• Title of article

    Bench scale production of nicotinic acid using a versatile amide-hydrolysing Geobacillus subterraneus RL-2a isolated from thermal spring of Manikaran, India

  • Author/Authors

    Mehta، نويسنده , , Praveen Kumar and Bhatia، نويسنده , , Shashi Kant and Bhatia، نويسنده , , Ravi Kant and Bhalla، نويسنده , , Tek Chand Bhalla، نويسنده ,

  • Issue Information
    روزنامه با شماره پیاپی سال 2014
  • Pages
    8
  • From page
    58
  • To page
    65
  • Abstract
    A new thermostable amidase-producing isolate identified as Geobacillus subterraneus RL-2a has been studied extensively for the optimization of enzyme operational conditions in the production of nicotinic acid in fed batch mode. The amidase of G. subterraneus RL-2a is constitutive in nature, active at broad pH (pH 4.5–13.0), temperature (40–90 °C) with optimal activity at 70 °C and pH 6.5. The enzyme was fairly stable at 70 °C with a deactivation constant (kd) and enzyme half-life of 4.15 × 10−5 s−1 and 6 h 4 min. Another advantage of this enzyme was its broad substrate specificity, including aliphatic, aromatic and amino acid amides respectively. In a fed batch reaction at one litre scale using resting cells corresponding to 8 U ml−1 amidase activity (7.76 mg dcw ml−1), a total of 88.6 g nicotinic acid was produced at a rate of 2.85 g h−1 g−1 dcw. This thermostable amidase represents the first reported broad substrate spectrum amidase with exceptional thermostability from a thermophilic G. subterraneus RL-2a.
  • Keywords
    Thermostable , Acyl transfer activity , amidase , Geobacillus subterraneus RL-2a , Isolation , Nicotinic acid
  • Journal title
    Journal of Molecular Catalysis B Enzymatic
  • Serial Year
    2014
  • Journal title
    Journal of Molecular Catalysis B Enzymatic
  • Record number

    1718847