<oai_dc:dc xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:oai_dc="http://www.openarchives.org/OAI/2.0/oai_dc/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/oai_dc/ http://www.openarchives.org/OAI/2.0/oai_dc.xsd">
  <dc:creator>Wenger, Alexander</dc:creator>
  <dc:creator>Schmidt, Remo S.</dc:creator>
  <dc:creator>Portmann, Reto</dc:creator>
  <dc:creator>Roetschi, Alexandra</dc:creator>
  <dc:creator>Eugster, Elisabeth</dc:creator>
  <dc:creator>Weisskopf, Laure</dc:creator>
  <dc:creator>Irmler, Stefan</dc:creator>
  <dc:date>2020-05-29</dc:date>
  <dc:description xmlns:ns0="xml" ns0:lang="en">During cheese ripening, the bacterial strain Pediococcus acidilactici FAM18098  produces the non-proteinogenic amino acid, α-aminobutyrate (AABA). The metabolic  processes that lead to the biosynthesis of this compound are unknown. In this study,  10 P. acidilactici, including FAM18098 and nine Pediococcus pentosaceus strains,  were screened for their ability to produce AABA. All P. acidilactici strains produced  AABA, whereas the P. pentosaceus strains did not. The genomes of the pediococcal  strains were sequenced and searched for genes encoding aminotransferases to test  the hypothesis that AABA could result from the transamination of α-ketobutyrate. A  GenBank and KEGG database search revealed the presence of a species-specific  aminotransferase in P. acidilactici. The gene was cloned and its gene product was  produced as a His-tagged fusion protein in Escherichia coli to determine the substrate  specificity of this enzyme. The purified recombinant protein showed aminotransferase  activity at pH 5.5. It catalyzed the transfer of the amino group from leucine,  methionine, AABA, alanine, cysteine, and phenylalanine to the amino group acceptor  α-ketoglutarate. Αlpha-ketobutyrate could replace α-ketoglutarate as an amino group  acceptor. In this case, AABA was produced at significantly higher levels than  glutamate. The results of this study show that P. acidilactici possesses a novel  aminotransferase that might play a role in cheese biochemistry and has the potential  to be used in biotechnological processes for the production of AABA.</dc:description>
  <dc:format>application/pdf</dc:format>
  <dc:identifier>https://folia.unifr.ch/global/documents/309064</dc:identifier>
  <dc:identifier>https://folia.unifr.ch/documents/309064/files/wen_iss.pdf</dc:identifier>
  <dc:identifier>https://folia.unifr.ch/documents/309064/files/wen_iss_sm.txt</dc:identifier>
  <dc:language>eng</dc:language>
  <dc:relation>info:eu-repo/semantics/altIdentifier/doi/10.1186/s13568-020-01034-2</dc:relation>
  <dc:rights>info:eu-repo/semantics/openAccess</dc:rights>
  <dc:rights>License undefined</dc:rights>
  <dc:source>AMB Express. - 2020, vol. 10, no. 1, p. 100</dc:source>
  <dc:subject>info:eu-repo/classification/udc/57</dc:subject>
  <dc:title xmlns:ns1="xml" ns1:lang="en">Identification of a species-specific aminotransferase in Pediococcus acidilactici capable of forming α-aminobutyrate</dc:title>
  <dc:type>http://purl.org/coar/resource_type/c_6501</dc:type>
</oai_dc:dc>
