Microbiology
ezat asgarani; elham godini; Jamshid Fooladi
Abstract
Catalase is an enzyme capable of catalyzing the alteration of H2O2 to O2 and H2O. It has recently acquired importance due to its application in the textile industries. Kocuria ASB107shows relative high resistance against ionizing and UV radiation. the antioxidant barrier in this bacterium consists enzymes ...
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Catalase is an enzyme capable of catalyzing the alteration of H2O2 to O2 and H2O. It has recently acquired importance due to its application in the textile industries. Kocuria ASB107shows relative high resistance against ionizing and UV radiation. the antioxidant barrier in this bacterium consists enzymes such as catalase. In order to achieve the highest rate of bacterial growth and catalase production, sugar cane molasses, sugar beet molasses and whey were used as cheap carbon sources. Growth curves were plotted and at the late logarithmic phase, fermentation product was harvested. Catalase activity was measured spectrophotometrically by monitoring the decrease in absorbance at 240 nm affected by the decomposition of hydrogen peroxide. bacterial growth was also stimated from the weight of dry biomass. The highest biomass (5.19 g/L) and catalase activity (2136.25 U/mL) were found in medium consisted 1% molasses and 2.5 % yeast extract. In addition with the 4% whey as a carbon source, catalase activity and growth were 3032.5 U/mL and 6.16 g/L respectively. The results showed molasses and whey are suitable and inexpensive substrate. on the other hand inorganic nitrogen sources such as urea are not suitable for the production of catalase and cell growth.
Abstract
Catalase is an enzyme capable of catalyzing the alteration of H2O2 to O2 and H2O. It has recently acquired importance due to its application in the textile industries. Kocuria ASB107 shows relative high resistance against ionizing and UV radiation. the antioxidant barrier in this bacterium ...
Read More
Catalase is an enzyme capable of catalyzing the alteration of H2O2 to O2 and H2O. It has recently acquired importance due to its application in the textile industries. Kocuria ASB107 shows relative high resistance against ionizing and UV radiation. the antioxidant barrier in this bacterium consists enzymes such as catalase. In order to achieve the highest rate of bacterial growth and catalase production, sugar cane molasses, sugar beet molasses and whey were used as cheap carbon sources . Growth curves were plotted and at the late logarithmic phase, fermentation product was harvested . Catalase activity was measured spectrophotometrically by monitoring the decrease in absorbance at 240 nm affected by the decomposition of hydrogen peroxide. bacterial growth was also stimated from the weight of dry biomass. The highest biomass (5.19g/L) and catalase activity (2136.25 U/mL) were found in medium consisted 1% molasses and 2.5% yeast extract. In addition with the 4 % whey as a carbon source, catalase activity and growth were 3032.5 U/mL and 6.16 g/L respectively. The results showed molasses and whey are suitable and inexpensive substrate. on the other hand inorganic nitrogen sources such as urea are not suitable for the production of catalase and cell growth .
shahla siamaki; Siavosh Salmanzadeh-Ahrabi; Trouska Soufizadeh; Tahereh Falsafi; Mahvash Saifali; Jamshid Fooladi
Abstract
In this study colorimetric medium, which has been developed at Alzahra University, was compared with Quicolor (Salubris Co, USA) and Muller Hinton agar media. Antibacterial susceptibility patterns of 100 isolates of Enterobacteriaceae against 6 different antibiotics were determined by using disk diffusion ...
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In this study colorimetric medium, which has been developed at Alzahra University, was compared with Quicolor (Salubris Co, USA) and Muller Hinton agar media. Antibacterial susceptibility patterns of 100 isolates of Enterobacteriaceae against 6 different antibiotics were determined by using disk diffusion method. The agreement of these methods was defined by kappa analysis. Coefficient of variation (CV) was calculated by repeating antibacterial susceptibility test for 10 times using 2 standard strains and 2 clinical isolates of Enterobacteriaceae on three medium noted above. Kappa value was higher than 0.5 for all cases indicating a good or an excellent agreement of 3 media. ( CV) values were less than 0.05 in majority of cases showing a good reproducibility of testing media. According to the results of this study colorimetric medium can be used for rapid antibacterial susceptibility testing of Enterobacteriaceae.In terms of ease of functional and performance of this medium is similsr to foriegn and standard media.
jamshid fooladi; nashmin fayazi hossini; khadijeh kiarostami
Abstract
Phytases are enzymes capable of hydrolyzing phytic acid to less-phosphorylated myo-inositol derivates. Phytic acid The major storage form of phosphorous in plants. Monogastric animals, such as pig, poultry and fish are not able to metabolize phytic acid. Adding phytase to diet monogastric animals lead ...
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Phytases are enzymes capable of hydrolyzing phytic acid to less-phosphorylated myo-inositol derivates. Phytic acid The major storage form of phosphorous in plants. Monogastric animals, such as pig, poultry and fish are not able to metabolize phytic acid. Adding phytase to diet monogastric animals lead to increased avalibility of phosphorus. The objective of the present study is to isolate and characterize phytase producing bacterial strains from rhizosphere of wheat. Phytase production was determined by production of clear zones around the colonies on the sodium phytate containing medium and the best phytase producing strain was identified using molecular analysis. Also, the isolate was tested for P-solubilizing potential using National Botanical Research Institute Phosphate (NBRIP) containing tricalcium phosphate as the sole P source. Among the 11 bacterial isolates, forming clear peripheral zones on a turbid agar plate, Staphylococcus pasteuri isolated able high potential for phytase production.This study showed that , Staphylococcus pasteuri capable production phytase and phosphatase enzyme.
