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

91 Citations (Scopus)

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
Publication status	Published - 2020 Apr 17

Bibliographical note

Funding Information:
This work was supported by the Cooperative Research Program for Agricultural Science & Technology Development (project no. PJ01492602), Rural Development Administration, Republic of Korea. H.-Y.S. and H.S. were supported by the Global Ph.D. Fellowship Program of the Korean Government (2017H1A2A1042052 and 2018H1A2A1061751, respectively).

Publisher Copyright:
© 2020 American Chemical Society.

Copyright:
Copyright 2020 Elsevier B.V., All rights reserved.

Keywords

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

ASJC Scopus subject areas

Catalysis
General Chemistry

Access to Document

10.1021/acscatal.9b05604

Cite this

@article{21d2c53b7c6a491caa381fce54e9ce0f,

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 = "Ideonella sakaiensis, MHETase, biodegradation, exo-PETase, extracellular production, 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}",

note = "Funding Information: This work was supported by the Cooperative Research Program for Agricultural Science & Technology Development (project no. PJ01492602), Rural Development Administration, Republic of Korea. H.-Y.S. and H.S. were supported by the Global Ph.D. Fellowship Program of the Korean Government (2017H1A2A1042052 and 2018H1A2A1061751, respectively). Publisher Copyright: {\textcopyright} 2020 American Chemical Society. Copyright: Copyright 2020 Elsevier B.V., All rights reserved.",

year = "2020",

month = apr,

day = "17",

doi = "10.1021/acscatal.9b05604",

language = "English",

volume = "10",

pages = "4805--4812",

journal = "ACS Catalysis",

issn = "2155-5435",

publisher = "American Chemical Society",

number = "8",

}

TY - JOUR

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

N1 - Funding Information: This work was supported by the Cooperative Research Program for Agricultural Science & Technology Development (project no. PJ01492602), Rural Development Administration, Republic of Korea. H.-Y.S. and H.S. were supported by the Global Ph.D. Fellowship Program of the Korean Government (2017H1A2A1042052 and 2018H1A2A1061751, respectively). Publisher Copyright: © 2020 American Chemical Society. Copyright: Copyright 2020 Elsevier B.V., All rights reserved.

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.

KW - Ideonella sakaiensis

KW - MHETase

KW - biodegradation

KW - exo-PETase

KW - extracellular production

KW - polyethylene terephthalate (PET)

UR - http://www.scopus.com/inward/record.url?scp=85084766885&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85084766885&partnerID=8YFLogxK

U2 - 10.1021/acscatal.9b05604

DO - 10.1021/acscatal.9b05604

M3 - Article

AN - SCOPUS:85084766885

SN - 2155-5435

VL - 10

SP - 4805

EP - 4812

JO - ACS Catalysis

JF - ACS Catalysis

IS - 8

ER -

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

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this