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    <record>
      <ref-type name="Journal Article">17</ref-type>
      <contributors>
        <authors>
          <author>B. Fatima</author>
          <author>Z. Hussain</author>
        </authors>
      </contributors>
      <titles>
        <title>XYLOSE ISOMERASES FROM THERMOTOGALES</title>
        <secondary-title>Journal of Animal and Plant Sciences</secondary-title>
        <alt-title>JAPS</alt-title>
      </titles>
      <dates><year>2015</year><pub-dates><date>2015/02/01</date></pub-dates></dates>
      <volume>25</volume>
      <number>1</number>
      <pages>10-18</pages>
      <isbn>1018-7081</isbn>
      <electronic-resource-num>NA</electronic-resource-num>
      <abstract>&lt;p&gt;Biotechnology has been directed primarily towards reproductive technology been employed for improvement of&lt;br&gt;industrial important enzymes which are foremost concern over the years for researchers. This review paper discusses the&lt;br&gt;exciting scientific and technical advances in molecular biology for the genetic improvement in thermotogales, the&lt;br&gt;hyperthermophiles with respect to xylose isomerase to meet the industrial demands. A thermo-acid stable enzyme&lt;br&gt;possesses neutral or slightly acidic pH optima and a higher affinity for glucose have a potential for industrial applications&lt;br&gt;for the production of high fructose corn syrup (HFCS). Xylose isomerases from Thermotoga sp are class II enzymes,&lt;br&gt;utilize a 1, 2 hydride shift catalytic mechanism, active only in the presence of Mn+2, Co+2 and Mg+2&lt;br&gt;. Recombinant xylose&lt;br&gt;isomerases from T. neapolitana existed both as homodimer as well as homotetramer have been produced under&lt;br&gt;mesophilic fermentation conditions, with a maximal activity at 97&amp;deg;C. Mutant enzyme in addition to this catalytically&lt;br&gt;active at pH 5.5 and showed 3.1 fold increased catalytic efficiency towards glucose. The addition of the carbohydrate&lt;br&gt;biding domain to Thermotoga&amp;rsquo;s xylose isomerase successfully immobilized the enzyme to chitin beads. The turnover&lt;br&gt;numbers (kcat) for glucose to fructose conversion for both unbound and immobilized mutants was greater than the wildtype enzyme.&lt;/p&gt;</abstract>
      <keywords><keyword>xylose isomerases, thermotogales, hyperthermophiles</keyword></keywords>
      <publisher>Pakistan Agricultural Scientists Forum</publisher>
      <urls><related-urls><url>https://thejaps.org.pk/AbstractView.aspx?mid=2015-JAPS-02</url></related-urls></urls>
    </record>
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