• Coimmobilization of D-amino acid oxidase and catalase by entrapment ofTrigonopsis variabilis in radiation polymerised Polyacrylamide beads

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    • Keywords

       

      Coimmobilization; D-amino acid oxidase; Trigonopsis variabilis ; Polyacryl-amide beads

    • Abstract

       

      Trigonopsis variabilis induced for D-amino acid oxidase and catalase was immobilized by entrapment in Polyacrylamide beads obtained by radiation polymerisation. Permeabilization of the cells was found to be essential for optimal activity of the enzymes in free cells. However, the process of entrapment itself was found to eliminate the permeability barrier of cells immobilized in Polyacrylamide. The two enzymes exhibited a differential response on Polyacrylamide entrapment. Thus, D-amino acid oxidase activity was stabilized to heat inactivation whereas catalase in the same cells showed a destabilization on entrapment in Polyacrylamide. The coimmobilized enzyme preparation showed an operational half life of 7–9 days after which the D-amino acid oxidase activity remained stable at a value 35–40% of that of the initial activity for a study period of 3 weeks. Coimmobilization of MnO2 was not effective in enhancing the operational life of the enzyme preparation.

    • Author Affiliations

       

      Ashwini Deshpande1 S F D’souza1 G B Nadkarni1

      1. Food Technology and Enzyme Engineering Division, Bhabha Atomic Research Centre, Bombay - 400 085, India
    • Dates

       
  • Journal of Biosciences | News

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