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        <identifier>oai:www.ideals.illinois.edu:2142/73046</identifier>
        <datestamp>2023-07-11</datestamp>
        <setSpec>col_2142_11615</setSpec>
        <setSpec>col_2142_5131</setSpec>
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        <setSpec>com_2142_8903</setSpec>
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          <dc:subject>poly-mannuronate (polyM)</dc:subject>
          <dc:subject>heteropolymeric M/G (polyMG)</dc:subject>
          <dc:contributor>Rao, Christopher V.</dc:contributor>
          <dc:creator>Badur, Ahmet</dc:creator>
          <dc:date>2015-01-21T19:58:51Z</dc:date>
          <dc:date>2015-01-21T19:58:51Z</dc:date>
          <dc:date>2017-01-22T10:15:38Z</dc:date>
          <dc:date>2014-12</dc:date>
          <dc:date>2015-01-21</dc:date>
          <dc:date>2014-12</dc:date>
          <dc:description>lginate is a polysaccharide found within brown seaweeds and has been
targeted as a carbon source for biofuel production. Alginate consists of α-L-guluronate
(G) and β-D-mannuronate (M) linked in various patterns, which results in either a homo-
or heteropolymeric structure. Alginate lyases are enzymes that degrade the linkage
between G and M blocks and can have specificity to either polyG, polyM, or polyMG
block degradation. The marine bacterium Vibrio splendidus 12B01 contains four
putative alginate lyases which were investigated in this study. We identified, purified,
and characterized the four PL7 alginates lyases. We found that these lyases have
optimal activity between pH 7.5-8.5 and 20-25°C, consistent with use in a marine
environment. Additionally, Ca 2+ is necessary for optimal enzyme activity. The binding
constant (K m ) of the lyases toward alginate was found to be between 22 and 123 mM
alginate and the maximum reaction rate (V max ) was found to be between 0.13 and 0.83
μM s -1 . The turnover numbers for the lyases was found to be between 0.60 and 7.1 s -1 .</dc:description>
          <dc:description>Item withdrawn by Laura Spradlin (lspradl2@illinois.edu) on 2014-11-07T22:14:27Z
Item was in collections:
University of Illinois Theses &amp; Dissertations (ID: 1)
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          <dc:description>Embargo set by: Seth Robbins for item 73235
Lift date: 2017-01-21T19:59:39Z
Reason: Author requested closed access (OA after 2yrs) in Vireo ETD system</dc:description>
          <dc:description>Limited Restriction Lifted for Item 73235 on 2017-01-22T10:15:38Z.</dc:description>
          <dc:identifier>http://hdl.handle.net/2142/73046</dc:identifier>
          <dc:language>en</dc:language>
          <dc:rights>Copyright 2014 Ahmet Badur</dc:rights>
          <dc:subject>Vibrio splendidus</dc:subject>
          <dc:subject>Vibrio splendidus 12B01</dc:subject>
          <dc:subject>alginate</dc:subject>
          <dc:subject>alginate lyase</dc:subject>
          <dc:subject>poly-guluronate (polyG)</dc:subject>
          <dc:subject>polyGM</dc:subject>
          <dc:subject>AlyA</dc:subject>
          <dc:subject>AlyB</dc:subject>
          <dc:subject>AlyC</dc:subject>
          <dc:subject>AlyD</dc:subject>
          <dc:subject>AlyE</dc:subject>
          <dc:title>Over-expression and characterization of four alginate lyases from vibrio splendidus 12B01</dc:title>
          <dc:type>text</dc:type>
          <degree>
            <department>Chemical &amp; Biomolecular Engr</department>
            <departmentCode>1687</departmentCode>
            <discipline>Chemical Engineering</discipline>
            <disciplineCode>0300</disciplineCode>
            <grantor>University of Illinois at Urbana-Champaign</grantor>
            <level>Thesis</level>
            <name>M.S.</name>
            <program>MS:Chemical Engineering -UIUC</program>
            <programCode>10KS0300MS</programCode>
          </degree>
        </thesis>
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