National Academy of Agricultural Sciences (NAAS)
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PRINT ISSN : 2319-7692
Online ISSN : 2319-7706 Issues : 12 per year Publisher : Excellent Publishers Email : editorijcmas@gmail.com / submit@ijcmas.com Editor-in-chief: Dr.M.Prakash Index Copernicus ICV 2018: 95.39 NAAS RATING 2020: 5.38 |
The present work was undertaken to obtain crude Peroxidase extract from radish to characterize it in terms of pH, temperature, number of times use and decolrization of some dyes. The results shows that peroxidase from radish gave highest specific activity 4391 U/mg, and potassium phosphate buffer (0.1 M, pH 7) was best extraction buffer for peroxidase extraction from radish with specific activity 4489 U/mg, while The highest specific activity was measured for crude extract at 1:2 ratio, it was 4479 U/mg protein. Entrapment of peroxidase enzyme by agarose was best method for immobilization. The optimum pH of free and immobilized peroxidase enzyme activity was 6.0, while the pH stability of free peroxidase enzyme from radish was 6.0, and the pH stability of immobilized peroxidase enzyme was range from 4.0-8.0. The optimum temperature for free peroxidase activity from radish was 35 á´¼C, while the free enzyme was stable in temperature 35-60 áµ’C, then the activity begun to decrease and was completely lost in 65-70áµ’C. The best temperature for immobilized peroxidase activity was 35 áµ’C, while the results showed that the immobilized enzyme was stable in temperatures between 35-45 áµ’C. The activity of the immobilized enzyme which incubated many times with substrate was decreased after eighth time using. Giemsa stain and acridine orange, were removed and make change in their absorbance after incubation with immobilized eighth enzyme for period of time, while no degradation of the other dyes occur.
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