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  <doc>
    <id>1851</id>
    <completedYear/>
    <publishedYear>2023</publishedYear>
    <thesisYearAccepted/>
    <language>eng</language>
    <pageFirst/>
    <pageLast/>
    <pageNumber/>
    <edition/>
    <issue/>
    <volume/>
    <type>masterthesis</type>
    <publisherName/>
    <publisherPlace/>
    <creatingCorporation/>
    <contributingCorporation/>
    <belongsToBibliography>0</belongsToBibliography>
    <completedDate>2023-12-21</completedDate>
    <publishedDate>--</publishedDate>
    <thesisDateAccepted>2023-10-31</thesisDateAccepted>
    <title language="eng">Survey of Eutheria for Alternative Caseins  Suitable for  Recombinant Production</title>
    <abstract language="eng">Caseins are the most abundant protein component in mammalian milk, and they are released as calcium-rich micelles. These phosphoproteins originate from four genes responsible for encoding αs1, αs2, β, and κ-caseins in the case of Bos taurus. Remarkably, the relative proportions of these caseins vary significantly among different species. Moreover, the primary sequences of αs1, αs2, and β-caseins exhibit substantial inter-species diversity, indicating a rapid evolutionary process stemming from a common precursor gene. In contrast, κ-caseins possess distinctive characteristics, implying a separate origin and role in stabilizing micelle structures.&#13;
&#13;
The precision fermentation industry has long focused on the recombinant production of bovine caseins. However, the milk composition of placental mammals exhibits substantial variability in protein, fat, and sugar content, as well as diverse casein gene orthologs. This variability raises the possibility of alternative casein forms within Eutheria, which may be better suited for deployment in recombinant expression systems.&#13;
&#13;
In the pursuit of this objective, the selection of β-casein and κ-casein proteins from various mammalian species was undertaken for recombinant production in Pichia pastoris.</abstract>
    <enrichment key="opus.source">publish</enrichment>
    <licence>CC BY-NC-ND 4.0 International - Namensnennung-Nicht kommerziell-Keine Bearbeitungen</licence>
    <author>Shalinee Matadeen Sen</author>
    <collection role="institutes" number="">Fakultät Life Sciences</collection>
    <thesisPublisher>Hochschule Rhein-Waal</thesisPublisher>
    <thesisGrantor>Hochschule Rhein-Waal</thesisGrantor>
  </doc>
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