Molecular Study and optimization alkaline protease from bacillus isolates

رجبلو, حميدرضا and زهري, دکتر صابر and اسدي, دكتر اسدالله (2011) Molecular Study and optimization alkaline protease from bacillus isolates. Masters thesis, University of Mohaghegh Ardabili.

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Abstract

Proteases are one of the industrially most important enzymes. Protease have found a wide range of applications in various industries such as food, detergent, pharmaceutical, leather, etc. They are usually produced by bacteria belong to the genus Bacillus for industrial application. In this study, an alkaliphilic protease producing bacterium, Bacillus sp. , was isolated from sabalan spring. The enzyme was active in the pH 7-12, with optimum activity at pH 9, although a small peak at pH 4 was also observed, Suggesting a presence of two protease. The enzyme was active in the temperatures range of 20-90˚C with maximum activity at 60˚C. The protease was markedly inhibited by Zn+2, Ba+2, Cu+2, Co+2; while partially inhibited by Fe+2, Na+2. Also Mn+2, Mg+2 and Ca+2 stimulated the enzyme activity. The crude enzyme preparation show many protein bands. Of the inhibitor tested (at 5mM concentration), EDTA was able to inhibit the protease, while PMSF exhibited partially inhibition. It can, therefore, be concluded that the protease studied in the present case, is a metal-activated enzyme with a loose interaction with metal, and which seems to have a serine residue at the active site. The km and specific activity of that on soluble casein were 1.625 mg/ml and 11443.082 U/mg, respectively. The enzyme had good biochemical characteristic such as stability in high temperatures and pH.

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