1 Ocak 2021 Dergi makalesi Açık Erişim

Bostan, Fatmanur; Surmeli, Nur Basak

MARC21 XML

<?xml version='1.0' encoding='UTF-8'?>
<record xmlns="http://www.loc.gov/MARC21/slim">
  <leader>00000nam##2200000uu#4500</leader>
  <datafield tag="260" ind1=" " ind2=" ">
    <subfield code="c">2021-01-01</subfield>
  </datafield>
  <datafield tag="100" ind1=" " ind2=" ">
    <subfield code="u">Izmir Inst Technol, Program Biotechnol &amp; Bioengn, Gulbahce, Urla Izmir, Turkey</subfield>
    <subfield code="a">Bostan, Fatmanur</subfield>
  </datafield>
  <datafield tag="540" ind1=" " ind2=" ">
    <subfield code="u">http://www.opendefinition.org/licenses/cc-by</subfield>
    <subfield code="a">Creative Commons Attribution</subfield>
  </datafield>
  <datafield tag="700" ind1=" " ind2=" ">
    <subfield code="u">Izmir Inst Technol, Dept Bioengn, Gulbahce, Urla Izmir, Turkey</subfield>
    <subfield code="a">Surmeli, Nur Basak</subfield>
  </datafield>
  <datafield tag="909" ind1="C" ind2="O">
    <subfield code="o">oai:aperta.ulakbim.gov.tr:239228</subfield>
    <subfield code="p">user-tubitak-destekli-proje-yayinlari</subfield>
  </datafield>
  <datafield tag="542" ind1=" " ind2=" ">
    <subfield code="l">open</subfield>
  </datafield>
  <datafield tag="520" ind1=" " ind2=" ">
    <subfield code="a">Silk consists of two proteins called fibroin and sericin. While fibroin is used in the textile industry and has various biomaterial applications, sericin has been considered as waste material until recently. Sericin is a multicomponent protein and it has important properties such as biocompatibility, biodegradability, cryoprotectivity, and antioxidant. Sericin from silkworm cocoons can be obtained by chemical, enzymatic, and heat treatment methods. However, sericin obtained with these treatment methods is not of consistent and high quality. Moreover, the exposure of sericin to harsh conditions during extraction leads to inconsistencies in the composition and structure of the sericin obtained. The inconsistencies in sericin structure and composition decrease application of sericin as a biomaterial. Here, we produce a sericin-like protein (Ser4mer) with native sequence of sericin encoding four repeats of the conserved 38 amino acid motif recombinantly in Escherichia coli and characterize its structural properties. Ser4mer protein shows similar structure to native sericin and higher solubility than previously obtained recombinant sericin-like proteins. Recombinant production of a soluble sericin-like protein will significantly expand its applications as a biomaterial. In addition, recombinant production of silk proteins will allow us to understand sequence-structure relationships in these proteins.</subfield>
  </datafield>
  <datafield tag="024" ind1=" " ind2=" ">
    <subfield code="a">10.1002/bab.2089</subfield>
    <subfield code="2">doi</subfield>
  </datafield>
  <controlfield tag="005">20221007102904.0</controlfield>
  <datafield tag="245" ind1=" " ind2=" ">
    <subfield code="a">Cloning, expression, and characterization of a novel sericin-like protein</subfield>
  </datafield>
  <datafield tag="909" ind1="C" ind2="4">
    <subfield code="p">BIOTECHNOLOGY AND APPLIED BIOCHEMISTRY</subfield>
  </datafield>
  <datafield tag="650" ind1="1" ind2="7">
    <subfield code="2">opendefinition.org</subfield>
    <subfield code="a">cc-by</subfield>
  </datafield>
  <controlfield tag="001">239228</controlfield>
  <datafield tag="980" ind1=" " ind2=" ">
    <subfield code="a">user-tubitak-destekli-proje-yayinlari</subfield>
  </datafield>
  <datafield tag="980" ind1=" " ind2=" ">
    <subfield code="b">article</subfield>
    <subfield code="a">publication</subfield>
  </datafield>
  <datafield tag="856" ind1="4" ind2=" ">
    <subfield code="u">https://aperta.ulakbim.gov.trrecord/239228/files/bib-fb95eb0f-bb40-4d93-9655-01b120048e88.txt</subfield>
    <subfield code="z">md5:4aa0e5d7bbfecb2cf23993f66cfa71c7</subfield>
    <subfield code="s">147</subfield>
  </datafield>
</record>