Abstract
The present study was aimed to exploit the free and immobilized peroxidase from Nigella sativa seeds to degradation of textile dyes polluting the environment and water. The optimum conditions for extracting the enzyme from the Nigella seeds were determined and the highest specific activity of the enzyme was obtained 1750 units / mg protein when extracting the enzyme from the ground seeds at a ratio of 1:20 (w: v) with sodium acetate buffer at 0.2 M and pH 5.0 for 15 minutes. The enzyme was purified using two steps including the concentration by sucrose and gel filtration by using Sephadex G-150. The results shown an increase in final purification folds 2.8 time with an enzyme yield of 35%. The immobilization of peroxidase were done by entrapment method using Ca- alginate and the immobilization ratio was reached to 49%. The removal efficiency of dyes by crude enzyme (free, immobilized) and partial purified peroxidase were studied with textile dyes such as yellow, red, black and blue dyes at optimum conditions pH 5, temperature 37oC after 3 hr. Maximum removal efficiency of dyes observed with crude peroxidase and reached (76.9, 88.7, 91 and 88) % respectively. These results were close to the efficiency of the purified enzyme in removing the four dyes, while the efficiency of the crude immobilized enzyme in removing the dyes was about (70, 81, 72 and 56.4)%, respectively.
Highlights
Peroxidase enzymes are widely distributed in plants, animal tissue and microorganisms. )Peroxidase was first found in the fig tree in 1936
The enzyme activity, protein concentration and specific activity were estimated in each experiment
Enzyme concentration by sucrose The crude enzyme solution was concentrated by sucrose using dialysis tubes, was taken to measure the enzyme activity, protein concentration and the specific activity
Summary
Peroxidase enzymes (donor: H2O2 Oxidoreductase, EC. 1.11.1.7) are widely distributed in plants, animal tissue and microorganisms. )Peroxidase was first found in the fig tree in 1936. Extraction ratio: One gram of black seed was homogenized in different volumes of 0.2 M sodium acetate buffer pH 5 for extraction the peroxidase for 15 min at 30oC. Extraction time: One gram of black seed was homogenized with 0.2 M sodium acetate buffer pH 5 in different time include 15, 30, and 60 min at 30 oC. Purification of peroxidase The peroxidase was purified from black seed using dialysis method for enzyme concentration, followed by gel filtration. 30 ̊C for 15 min Type of extraction buffer The specific activity of peroxidase was estimated after extraction using different buffers, and the results were illustrated in (Fig. 2) These results show that sodium acetate buffer (0.2 M, pH 5.0) was best extraction buffer with specific activity 1584 U/mg protein.
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