Rational Protein Engineering of Thermo-Stable PETase from Ideonella sakaiensis for Highly Efficient PET Degradation

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dc.contributor.authorSon, Hyeoncheol Francisko
dc.contributor.authorCho, In Jinko
dc.contributor.authorJoo, Seongjoonko
dc.contributor.authorSeo, Hogyunko
dc.contributor.authorSagong, Hye-Youngko
dc.contributor.authorChoi, So Youngko
dc.contributor.authorLee, Sang Yupko
dc.contributor.authorKim, Kyung-Jinko
dc.date.accessioned2019-05-02T02:50:15Z-
dc.date.available2019-05-02T02:50:15Z-
dc.date.created2019-04-29-
dc.date.issued2019-04-
dc.identifier.citationACS CATALYSIS, v.9, no.4, pp.3519 - 3526-
dc.identifier.issn2155-5435-
dc.identifier.urihttp://hdl.handle.net/10203/261706-
dc.description.abstractWidespread utilization of polyethylene terephthalate (PET) has caused a variety of environmental and health problems; thus, the enzymatic degradation of PET can be a promising solution. Although PETase from Ideonalla sakaiensis (IsPETase) has been reported to have the highest PET degradation activity under mild conditions of all PET-degrading enzymes reported to date, its low thermal stability limits its ability for efficient and practical enzymatic degradation of PET. Using the structural information on IsPETase, we developed a rational protein engineering strategy using several IsPETase variants that were screened for high thermal stability to improve PET degradation activity. In particular, the IsPETa- se(S121E/D186H/R280A) variant, which was designed to have a stabilized beta 6-beta 7 connecting loop and extended subsite IIc, had a T-m value that was increased by 8.81 degrees C and PET degradation activity was enhanced by 14-fold at 40 degrees C in comparison with IsPETase(WT). The designed structural modifications were further verified through structure determination of the variants, and high thermal stability was further confirmed by a heat-inactivation experiment. The proposed strategy and developed variants represent an important advancement for achieving the complete biodegradation of PET under mild conditions.-
dc.languageEnglish-
dc.publisherAMER CHEMICAL SOC-
dc.titleRational Protein Engineering of Thermo-Stable PETase from Ideonella sakaiensis for Highly Efficient PET Degradation-
dc.typeArticle-
dc.identifier.wosid000464075700079-
dc.identifier.scopusid2-s2.0-85063469706-
dc.type.rimsART-
dc.citation.volume9-
dc.citation.issue4-
dc.citation.beginningpage3519-
dc.citation.endingpage3526-
dc.citation.publicationnameACS CATALYSIS-
dc.identifier.doi10.1021/acscatal.9b00568-
dc.contributor.localauthorLee, Sang Yup-
dc.contributor.nonIdAuthorSon, Hyeoncheol Francis-
dc.contributor.nonIdAuthorJoo, Seongjoon-
dc.contributor.nonIdAuthorSeo, Hogyun-
dc.contributor.nonIdAuthorSagong, Hye-Young-
dc.contributor.nonIdAuthorKim, Kyung-Jin-
dc.description.isOpenAccessN-
dc.type.journalArticleArticle-
dc.subject.keywordAuthorpolyethylene terephthalate (PET)-
dc.subject.keywordAuthorbiodegradation-
dc.subject.keywordAuthorPETase from Ideonella sakaiensis (IsPETase)-
dc.subject.keywordAuthorrational protein engineering-
dc.subject.keywordAuthorthermal stability-
dc.subject.keywordPlusPOLY(ETHYLENE-TEREPHTHALATE)-
dc.subject.keywordPlusCUTINASE-
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CBE-Journal Papers(저널논문)
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