biocatalyst at low temperatures is an advantage allowing for the hydrolysis of synthetic polymers at 15 • C (Haernvall et al, 2018).…”

Section: Resultsmentioning

confidence: 99%

A Novel Polyester Hydrolase From the Marine Bacterium Pseudomonas aestusnigri – Structural and Functional Insights

et al. 2020

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Biodegradation of synthetic polymers, in particular polyethylene terephthalate (PET), is of great importance, since environmental pollution with PET and other plastics has become a severe global problem. Here, we report on the polyester degrading ability of a novel carboxylic ester hydrolase identified in the genome of the marine hydrocarbonoclastic bacterium Pseudomonas aestusnigri VGXO14 T. The enzyme, designated PE-H, belongs to the type IIa family of PET hydrolytic enzymes as indicated by amino acid sequence homology. It was produced in Escherichia coli, purified and its crystal structure was solved at 1.09 Å resolution representing the first structure of a type IIa PET hydrolytic enzyme. The structure shows a typical α/β-hydrolase fold and high structural homology to known polyester hydrolases. PET hydrolysis was detected at 30 • C with amorphous PET film (PETa), but not with PET film from a commercial PET bottle (PETb). A rational mutagenesis study to improve the PET degrading potential of PE-H yielded variant PE-H (Y250S) which showed improved activity, ultimately also allowing the hydrolysis of PETb. The crystal structure of this variant solved at 1.35 Å resolution allowed to rationalize the improvement of enzymatic activity. A PET oligomer binding model was proposed by molecular docking computations. Our results indicate a significant potential of the marine bacterium P. aestusnigri for PET degradation.

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“…Another study describes the hydrolysis of poly(oxyethylene terephthalate) (PET-PEO) by an enzyme mixture of an esterase and a cutinase from Pseudomonas pseudoalcaligenes, and a lipase from Pseudomonas pelagia, in order to facilitate further degradation of the material in wastewater treatment plants (WWTP) [116]. It is common to introduce polymers with polyoxyethylene chains in order to regulate their characteristics, such as crystallinity, glass-transition temperature, flexibility, water solubility, and adsorption onto hydrophilic surfaces.…”

Section: Degradation Of Other Synthetic Polymersmentioning

confidence: 99%

A Middle-Aged Enzyme Still in Its Prime: Recent Advances in the Field of Cutinases

et al. 2018

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Cutinases are α/β hydrolases, and their role in nature is the degradation of cutin. Such enzymes are usually produced by phytopathogenic microorganisms in order to penetrate their hosts. The first focused studies on cutinases started around 50 years ago. Since then, numerous cutinases have been isolated and characterized, aiming at the elucidation of their structure–function relations. Our deeper understanding of cutinases determines the applications by which they could be utilized; from food processing and detergents, to ester synthesis and polymerizations. However, cutinases are mainly efficient in the degradation of polyesters, a natural function. Therefore, these enzymes have been successfully applied for the biodegradation of plastics, as well as for the delicate superficial hydrolysis of polymeric materials prior to their functionalization. Even though research on this family of enzymes essentially began five decades ago, they are still involved in many reports; novel enzymes are being discovered, and new fields of applications arise, leading to numerous related publications per year. Perhaps the future of cutinases lies in their evolved descendants, such as polyesterases, and particularly PETases. The present article reviews the biochemical and structural characteristics of cutinases and cutinase-like hydrolases, and their applications in the field of bioremediation and biocatalysis.

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Enzymes as Enhancers for the Biodegradation of Synthetic Polymers in Wastewater

Cited by 19 publications

References 67 publications

Polyol Structure Influences Enzymatic Hydrolysis of Bio‐Based 2,5‐Furandicarboxylic Acid (FDCA) Polyesters

Polyol Structure Influences Enzymatic Hydrolysis of Bio‐Based 2,5‐Furandicarboxylic Acid (FDCA) Polyesters

A Novel Polyester Hydrolase From the Marine Bacterium Pseudomonas aestusnigri – Structural and Functional Insights

A Middle-Aged Enzyme Still in Its Prime: Recent Advances in the Field of Cutinases

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