[{
  "type": "article-journal",
  "title": "SOLUBLE EXPRESSION OF BACILLUS LICHENIFORMIS ATCC 27811 α-AMYLASE AND CHARACHTERIZATION OF PURIFIED RECOMBINANT ENZYME",
  "author": [
    {
      "family": "Muazzam",
      "given": ""
    },
    {
      "family": "2",
      "given": ""
    },
    {
      "family": "Malik",
      "given": ""
    },
    {
      "family": "Rashid",
      "given": ""
    },
    {
      "family": "Irshad",
      "given": ""
    },
    {
      "family": "Fatima",
      "given": ""
    }
  ],
  "issued": {
    "date-parts": [[2019]]
  },
  "container-title": "Journal of Animal and Plant Sciences",
  "ISSN": "1018-7081",
  "volume": "29",
  "issue": "1",
  "page": "99-108",
  "DOI": "N/A",
  "abstract": "<p>Alpha amylase (&alpha;-amylase) from<em>&nbsp;Bacillus licheniformis</em>&nbsp;shows great role in starch hydrolysis for industrial application due to its thermostability, long half-life and specificity. However, it is difficult to produce this enzyme in large quantities because of formation of inclusion bodies, but lowering the temperature to 18 &deg;C leads to a soluble expression of protein. This also&nbsp;highlighted the efficacy of&nbsp;<em>Escherichia coli</em>&nbsp;as one of the best host for secretion of recombinant proteins. A further study to find an approach for a soluble expression of &alpha;-amylase was conducted here, using pET-22b(+)&nbsp; as an expression vector and temperature optimization. Purified monomeric enzyme displayed a specific activity of 584.61 U/mg at 37 &deg;C and a molecular mass of 52&nbsp;<em>kDa</em>. Purification fold of recombinant &alpha;-amylase was 2.04 times in comparison to crude amylase extract.&nbsp; Relative activity of enzymewas remarkably enhanced by Ca+2 but strongly impeded by Cu2+ and Na+1, highlighted the significance of Ca+2 as a cofactor for optimal amylase activity.</p>",
  "publisher": "Pakistan Agricultural Scientists Forum",
  "URL": "https://thejaps.org.pk/AbstractView.aspx?mid=Bioch-17-0026"
}]