Rate Response of Poly(Ethylene Terephthalate) (PET)-Hydrolases to Substrate Crystallinity: Basis for Understanding the Lag Phase

Thore B. Thomsen; Sune Schubert; Cameron J. Hunt; Kim Borch; Kenneth Jensen; Jesper Brask; Peter Westh; Anne S. Meyer

doi:10.1002/cssc.202300291

Rate Response of Poly(Ethylene Terephthalate) (PET)-Hydrolases to Substrate Crystallinity: Basis for Understanding the Lag Phase

Thore B. Thomsen, Sune Schubert, Cameron J. Hunt, Kim Borch, Kenneth Jensen, Jesper Brask, Peter Westh, Anne S. Meyer^*

^*Corresponding author for this work

Novozymes A/S

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Abstract

The rate response of PET-hydrolases to increased substrate crystallinity (X_C) of poly(ethylene terephthalate) (PET) manifests as a rate-lowering effect that varies significantly for different enzymes. Herein, we report the influence of X_C on the product release rate of six thermostable PET-hydrolases. All enzyme reactions displayed a distinctive lag phase until measurable product formation occurred. The duration of the lag phase increased with X_C. The recently discovered PET-hydrolase PHL7 worked efficiently on “amorphous” PET disks (X_C ∼10, but this enzyme was extremely sensitive to increased XC, whereas the enzymes LCC_ICCG, LCC, and DuraPETase had higher tolerance to increases in X_C and had activity on PET disks having X_C of 24.4 during reaction. Structural and molecular dynamics analysis of the PET-hydrolyzing enzymes disclosed that surface electrostatics and enzyme flexibility may account for the observed differences.

Original language	English
Article number	e202300291
Journal	ChemSusChem
Volume	16
Issue number	13
Number of pages	13
ISSN	1864-5631
DOIs	https://doi.org/10.1002/cssc.202300291
Publication status	Published - 2023

Keywords

PET crystallinity
PET-hydrolase kinetics
PET surface erosion
Enzyme surface electrostatics
Molecular Dynamics

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title = "Rate Response of Poly(Ethylene Terephthalate) (PET)-Hydrolases to Substrate Crystallinity: Basis for Understanding the Lag Phase",

abstract = "The rate response of PET-hydrolases to increased substrate crystallinity (XC) of poly(ethylene terephthalate) (PET) manifests as a rate-lowering effect that varies significantly for different enzymes. Herein, we report the influence of XC on the product release rate of six thermostable PET-hydrolases. All enzyme reactions displayed a distinctive lag phase until measurable product formation occurred. The duration of the lag phase increased with XC. The recently discovered PET-hydrolase PHL7 worked efficiently on “amorphous” PET disks (XC ∼10, but this enzyme was extremely sensitive to increased XC, whereas the enzymes LCCICCG, LCC, and DuraPETase had higher tolerance to increases in XC and had activity on PET disks having XC of 24.4 during reaction. Structural and molecular dynamics analysis of the PET-hydrolyzing enzymes disclosed that surface electrostatics and enzyme flexibility may account for the observed differences.",

keywords = "PET crystallinity, PET-hydrolase kinetics, PET surface erosion, Enzyme surface electrostatics, Molecular Dynamics",

author = "Thomsen, {Thore B.} and Sune Schubert and Hunt, {Cameron J.} and Kim Borch and Kenneth Jensen and Jesper Brask and Peter Westh and Meyer, {Anne S.}",

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T1 - Rate Response of Poly(Ethylene Terephthalate) (PET)-Hydrolases to Substrate Crystallinity: Basis for Understanding the Lag Phase

AU - Thomsen, Thore B.

AU - Schubert, Sune

AU - Hunt, Cameron J.

AU - Borch, Kim

AU - Jensen, Kenneth

AU - Brask, Jesper

AU - Westh, Peter

AU - Meyer, Anne S.

PY - 2023

Y1 - 2023

N2 - The rate response of PET-hydrolases to increased substrate crystallinity (XC) of poly(ethylene terephthalate) (PET) manifests as a rate-lowering effect that varies significantly for different enzymes. Herein, we report the influence of XC on the product release rate of six thermostable PET-hydrolases. All enzyme reactions displayed a distinctive lag phase until measurable product formation occurred. The duration of the lag phase increased with XC. The recently discovered PET-hydrolase PHL7 worked efficiently on “amorphous” PET disks (XC ∼10, but this enzyme was extremely sensitive to increased XC, whereas the enzymes LCCICCG, LCC, and DuraPETase had higher tolerance to increases in XC and had activity on PET disks having XC of 24.4 during reaction. Structural and molecular dynamics analysis of the PET-hydrolyzing enzymes disclosed that surface electrostatics and enzyme flexibility may account for the observed differences.

AB - The rate response of PET-hydrolases to increased substrate crystallinity (XC) of poly(ethylene terephthalate) (PET) manifests as a rate-lowering effect that varies significantly for different enzymes. Herein, we report the influence of XC on the product release rate of six thermostable PET-hydrolases. All enzyme reactions displayed a distinctive lag phase until measurable product formation occurred. The duration of the lag phase increased with XC. The recently discovered PET-hydrolase PHL7 worked efficiently on “amorphous” PET disks (XC ∼10, but this enzyme was extremely sensitive to increased XC, whereas the enzymes LCCICCG, LCC, and DuraPETase had higher tolerance to increases in XC and had activity on PET disks having XC of 24.4 during reaction. Structural and molecular dynamics analysis of the PET-hydrolyzing enzymes disclosed that surface electrostatics and enzyme flexibility may account for the observed differences.

KW - PET crystallinity

KW - PET-hydrolase kinetics

KW - PET surface erosion

KW - Enzyme surface electrostatics

KW - Molecular Dynamics

U2 - 10.1002/cssc.202300291

DO - 10.1002/cssc.202300291

M3 - Journal article

C2 - 37073816

SN - 1864-5631

VL - 16

JO - ChemSusChem

JF - ChemSusChem

IS - 13

M1 - e202300291

ER -

Rate Response of Poly(Ethylene Terephthalate) (PET)-Hydrolases to Substrate Crystallinity: Basis for Understanding the Lag Phase

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Keywords

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