Coimmobilization of D-amino acid oxidase and catalase by entrapment of Trigonopsis variabilis in radiation polymerised Polyacrylamide beads.
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Date
1987-03
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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.
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Keywords
Coimmobilization, D-amino acid oxidase, Trigonopsis variabilis, Polyacrylamide beads
Citation
Despande Ashwini, D'Souza S F, Nadkarni G B. Coimmobilization of D-amino acid oxidase and catalase by entrapment of Trigonopsis variabilis in radiation polymerised Polyacrylamide beads. Journal of Biosciences. 1987 Mar; 11(1-4): 137-144.