Enzymatic recovery of polyester building blocks from polymer blends. (August 2017)
- Record Type:
- Journal Article
- Title:
- Enzymatic recovery of polyester building blocks from polymer blends. (August 2017)
- Main Title:
- Enzymatic recovery of polyester building blocks from polymer blends
- Authors:
- Gamerith, Caroline
Zartl, Barbara
Pellis, Alessandro
Guillamot, Frédérique
Marty, Alain
Acero, Enrique Herrero
Guebitz, Georg M. - Abstract:
- Graphical abstract: Highlights: Thc_Cut1 hydrolyzes PET in polymer blends without prior separation. Significant inhibitory effect of soluble released products is detectable. Main process influencing factors are particle size, temperature & enzyme stability. Abstract: In this study we investigated the ability of a cutinase from Thermobifida cellulosilytica (Thc_Cut1) to hydrolyze poly (ethylene terephthalate) (PET) moieties in different polymer blends. The composition of various materials including commercial available bottles and packaging was determined using Fourier Transform InfraRed spectroscopy (FT-IR) and Differential Scanning Calorimetry (DSC). When incubated with PET blended with polyethylene (PE) or polyamide (PA) from packaging and bottles without prior separation, Thc_Cut1 selectively hydrolyzed the PET moieties releasing terephthalic acid (TPA) and mono(2-hydroxyethyl) terephthalate (MHET). Polymer blends were hydrolyzed in an up to 9 times higher extent compared to higher crystalline pure PET. The influence of various parameters like temperature, particle size, crystallinity and product inhibition on hydrolysis of PET moieties by Thc_Cut1 was investigated. The amount of products released was up to 10 times higher when the incubation temperature was increased from 40 °C to 60 °C. The smaller the particle size the higher the hydrolysis rates were. Interestingly, semi-crystalline (24%) PET from bottles was hydrolyzed faster than powder from amorphous PET filmsGraphical abstract: Highlights: Thc_Cut1 hydrolyzes PET in polymer blends without prior separation. Significant inhibitory effect of soluble released products is detectable. Main process influencing factors are particle size, temperature & enzyme stability. Abstract: In this study we investigated the ability of a cutinase from Thermobifida cellulosilytica (Thc_Cut1) to hydrolyze poly (ethylene terephthalate) (PET) moieties in different polymer blends. The composition of various materials including commercial available bottles and packaging was determined using Fourier Transform InfraRed spectroscopy (FT-IR) and Differential Scanning Calorimetry (DSC). When incubated with PET blended with polyethylene (PE) or polyamide (PA) from packaging and bottles without prior separation, Thc_Cut1 selectively hydrolyzed the PET moieties releasing terephthalic acid (TPA) and mono(2-hydroxyethyl) terephthalate (MHET). Polymer blends were hydrolyzed in an up to 9 times higher extent compared to higher crystalline pure PET. The influence of various parameters like temperature, particle size, crystallinity and product inhibition on hydrolysis of PET moieties by Thc_Cut1 was investigated. The amount of products released was up to 10 times higher when the incubation temperature was increased from 40 °C to 60 °C. The smaller the particle size the higher the hydrolysis rates were. Interestingly, semi-crystalline (24%) PET from bottles was hydrolyzed faster than powder from amorphous PET films (12%). An inhibitory effect of bis(2-hydroxyethyl) terephthalate (BHET) on hydrolysis of PET by Thc_Cut1 was observed. … (more)
- Is Part Of:
- Process biochemistry. Volume 59:Part A(2017)
- Journal:
- Process biochemistry
- Issue:
- Volume 59:Part A(2017)
- Issue Display:
- Volume 59, Issue 1 (2017)
- Year:
- 2017
- Volume:
- 59
- Issue:
- 1
- Issue Sort Value:
- 2017-0059-0001-0000
- Page Start:
- 58
- Page End:
- 64
- Publication Date:
- 2017-08
- Subjects:
- Enzymatic polymer recycling -- Cutinase -- Poly (ethylene terephthalate) -- Thermobifida cellulosilytica -- Polymer blends
Biochemical engineering -- Periodicals
Biotechnology -- Periodicals
Biochemistry -- periodicals
Biotechnology -- periodicals
Chemical Engineering -- periodicals
Génie biochimique -- Périodiques
Biotechnologie -- Périodiques
Biochemical engineering
Biotechnology
Periodicals
660.63 - Journal URLs:
- http://www.sciencedirect.com/science/journal/13595113 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.procbio.2017.01.004 ↗
- Languages:
- English
- ISSNs:
- 1359-5113
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 6849.983500
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 4661.xml