Immobilization of Haloferax mediterranei aldolase by cross-linking in a proteinic matrix: stability and halophilic characteristics |
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Authors: | D'Souza S.E. Altekar W. D'Souza S.F. |
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Affiliation: | (1) Radiation Biology and Biochemistry Division of Bhabha Atomic Research Centre, Trombay, Mumbai, 400 085, India |
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Abstract: | Fructose-1,6-bisphosphate (FBP) aldolase (EC 4.1.2.13) of Haloferax mediterranei was immobilized by treating the cell extract in the presence of 10% BSA, with the cross-linking reagent, 0.5% glutaraldehyde for 15min, with the retention of 60% of its original activity. The immobilized preparation exhibited a shift in the temperature optimum from 55°C to 65°C. The enzyme showed enhanced stability towards inactivation by radiation and storage (0–5°C) on immobilization. Immobilization also made the enzyme less halophilic, reducing its denaturation on prolonged storage in a non-salt medium, as well as exhibiting optimal activity at a lower KCl concentration (0.5m) as compared to the soluble enzyme (1–2m). |
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Keywords: | Cross-linking fructose-1 6-bis phosphate (FBP) aldolase Haloferax mediterranei halophilic immobilized |
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