Acceleration of Enzymatic Degradation of Poly(ethylene terephthalate) by Surface Coating with Anionic Surfactants

Makoto Furukawa, Norifumi Kawakami, Kohei Oda, Kenji Miyamoto

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

Enzymatic degradation of poly(ethylene terephthalate) (PET) is promising because this process is safer than conventional industrial approaches. Recently, a cationic PET hydrolase (PETase) was identified from Ideonella sakaiensis. Pre-incubation of a low-crystallinity PET film with anionic surfactants prior to initiating the reaction was found to improve PETase activity 120-fold. After 36 h at 30 °C, the film thickness decreased by 22 %. The binding of surfactants to the film makes the surface anionic, thereby attracting the cationic PETase. Mutagenesis of PETase showed that the surface cationic region formed by R53, R90, and K95, which are located on the same side as the substrate binding pocket, was crucial for efficient acceleration of activity by the anionic surfactant. Thus, surfactant bound on PET aligns the orientation of the active site to the surface, resulting in efficient hydrolysis. We believe that this approach using PETase could be further improved by designing surfactant molecules for the more efficient enzymatic PET degradation.

Original languageEnglish
Pages (from-to)4018-4025
Number of pages8
JournalChemSusChem
Volume11
Issue number23
DOIs
Publication statusPublished - 2018 Dec 11

Fingerprint

Hydrolases
Polyethylene Terephthalates
Anionic surfactants
Polyethylene terephthalates
ethylene
surfactant
coating
Degradation
Coatings
degradation
Surface-Active Agents
Surface active agents
Mutagenesis
crystallinity
Film thickness
hydrolysis
Hydrolysis
incubation
fold
substrate

Keywords

  • biocatalysis
  • hydrolysis
  • polymers
  • surface chemistry
  • surfactants

ASJC Scopus subject areas

  • Environmental Chemistry
  • Chemical Engineering(all)
  • Materials Science(all)
  • Energy(all)

Cite this

Acceleration of Enzymatic Degradation of Poly(ethylene terephthalate) by Surface Coating with Anionic Surfactants. / Furukawa, Makoto; Kawakami, Norifumi; Oda, Kohei; Miyamoto, Kenji.

In: ChemSusChem, Vol. 11, No. 23, 11.12.2018, p. 4018-4025.

Research output: Contribution to journalArticle

@article{2db04ff65c7d4154b394b74a21fddbc5,
title = "Acceleration of Enzymatic Degradation of Poly(ethylene terephthalate) by Surface Coating with Anionic Surfactants",
abstract = "Enzymatic degradation of poly(ethylene terephthalate) (PET) is promising because this process is safer than conventional industrial approaches. Recently, a cationic PET hydrolase (PETase) was identified from Ideonella sakaiensis. Pre-incubation of a low-crystallinity PET film with anionic surfactants prior to initiating the reaction was found to improve PETase activity 120-fold. After 36 h at 30 °C, the film thickness decreased by 22 {\%}. The binding of surfactants to the film makes the surface anionic, thereby attracting the cationic PETase. Mutagenesis of PETase showed that the surface cationic region formed by R53, R90, and K95, which are located on the same side as the substrate binding pocket, was crucial for efficient acceleration of activity by the anionic surfactant. Thus, surfactant bound on PET aligns the orientation of the active site to the surface, resulting in efficient hydrolysis. We believe that this approach using PETase could be further improved by designing surfactant molecules for the more efficient enzymatic PET degradation.",
keywords = "biocatalysis, hydrolysis, polymers, surface chemistry, surfactants",
author = "Makoto Furukawa and Norifumi Kawakami and Kohei Oda and Kenji Miyamoto",
year = "2018",
month = "12",
day = "11",
doi = "10.1002/cssc.201802096",
language = "English",
volume = "11",
pages = "4018--4025",
journal = "ChemSusChem",
issn = "1864-5631",
publisher = "Wiley-VCH Verlag",
number = "23",

}

TY - JOUR

T1 - Acceleration of Enzymatic Degradation of Poly(ethylene terephthalate) by Surface Coating with Anionic Surfactants

AU - Furukawa, Makoto

AU - Kawakami, Norifumi

AU - Oda, Kohei

AU - Miyamoto, Kenji

PY - 2018/12/11

Y1 - 2018/12/11

N2 - Enzymatic degradation of poly(ethylene terephthalate) (PET) is promising because this process is safer than conventional industrial approaches. Recently, a cationic PET hydrolase (PETase) was identified from Ideonella sakaiensis. Pre-incubation of a low-crystallinity PET film with anionic surfactants prior to initiating the reaction was found to improve PETase activity 120-fold. After 36 h at 30 °C, the film thickness decreased by 22 %. The binding of surfactants to the film makes the surface anionic, thereby attracting the cationic PETase. Mutagenesis of PETase showed that the surface cationic region formed by R53, R90, and K95, which are located on the same side as the substrate binding pocket, was crucial for efficient acceleration of activity by the anionic surfactant. Thus, surfactant bound on PET aligns the orientation of the active site to the surface, resulting in efficient hydrolysis. We believe that this approach using PETase could be further improved by designing surfactant molecules for the more efficient enzymatic PET degradation.

AB - Enzymatic degradation of poly(ethylene terephthalate) (PET) is promising because this process is safer than conventional industrial approaches. Recently, a cationic PET hydrolase (PETase) was identified from Ideonella sakaiensis. Pre-incubation of a low-crystallinity PET film with anionic surfactants prior to initiating the reaction was found to improve PETase activity 120-fold. After 36 h at 30 °C, the film thickness decreased by 22 %. The binding of surfactants to the film makes the surface anionic, thereby attracting the cationic PETase. Mutagenesis of PETase showed that the surface cationic region formed by R53, R90, and K95, which are located on the same side as the substrate binding pocket, was crucial for efficient acceleration of activity by the anionic surfactant. Thus, surfactant bound on PET aligns the orientation of the active site to the surface, resulting in efficient hydrolysis. We believe that this approach using PETase could be further improved by designing surfactant molecules for the more efficient enzymatic PET degradation.

KW - biocatalysis

KW - hydrolysis

KW - polymers

KW - surface chemistry

KW - surfactants

UR - http://www.scopus.com/inward/record.url?scp=85057325240&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85057325240&partnerID=8YFLogxK

U2 - 10.1002/cssc.201802096

DO - 10.1002/cssc.201802096

M3 - Article

VL - 11

SP - 4018

EP - 4025

JO - ChemSusChem

JF - ChemSusChem

SN - 1864-5631

IS - 23

ER -