Isolation, characterization and determination of alkaline protease activity of Bacillus genus from the various proteolytic substrates
2018
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Advisor: Prof. Dr. Abdurrahman Üsame Tamer
Abstract (EN)
In this study, we were performed isolation of the alkaline protease producer bacteria and the most active enzyme producer strains (economically valuable) was intended to obtain. The soil samples were collected from 14 different stations which is inside the Izmir, Manisa and Aydın provinces border. We used dilution and petri plate method was for bacteria isolation. Biochemical tests and API test kits were applied to the izolates, which was selected according to the hydrolyzed casein zones. 2 isolates (S9-UKM and S11-UKM) were selected, which was predicted to be involved in Bacillus genus, and spectrophotometric method was used to identification of the enzyme activity. During the study, different incubation time, medium temperature, medium pH, carbon and nitrogen sources was tried. Maximum protease activity for S9-UKM isolate was reached at the end of the third day and in the conditions of 300C, pH 8.0, fructose as carbone source and skim milk as nitrogen source. Also, maximum protease acitivity for S11-UKM isolate was reached at the end of the third day and in the conditions of 330C, pH 7.2, maltose as carbone source and yeast extract as nitrogen source. Usage of proteases area have increased quite progressively. Proteases are used almost in every area and importance of these enzymes will increased in the future. The results obtained from the study, it is shown that there may be differences in the parameters of alkaline protease production among the same bacterias, which is in the same genus. With this type of studies, importance of detection of the most suitable organism putted forward.
Author
Umut Kovancılar
Institution
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Umut Kovancılar (Master Thesis). Isolation, characterization and determination of alkaline protease activity of Bacillus genus from the various proteolytic substrates, 2018, Manisa Celal Bayar University.
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