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Enzyme Research
Volume 2013 (2013), Article ID 874050, 7 pages
Research Article

Optimization and Immobilization of Purified Labeo rohita Visceral Protease by Entrapment Method

Department of Biochemistry, Biotechnology and Bioinformatics, Avinashilingam Institute of Home Science and Higher Education for Women, Coimbatore, Tamil Nadu 641 043, India

Received 18 December 2012; Accepted 22 January 2013

Academic Editor: Robert Pike

Copyright © 2013 S. Geethanjali and Anitha Subash. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


The 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 optimal pH, temperature, storage stability and reusability. The results on immobilization with sodium alginate and calcium chloride showed 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% residual 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 activity on the second reuse, 25% residual activity on the third use and complete loss in the activity on the fourth reuse.