Cellular biocatalysts using synthetic genetic circuits for prolonged and durable enzymatic activity

buir.contributor.authorAhan, Recep Erdem
buir.contributor.authorŞaltepe, Behide
buir.contributor.authorApaydın, Onur
buir.contributor.authorŞeker, Urartu Özgür Şafak
dc.citation.epage1809en_US
dc.citation.issueNumber14en_US
dc.citation.spage1799en_US
dc.citation.volumeNumber20en_US
dc.contributor.authorAhan, Recep Erdemen_US
dc.contributor.authorŞaltepe, Behideen_US
dc.contributor.authorApaydın, Onuren_US
dc.contributor.authorŞeker, Urartu Özgür Şafaken_US
dc.date.accessioned2020-02-10T08:15:44Z
dc.date.available2020-02-10T08:15:44Z
dc.date.issued2019
dc.departmentInstitute of Materials Science and Nanotechnology (UNAM)en_US
dc.departmentNanotechnology Research Center (NANOTAM)en_US
dc.description.abstractCellular biocatalysts hold great promise for the synthesis of difficult to achieve compounds, such as complex active molecules. Whole‐cell biocatalysts can be programmed through genetic circuits to be more efficient, but they suffer from low stability. The catalytic activity of whole cells decays under stressful conditions, such as prolonged incubation times or high temperatures. In nature, microbial communities cope with these conditions by forming biofilm structures. In this study, it is shown that the use of biofilm structures can enhance the stability of whole‐cell biocatalysts. We employed two different strategies to increase the stability of whole‐cell catalysts and decrease their susceptibility to high temperature. In the first approach, the formation of a biofilm structure is induced by controlling the expression of one of the curli component, CsgA. The alkaline phosphatase (ALP) enzyme was used to monitor the catalytic activity of cells in the biofilm structure. In the second approach, the ALP enzyme was fused to the CsgA curli fiber subunit to utilize the protective properties of the biofilm on enzyme biofilms. Furthermore, an AND logic gate is introduced between the expression of CsgA and ALP by toehold RNA switches and recombinases to enable logical programming of the whole‐cell catalyst for biofilm formation and catalytic action with different tools. The study presents viable approaches to engineer a platform for biocatalysis processes.en_US
dc.description.provenanceSubmitted by Onur Emek (onur.emek@bilkent.edu.tr) on 2020-02-10T08:15:44Z No. of bitstreams: 1 Bilkent-research-paper.pdf: 268963 bytes, checksum: ad2e3a30c8172b573b9662390ed2d3cf (MD5)en
dc.description.provenanceMade available in DSpace on 2020-02-10T08:15:44Z (GMT). No. of bitstreams: 1 Bilkent-research-paper.pdf: 268963 bytes, checksum: ad2e3a30c8172b573b9662390ed2d3cf (MD5) Previous issue date: 2019en
dc.description.sponsorshipTUBITAK. Grant Number: 114M163en_US
dc.embargo.release2020-07-15
dc.identifier.doi10.1002/cbic.201800767en_US
dc.identifier.issn1439-4227
dc.identifier.urihttp://hdl.handle.net/11693/53214
dc.language.isoEnglishen_US
dc.publisherWiley‐VCH Verlag GmbH & Co. KGaA, Weinheimen_US
dc.relation.isversionofhttps://doi.org/10.1002/cbic.201800767en_US
dc.source.titleChemBioChemen_US
dc.subjectBiofilmsen_US
dc.subjectCurli fibersen_US
dc.subjectEnzymesen_US
dc.subjectSynthetic biologyen_US
dc.subjectWhole-cell biocatalysisen_US
dc.titleCellular biocatalysts using synthetic genetic circuits for prolonged and durable enzymatic activityen_US
dc.typeArticleen_US

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