Optimization and Immobilization of Purified Laheo rohita Visceral Protease by Entrapment Method
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Date
2012
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Abstract
lire purified fish visceral protease enzyme was immobilized by using various concentrations of sodium alginate and calcium
chloride to optimize the best concentration for the formation of the beads. Then it was characterized by assaying the cjptimal pH.
temperature, storage stability and reusability. The results on immobilization with sodium alginate and calcium chloride ^howed that
a combination of 2% sodium alginate and 0.3 M calcium chloride weas found to be the optimum concentration for the formation
of spherical and stable beads, this gave a maximal entrapped activity of 48.31%, and there was no change in the optimum pH 8.0
and temperature 40*C of protease before and after entrapment. The results on stability and reusability indicated that it was stable
at 4‘C retaining 100% rc.sidual activity after 5 days of storage and 67% loss of activity after ten days of storage and it retained 100%
residual activity on the first reuse, 75% residual acthity on the second reuse, 25% residual activity on the third use and complete
loss in the activity on the fourth reuse.