Leinamycin is a thiol dependent DNA alkylating agent which shows very potent activity against various cancer cell lines. This natural compound forms guanine adducts (N7) in DNA which are converted into a basic sites and simultaneously generates Reactive Oxygen Species (ROS), to produce DNA strand breaks in human cancer cells. In present study, eight different strains isolated from Iraqi soils were taxonomically assigned as Streptomyces.atroolivaceous. Remarkably the strain named as THS-44 was distinguished in productivity in comparison with other strains; the amount of leinamycin was 50.98 mg/l. In this study, we assessed the cytotoxic activity of leinamycin against RD and ANM3 cancer cell line in compare with REF cell line as a normal control. leinamycin revealed a potent activity against growth of both RD , and AMN3 cell lines with inhibition rate 93.56%, and 86.67%) respectively at 100mg/ml as a highest concentration. Moreover, leinamycin from HS-44 strain was mediate apoptotic effects on cancer cells without affecting on the normal cell line REF; a clear cut difference in the % of fragmented DNA was found between both RD, and AMN3 malignant cells, and REF normal cell line (89.16, and 83.1466, and 13.75; p< 0.001, and p< 0.001) respectively after exposure to 4.5μg/ml, leinamycin for 24hrs of incubation period.
Endoglucanase produced from Aspergillus flavus was purified by several steps including precipitation with 25 % ammonium sulphate followed by Ion –exchange chromatography, the obtained specific activity was 377.35 U/ mg protein, with a yield of 51.32 % .This step was followed by gel filtration chromatography (Sepharose -6B), when a value of specific activity was 400 U/ mg protein, with a yield of 48 %. Certain properties of this purified enzyme were investigated, the optimum pH of activity was 7 and the pH of its stability was 4.5, while the temperature stability was 40 °C for 60 min. The enzyme retained 100% of its original activity after incubation at 40 °C for 60 min; the optimum temperature for enzyme activity was 40 °C.
Twenty isolates of Serratia marcescens were isolated from inflammation of the urinary tract (UTI)., These isolates were found to produce hemolysin as indicated by blood agar plates in which the hemolysis of red blood cell indicate a positive result. Isolates were selected according to their hemolysis activity by measuring absorbance of hemoglobin at 405 nm that released from red blood cell. Hemolysin was completely purified using 50-75% saturation of ammonium sulphate followed by ion exchange chromatography with DEAE-cellulose then gel filtration chromatography by sepharose 4B. Accordingly molecular weight for the purified toxin was estimated as 45 KD.
Six isolates of Bacillus thuringiensis were isolated from Iraqi soil characterized as non- insecticidal and non- hemolytic parasporal inclusion proteins. Bacterial isolates were propagated on nutrient broth. Then, the parasporal inclusion proteins were extracted and processed with proteinase K and trypsin. The major protein segments produced of 64KDa were characterized and tested for cytocidal activity against human leukemic T- cells (CLL) (Chronic lymphoid leukemia). Results indicated that the treated parasporal proteins of four isolates (Bt2, Bt3, Bt4 and Bt6) showed strong cytotoxicity with no significant differences between normal lymphocytes and leukemic lymphocytes. Two isolates BtA1 and BtA5 show discriminative cytotoxicity between n
... Show MoreSixty four local isolated of Klebsiella spp. have been isolated from environment samples (soil and water). These isolates were identified and diagnosis according to phenotype and biochemical tests. These isolates were subjected to primary and secondary screening, to select the isolate with the highest laccase activity. Fifteen isolates chosen from primary screening for screening their enzyme activity in secondary screening. It has been found the Klebsiella(K7) has the highest productivity of the enzyme (12 Unit/ml).Klebsiella(K7) isolate was diagnosis by Vitak 2 system, it was identified asK. pneumonia. The laccase purified was characterization, the experiments showed that: The molecular weight of laccase was 120KD and the optimum pH for th
... Show MoreImidacloprid is systemic insecticide (1-[(6-chloro-3-pyridinyl) methyl]-N-nitro-2-imidazolidinimine) and the world’s most widely used has significant efficacy against a broad variety of pests and a unique mode of action by using it spreader and irrigation. The persistence of this pesticide in the soil means that it causes environmental damage that must be cleaned up. In this study collected and identified the best bacteria isolate that breakdown imidacloprid from the Plant Protection Director in Baghdad, which has been using neonicotinoid pesticides for years in their own greenhouse for pest control. Using high-performance liquid chromatography HPLC to measuring the residual concentrations of imidacloprid in MSM media at a concentration o
... Show MorePesticide biodegradation can be accomplished by the technique of bioremediation, which makes use of microorganisms’ ability to degrade pesticide residues. This study aimed to separate and identify imidacloprid-biodegradable from botanical fields soil of greenhouses in the Plant Protection Directorate /Ministry of Agriculture in Baghdad, which has been using imidacloprid pesticides for many years. Using high-performance liquid chromatography, residual imidacloprid concentrations in MSM medium at a concentration of 25 mg/L after 21 days were measured to identify the best degrading bacterial isolates. Isolate No.37 the best bacterial isolate was able to degrade 63% of imidacloprid. was
Beta-lactamase was purified from local isolate Klebsiella pneumonia by several steps included precipitation with ammonium sulphate at 20-40% saturation, DEAE- ion exchange chromatography and gel filtration on Sephacryl S-200 column. The obtained purification fold and recovery were 32.66; 47.04% respectively. The characterization of the purified beta-lactamase showed that the molecular weight was about 4000 daltons as determined by gel filtration.Purified enzyme had an optimal pH of 7 for activity and an optimal stability between pH 6.5-7.5, results shows that the optimal temperature appear to be 35 ? C .During storage the enzyme retained 72% at -20 ? C and retained 25% of the activity at the same period at 4 ? C.
Bacteriocin is an important antimicrobial peptide that can be used in industrial and medical fields due to its characteristics of antibacterial, food preservation and anticancer activities. Fifty isolates of Bacillus sp were collected from different soil samples which were already recognized via morphological and biochemical identification process. The isolates were screened for bacteriocin production effective against Staphylococcus spp in order to select the highest producing isolate. The isolate NK16 showed the maximum bacteriocin production (80 AU/ml) which was further characterized as Bacillus subtilis NK 16 through using API identification system (API 20E and API 50CHB). Then, next step was to detect the optimal conditions for maximum
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