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