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Optimization of β-galactosidase Production by local sporeforming bacteria isolated from Milk

أمثلة إنتاج أنزيم β-galactosidase من بكتيريا محلية متبوغة معزولة من الحليب

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 Publication date 2017
  fields Food Sciences
and research's language is العربية
 Created by Shamra Editor




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40 samples were collected from milk from Homs to isolate the bacteria and study their ability to produce the enzyme β- galactosidase and diagnose isolates the most efficient in the production of the enzyme, the results showed the presence of 25 sporeforming isolates producing the enzyme β-galactosidase , the effectiveness of β-galactosidase was estimated using spectrophotometer at a wavelength of 420 nm.



References used
ACAN, N, 2011- High level production of extracellular β- galactosidase from Bacillus licheniformis ATCC 12759 in submerged fermentation. African Journal of Microbiology Research, 5, 4615-4621
AMMINI, P, KIRAN, K, JIYA, J, NEETHA, J, SANTHA, N, 2009- Biochemical and molecular characterization of Bacillus pumilus isolated from coastal environment in Cochin. Braz. J. Microbiol, India, 40, 269-275
ARTOLOZAGA, M, JONES, R, SCHNRIDER, A, FURLAN, S, CARVALLO,F, 1998- Bioseparation. 7, 137-143
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Some characteristics of β-galactosidase enzyme that was isolated from a new born goat brain were studied. This study concluded that the enzyme is glucoenzyme in which the carbohydrate part constitutes 22.1% in accordance with phenol –sulfate acid method. The optimum pH for the enzyme activity is 5.5. The enzyme lost its activity completely at pH8.5, and showed great stability at the range of pH 4-6. The results indicated that the optimum temperature for the enzyme activity is 55Co at the optimum pH. The stability temperature for the enzyme is 35-60Co. The analytical results of 5%lactose solution hydrolyzed by the enzyme have indicated that the hydrolysis rate is between 40% after 60 minutes, to 95% after 270 minutes.
β-galactosidase enzyme was isolated from the new born goat brain by nine methods, It was found that the sodium acetate 0.2 Mole/Liter +0.2Mole/Liter NaCl PH5 method have given the highest specific activity of crude enzyme in comparison with the ot her methods. Also, this enzyme was purified by using four methods, the second one (cold acetone) was the butter. As a result the purification fold was about 135.46 times and the yield about 77.14% by using Sephacryl S200 (second step). This enzyme is 187.437 KDa as a molecular weight.
B-D-Galactosidase (B-D- galactoside galactohydrolase , E. C. 3.2.1.23) , is one of the most important enzymes used in food processing . It a specific example of a glycosidase enzyme. Many organisms naturally synthesize B- galactosidase , including mi croorganisms , plants and animal cells . Among these possibilities , microbial sources are the best.
45 samples were collected from various sources (soil, degraded wood and mushroom compost) from three cities (Damascus, Homs and Lattakia). 18 Trichoderma isolates were isolated and identified by microscope. These isolates were screened using CMC m edium with Congo red dy to identify their ability to produce cellulase complex. The amount of enzyme production was determined depending on the radius of clear zone around the colony. Results showed that the most productive isolate was Tr with radius 7 ± 0.2 cm followed by Tg and Ti. Optimization of cellulase production was performed using response surface methodology (RSM). The optimal parameters were: temperature 29.5 ˚C, pH = 6، incubation time 4 days, aeration speed 175 rpm and wheat straw concentration 3%. All studied parameters had significant effect on cellulase enzyme activity.
The conditions for producing cellulase enzyme were optimized using corn husks as substrate in submerged fermentation. The effects of five parameters (incubation temperature, pH, substrate concentration, inoculum volume, fermentation time) on the s train growth and enzyme production were studied. For this purpose the statistical program Minitab and the statistical design Response Surface Methodology (RSM) were applied.
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