BackgroundChitin is the main structural component of cell walls of fungi, exoskeletons of insects and other arthropods and shells of crustaceans. Chitinase enzyme is capable of degrading chitin, and this enzyme can be used as a biological fungicide against phytopathogenic fungi, as well as an insecticide against insect pests.MethodsIn this study, 158 isolates, which were derived from bacteria cultures isolated from leaves and root rhizospheres of certain plants in Turkey, were selected after confirming that they are not phytopathogenic based on the hypersensitivity test performed on tobacco; and antifungal activity test was performed against Fusarium culmorum, which is a pathogenic fungi that cause decomposition of roots of vegetables. Accordingly, chitinase enzyme activity assay was performed on 31 isolates that have an antifungal activity, and among them the isolate of Bacillus subtilis TV-125 was selected, which has demonstrated the highest activity.ResultsChitinase enzyme was purified by using ammonium sulphate and DEAE-sephadex ion exchange chromatography. Ammonium sulphate precipitation of chitinase enzyme from Bacillus subtilis TV-125 isolate was performed at maximum range of 0-20%, and 28.4-fold purification was obtained with a 13.4% of yield. Optimum activity of the purified enzyme was observed at pH 4.0 and at 50°C of temperature. In addition, it was identified that Bacillus subtilis TV-125A isolate retains 42% of its activity at 80°C temperature.ConclusionIn the last phase of the study, chitinase enzyme purified from Bacillus subtilis TV-125A was tested on four fungal agents, although all the results were positive, it was particularly effective on F. culmorum according to the findings.

Phytases (myo-inositol hexakisphosphate phosphohydrolase, EC 3.1.3.8) catalyze the release of phosphate from phytates. Many of the cereal grains, legumes and oilseeds store phosphorus in phytate form. Phytases can be produced by plants, animals and microorganisms. However, the ones with microbial origin are the most promising for commercial uses and biotechnological applications. In this study, phytase enzyme isolation from Lactobacillus spp. ATCC strain and its characterization was carried out. Phytase production from bacterial strains was determined by zone production formed around colonies after 48 h of incubation at 30°C in MRS medium. Optimum pH and optimum temperature values of the phytase enzyme that was partially purified by precipitation of ammonium sulphate from Lactobacillus plantarum, extracellularly from bacteria put into liquid culture medium, were measured. Optimum activity of the enzyme derived from L. plantarum bacterium was at 30°C and pH 6.0. It was observed that L. plantarum's extracellular enzyme maintains its 90% of activity at 10-100°C for 120 min. Effects of certain metal ions on activity of phytase enzyme derived from L. plantarum were also investigated. Of these, CuCl 2 , MnCl 2 , CoCl 2 , CaCl 2 and ZnCl 2 decreased enzyme activity significantly. FeCl 2 increased enzyme activity by 121%. Based on these results, the phytase enzyme of L. plantarum is considered suitable for use in many industrial areas, in feed and food industries in particular, due to its thermal stability and resistance to metal ions.