Decomposition of the PET Film by MHETase Using Exo-PETase Function

Hye Young Sagong; Hogyun Seo; Taeho Kim; Hyeoncheol Francis Son; Seongjoon Joo; Seul Hoo Lee; Seongmin Kim; Jae Sung Woo; Sung Yeon Hwang; Kyung Jin Kim

doi:10.1021/acscatal.9b05604

Decomposition of the PET Film by MHETase Using Exo-PETase Function

Hye Young Sagong, Hogyun Seo, Taeho Kim, Hyeoncheol Francis Son, Seongjoon Joo, Seul Hoo Lee, Seongmin Kim, Jae Sung Woo, Sung Yeon Hwang, Kyung Jin Kim

Research output: Contribution to journal › Article › peer-review

104 Scopus citations

Abstract

Monohydroxyethyl terephthalate (MHET) hydrolase (MHETase) is an enzyme known to be involved in the final degradation step of poly(ethylene terephthalate) (PET) by hydrolyzing MHET into terephthalic acid and ethylene glycol in Ideonella sakaiensis. Here, we report the extracellular production of MHETase in an active form with a proper folding. Based on the structural observations and biochemical experiments, we reveal that MHETase also functions as exo-PETase by hydrolyzing the synthesized PET pentamer. We further present that MHETase has a hydrolysis activity against the termini-generated PET film, demonstrating the exo-PETase function of the enzyme. We also develop a MHETase^{R411K/S416A/F424I} variant with a higher BHET activity, and the variant exhibits an enhanced degradation activity against the PET film. Based on these results, we propose that MHETase plays several roles in the biodegradation of PET using the BHETase and exo-PETase activities as well as the MHET hydrolysis function.

Original language	English
Pages (from-to)	4805-4812
Number of pages	8
Journal	ACS Catalysis
Volume	10
Issue number	8
DOIs	https://doi.org/10.1021/acscatal.9b05604
State	Published - 17 Apr 2020

Keywords

biodegradation
exo-PETase
extracellular production
Ideonella sakaiensis
MHETase
polyethylene terephthalate (PET)

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10.1021/acscatal.9b05604

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title = "Decomposition of the PET Film by MHETase Using Exo-PETase Function",

abstract = "Monohydroxyethyl terephthalate (MHET) hydrolase (MHETase) is an enzyme known to be involved in the final degradation step of poly(ethylene terephthalate) (PET) by hydrolyzing MHET into terephthalic acid and ethylene glycol in Ideonella sakaiensis. Here, we report the extracellular production of MHETase in an active form with a proper folding. Based on the structural observations and biochemical experiments, we reveal that MHETase also functions as exo-PETase by hydrolyzing the synthesized PET pentamer. We further present that MHETase has a hydrolysis activity against the termini-generated PET film, demonstrating the exo-PETase function of the enzyme. We also develop a MHETaseR411K/S416A/F424I variant with a higher BHET activity, and the variant exhibits an enhanced degradation activity against the PET film. Based on these results, we propose that MHETase plays several roles in the biodegradation of PET using the BHETase and exo-PETase activities as well as the MHET hydrolysis function.",

keywords = "biodegradation, exo-PETase, extracellular production, Ideonella sakaiensis, MHETase, polyethylene terephthalate (PET)",

author = "Sagong, {Hye Young} and Hogyun Seo and Taeho Kim and Son, {Hyeoncheol Francis} and Seongjoon Joo and Lee, {Seul Hoo} and Seongmin Kim and Woo, {Jae Sung} and Hwang, {Sung Yeon} and Kim, {Kyung Jin}",

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T1 - Decomposition of the PET Film by MHETase Using Exo-PETase Function

AU - Sagong, Hye Young

AU - Seo, Hogyun

AU - Kim, Taeho

AU - Son, Hyeoncheol Francis

AU - Joo, Seongjoon

AU - Lee, Seul Hoo

AU - Kim, Seongmin

AU - Woo, Jae Sung

AU - Hwang, Sung Yeon

AU - Kim, Kyung Jin

PY - 2020/4/17

Y1 - 2020/4/17

N2 - Monohydroxyethyl terephthalate (MHET) hydrolase (MHETase) is an enzyme known to be involved in the final degradation step of poly(ethylene terephthalate) (PET) by hydrolyzing MHET into terephthalic acid and ethylene glycol in Ideonella sakaiensis. Here, we report the extracellular production of MHETase in an active form with a proper folding. Based on the structural observations and biochemical experiments, we reveal that MHETase also functions as exo-PETase by hydrolyzing the synthesized PET pentamer. We further present that MHETase has a hydrolysis activity against the termini-generated PET film, demonstrating the exo-PETase function of the enzyme. We also develop a MHETaseR411K/S416A/F424I variant with a higher BHET activity, and the variant exhibits an enhanced degradation activity against the PET film. Based on these results, we propose that MHETase plays several roles in the biodegradation of PET using the BHETase and exo-PETase activities as well as the MHET hydrolysis function.

AB - Monohydroxyethyl terephthalate (MHET) hydrolase (MHETase) is an enzyme known to be involved in the final degradation step of poly(ethylene terephthalate) (PET) by hydrolyzing MHET into terephthalic acid and ethylene glycol in Ideonella sakaiensis. Here, we report the extracellular production of MHETase in an active form with a proper folding. Based on the structural observations and biochemical experiments, we reveal that MHETase also functions as exo-PETase by hydrolyzing the synthesized PET pentamer. We further present that MHETase has a hydrolysis activity against the termini-generated PET film, demonstrating the exo-PETase function of the enzyme. We also develop a MHETaseR411K/S416A/F424I variant with a higher BHET activity, and the variant exhibits an enhanced degradation activity against the PET film. Based on these results, we propose that MHETase plays several roles in the biodegradation of PET using the BHETase and exo-PETase activities as well as the MHET hydrolysis function.

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KW - exo-PETase

KW - extracellular production

KW - Ideonella sakaiensis

KW - MHETase

KW - polyethylene terephthalate (PET)

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Decomposition of the PET Film by MHETase Using Exo-PETase Function

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