Please use this identifier to cite or link to this item: http://dx.doi.org/10.14279/depositonce-10334
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dc.contributor.authorPerfumo, Amedea-
dc.contributor.authorSaß, Georg Johannes Freiherr von-
dc.contributor.authorNordmann, Eva-Lena-
dc.contributor.authorBudisa, Nediljko-
dc.contributor.authorWagner, Dirk-
dc.date.accessioned2020-06-22T10:15:07Z-
dc.date.available2020-06-22T10:15:07Z-
dc.date.issued2020-05-13-
dc.identifier.urihttps://depositonce.tu-berlin.de/handle/11303/11453-
dc.identifier.urihttp://dx.doi.org/10.14279/depositonce-10334-
dc.description.abstractFollowing a screening of Antarctic glacier forefield-bacteria for novel cold-active enzymes, a psychrophilic strain Psychrobacter sp. 94-6PB was selected for further characterization of enzymatic activities. The strain produced lipases and proteases in the temperature range of 4–18°C. The coding sequence of an extracellular serine-protease was then identified via comparative analysis across Psychrobacter sp. genomes, PCR-amplified in our strain 94-6PB and expressed in the heterologous host E. coli. The purified enzyme (80 kDa) resulted to be a cold-active alkaline protease, performing best at temperatures of 20–30°C and pH 7-9. It was stable in presence of common inhibitors [β-mercaptoethanol (β-ME), dithiothreitol (DTT), urea, phenylmethylsulfonyl fluoride (PMSF) and ethylenediaminetetraacetic acid (EDTA)] and compatible with detergents and surfactants (Tween 20, Tween 80, hydrogen peroxide and Triton X-100). Because of these properties, the P94-6PB protease may be suitable for use in a new generation of laundry products for cold washing. Furthermore, we assessed the microdiversity of this enzyme in Psychrobacter organisms from different cold habitats and found several gene clusters that correlated with specific ecological niches. We then discussed the role of habitat specialization in shaping the biodiversity of proteins and enzymes and anticipate far-reaching implications for the search of novel variants of biotechnological products.en
dc.description.sponsorshipEC/H2020/657473/EU/Life at its Extremes: Biodiversity and Activity of Microorganisms in deep Permafrost/BioFrosten
dc.description.sponsorshipEC/H2020/764591/EU/Synthetic Circuits for Robust Orthogonal Production/SynCropen
dc.description.sponsorshipDFG, 5472008, SPP 1158: Bereich Infrastruktur - Antarktisforschung mit vergleichenden Untersuchungen in arktischen Eisgebietenen
dc.language.isoenen
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/en
dc.subject.ddc540 Chemie und zugeordnete Wissenschaftende
dc.subject.otherbioprospectingen
dc.subject.otherextremophilic bacteriaen
dc.subject.othercold-active enzymesen
dc.subject.othergenome miningen
dc.subject.otherheterologous protein expressionen
dc.subject.othermicrodiversityen
dc.titleDiscovery and Characterization of a New Cold-Active Protease From an Extremophilic Bacterium via Comparative Genome Analysis and in vitro Expressionen
dc.typeArticleen
dc.date.updated2020-05-13T07:05:49Z-
tub.accessrights.dnbfreeen
tub.publisher.universityorinstitutionTechnische Universität Berlinen
dc.identifier.eissn1664-302X-
dc.type.versionpublishedVersionen
dcterms.bibliographicCitation.doi10.3389/fmicb.2020.00881en
dcterms.bibliographicCitation.journaltitleFrontiers in Microbiologyen
dcterms.bibliographicCitation.originalpublisherplaceLausanneen
dcterms.bibliographicCitation.volume11en
dcterms.bibliographicCitation.originalpublishernameFrontiers Media S.A.en
dcterms.bibliographicCitation.articlenumber881en
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